Cited by 872

The DOI matches its Crossref record; 212 of the 212 references it cites were found in a registry or an index.

Structural Basis of Protein Kinase C Isoform Function

Open access

Steinberg, Susan F.·2008·Physiological Reviews

DOI 10.1152/physrev.00034.2007

Open this paper in CoChat — free account

Abstract

Protein kinase C (PKC) isoforms comprise a family of lipid-activated enzymes that have been implicated in a wide range of cellular functions. PKCs are modular enzymes comprised of a regulatory domain (that contains the membrane-targeting motifs that respond to lipid cofactors, and in the case of some PKCs calcium) and a relatively conserved catalytic domain that binds ATP and substrates. These enzymes are coexpressed and respond to similar stimulatory agonists in many cell types. However, there is growing evidence that individual PKC isoforms subserve unique (and in some cases opposing) functions in cells, at least in part as a result of isoform-specific subcellular compartmentalization patterns, protein-protein interactions, and posttranslational modifications that influence catalytic function. This review focuses on the structural basis for differences in lipid cofactor responsiveness for individual PKC isoforms, the regulatory phosphorylations that control the normal maturation, activation, signaling function, and downregulation of these enzymes, and the intra-/intermolecular interactions that control PKC isoform activation and subcellular targeting in cells. A detailed understanding of the unique molecular features that underlie isoform-specific posttranslational modification patterns, protein-protein interactions, and subcellular targeting (i.e., that impart functional specificity) should provide the basis for the design of novel PKC isoform-specific activator or inhibitor compounds that can achieve therapeutically useful changes in PKC signaling in cells.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1152/physrev.00034.2007

Cites

212 of 212 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Specificity and mechanism of action of some commonly used protein kinase inhibitors
DAVIES, S. P., REDDY, H., CAIVANO, M., & COHEN, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,132
Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,759
The multiple faces of caveolae
Parton, R. G., & Simons, K. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2122 · Cited by 1,454
Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1
Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P., & Parker, P. J. (1998) · Science · doi:10.1126/science.281.5385.2042 · Cited by 1,110
Protein kinase C and other diacylglycerol effectors in cancer
Griner, E. M., & Kazanietz, M. G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2110 · Cited by 978
Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862343 · Cited by 960
Protein kinase C isozymes and the regulation of diverse cell responses
Dempsey, E. C., Newton, A. C., Mochly-Rosen, D., Fields, A. P., Reyland, M. E., Insel, P. A., & Messing, R. O. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l429 · Cited by 737
Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change
Taparowsky, E., Suard, Y., Fasano, O., Shimizu, K., Goldfarb, M., & Wigler, M. (1982) · Nature · doi:10.1038/300762a0 · Cited by 703
Protein kinase C signaling and oxidative stress
Gopalakrishna, R., & Jaken, S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00221-5 · Cited by 701 · cited 1×
“While the focus of most studies in the literature has been on the effects of oxidative stress to activate Src family kinases and alter PKC signaling mechanisms through PKC tyrosine phosphorylation, PKCs are also direct targets for redox modifications (69).”
Background
Proteolytic activation of protein kinase C delta by an ICE-like protease in apoptotic cells.
Emoto, Y., Manome, Y., Meinhardt, G., Kisaki, H., Kharbanda, S., Robertson, M., Ghayur, T., Wong, W. W., Kamen, R., & Weichselbaum, R. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00305.x · Cited by 670
Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester
Zhang, G., Kazanietz, M. G., Blumberg, P. M., & Hurley, J. H. (1995) · Cell · doi:10.1016/0092-8674(95)90011-x · Cited by 652
Activation of protein kinase C by tyrosine phosphorylation in response to H 2 O 2
Konishi, H., Tanaka, M., Takemura, Y., Matsuzaki, H., Ono, Y., Kikkawa, U., & Nishizuka, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11233 · Cited by 605
Multiple pathways control protein kinase C phosphorylation
Parekh, D. B., Ziegler, W., & Parker, P. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.496 · Cited by 601
A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
Violin, J. D., Zhang, J., Tsien, R. Y., & Newton, A. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302125 · Cited by 552
PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid.
Müller, G., Ayoub, M., Storz, P., Rennecke, J., Fabbro, D., & Pfizenmaier, K. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07188.x · Cited by 494
The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
Williams, M. R., Arthur, J. S. C., Balendran, A., van der Kaay, J., Poli, V., Cohen, P., & Alessi, D. R. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00441-3 · Cited by 480
Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
Keranen, L. M., Dutil, E. M., & Newton, A. C. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00277-6 · Cited by 470
Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation
Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., & Barford, D. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00550-6 · Cited by 418
Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation
O'Connell, M. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.545 · Cited by 398
The RACK1 Scaffold Protein: A Dynamic Cog in Cell Response Mechanisms
McCahill, A., Warwicker, J., Bolger, G. B., Houslay, M. D., & Yarwood, S. J. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.6.1261 · Cited by 386
Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
Dutil, E. M., Toker, A., & Newton, A. C. (1998) · Current Biology · doi:10.1016/s0960-9822(98)00017-7 · Cited by 381
A Protein Kinase C Translocation Inhibitor as an Isozyme-selective Antagonist of Cardiac Function
Johnson, J. A., Gray, M. O., Chen, C.-H., & Mochly-Rosen, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24962 · Cited by 377
Distinctive activation mechanisms and functions for protein kinase Cδ
STEINBERG, S. F. (2004) · Biochemical Journal · doi:10.1042/bj20040704 · Cited by 376
Self-citation
Adaptor proteins in protein kinase C-mediated signal transduction
Schechtman, D., & Mochly-Rosen, D. (2001) · Oncogene · doi:10.1038/sj.onc.1204778 · Cited by 352
Localization of Protein Kinase C Isozymes in Cardiac Myocytes
Disatnik, M.-H., Buraggi, G., & Mochly-Rosen, D. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1041 · Cited by 333
Ca2+ bridges the C2 membrane-binding domain of protein kinase Cα directly to phosphatidylserine
Verdaguer, N., Corbalan-Garcia, S., Ochoa, W. F., Fita, I., & Gómez-Fernández, J. C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6329 · Cited by 328
Green Fluorescent Protein (GFP)-tagged Cysteine-rich Domains from Protein Kinase C as Fluorescent Indicators for Diacylglycerol Signaling in Living Cells
Oancea, E., Teruel, M. N., Quest, A. F. G., & Meyer, T. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.485 · Cited by 322
C2 Region-derived Peptides Inhibit Translocation and Function of β Protein Kinase C in Vivo
Ron, D., Luo, J., & Mochly-Rosen, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24180 · Cited by 319
Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts
Wolfman, A., & Macara, I. G. (1987) · Nature · doi:10.1038/325359a0 · Cited by 315
Protein kinase C and the development of diabetic vascular complications
Way, K. J., Katai, N., & King, G. L. (2001) · Diabetic Medicine · doi:10.1046/j.0742-3071.2001.00638.x · Cited by 313
Caspase-3-mediated Cleavage of Protein Kinase C θ in Induction of Apoptosis
Datta, R., Kojima, H., Yoshida, K., & Kufe, D. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20317 · Cited by 313
Rottlerin: an inappropriate and ineffective inhibitor of PKCδ
Soltoff, S. P. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.07.003 · Cited by 311
Immunocytochemical Localization of Eight Protein Kinase C Isozymes Overexpressed in NIH 3T3 Fibroblasts
Goodnight, J., Mischak, H., Kolch, W., & Mushinski, J. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.9991 · Cited by 300
PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system.
Staudinger, J., Zhou, J., Burgess, R., Elledge, S. J., & Olson, E. N. (1995) · The Journal of cell biology · doi:10.1083/jcb.128.3.263 · Cited by 298
Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase C-delta subspecies.
Watanabe, T., Ono, Y., Taniyama, Y., Hazama, K., Igarashi, K., Ogita, K., Kikkawa, U., & Nishizuka, Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10159 · Cited by 296
Imaging Protein Kinase Cα Activation in Cells
Ng, T., Squire, A., Hansra, G., Bornancin, F., Prevostel, C., Hanby, A., Harris, W., Barnes, D., Schmidt, S., Mellor, H., et al. (1999) · Science · doi:10.1126/science.283.5410.2085 · Cited by 287
Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules
Newton, A. C., & Johnson, J. E. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00003-3 · Cited by 274
PKCε‐mediated phosphorylation of vimentin controls integrin recycling and motility
Ivaska, J., Vuoriluoto, K., Huovinen, T., Izawa, I., Inagaki, M., & Parker, P. J. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600847 · Cited by 266
Signaling and Subcellular Targeting by Membrane-Binding Domains
Hurley, J. H., & Misra, S. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.49 · Cited by 261
Regulation of Phospholipase D by Protein Kinase C Is Synergistic with ADP-ribosylation Factor and Independent of Protein Kinase Activity
Singer, W. D., Brown, H. A., Jiang, X., & Sternweis, P. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4504 · Cited by 254
Clinical resistance to the kinase inhibitor STI-571 in chronic myeloid leukemia by mutation of Tyr-253 in the Abl kinase domain P-loop
Roumiantsev, S., Shah, N. P., Gorre, M. E., Nicoll, J., Brasher, B. B., Sawyers, C. L., & Van Etten, R. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162140299 · Cited by 253
The Coatomer Protein β′-COP, a Selective Binding Protein (RACK) for Protein Kinase Cε
Csukai, M., Chen, C.-H., De Matteis, M. A., & Mochly-Rosen, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29200 · Cited by 251
Caveolin Interaction with Protein Kinase C
Oka, N., Yamamoto, M., Schwencke, C., Kawabe, J.-I., Ebina, T., Ohno, S., Couet, J., Lisanti, M. P., & Ishikawa, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33416 · Cited by 250
Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function.
Prekeris, R., Mayhew, M. W., Cooper, J. B., & Terrian, D. M. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.1.77 · Cited by 247
The C2 Domain of PKCδ Is a Phosphotyrosine Binding Domain
Benes, C. H., Wu, N., Elia, A. E. H., Dharia, T., Cantley, L. C., & Soltoff, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.019 · Cited by 246
Phosphorylation sites of protein kinase C δ in H 2 O 2 -treated cells and its activation by tyrosine kinase in vitro
Konishi, H., Yamauchi, E., Taniguchi, H., Yamamoto, T., Matsuzaki, H., Takemura, Y., Ohmae, K., Kikkawa, U., & Nishizuka, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111158798 · Cited by 242
Missense Mutations in the Regulatory Domain of PKCγ: A New Mechanism for Dominant Nonepisodic Cerebellar Ataxia
Chen, D.-H., Brkanac, Z., Christophe Verlinde, L. M. J., Tan, X.-J., Bylenok, L., Nochlin, D., Matsushita, M., Lipe, H., Wolff, J., Fernandez, M., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/373883 · Cited by 237
Ceramide Directly Activates Protein Kinase C ζ to Regulate a Stress-activated Protein Kinase Signaling Complex
Bourbon, N. A., Yun, J., & Kester, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007346200 · Cited by 233
Nuclear import of PKCδ is required for apoptosis: identification of a novel nuclear import sequence
DeVries, T. A., Neville, M. C., & Reyland, M. E. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf606 · Cited by 231
Rottlerin Is a Mitochondrial Uncoupler That Decreases Cellular ATP Levels and Indirectly Blocks Protein Kinase Cδ Tyrosine Phosphorylation
Soltoff, S. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105073200 · Cited by 223
Membrane Targeting by C1 and C2 Domains
Cho, W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100007200 · Cited by 223
Novel “Nonkinase” Phorbol Ester Receptors: The C1 Domain Connection
Kazanietz, M. G. (2002) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12326-7 · Cited by 221
PKC-δ is an apoptotic lamin kinase
Cross, T., Griffiths, G., Deacon, E., Sallis, R., Gough, M., Watters, D., & Lord, J. M. (2000) · Oncogene · doi:10.1038/sj.onc.1203555 · Cited by 216
Interaction between Protein Kinase C δ and the c-Abl Tyrosine Kinase in the Cellular Response to Oxidative Stress
Sun, X., Wu, F., Datta, R., Kharbanda, S., & Kufe, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7470 · Cited by 208
Inactivation of DNA-Dependent Protein Kinase by Protein Kinase Cδ: Implications for Apoptosis
Bharti, A., Kraeft, S.-K., Gounder, M., Pandey, P., Jin, S., Yuan, Z.-M., Lees-Miller, S. P., Weichselbaum, R., Weaver, D., Chen, L. B., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6719 · Cited by 208
The Role of Protein Kinase C in Cerebral Ischemic and Reperfusion Injury
Bright, R., & Mochly-Rosen, D. (2005) · Stroke · doi:10.1161/01.str.0000189996.71237.f7 · Cited by 202
The protein kinase C inhibitors Ro 318220 and GF 109203X are equally potent inhibitors of MAPKAP kinase‐1β (Rsk‐2) and p70 S6 kinase
Alessi, D. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01510-4 · Cited by 200
An autoregulatory region in protein kinase C: the pseudoanchoring site.
Ron, D., & Mochly-Rosen, D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.2.492 · Cited by 199
Tyrosine Phosphorylation of Protein Kinase Cδ Is Essential for Its Apoptotic Effect in Response to Etoposide
Blass, M., Kronfeld, I., Kazimirsky, G., Blumberg, P. M., & Brodie, C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.182-195.2002 · Cited by 197
Cell Signaling and Function Organized by PB1 Domain Interactions
Moscat, J., Diaz-Meco, M. T., Albert, A., & Campuzano, S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.002 · Cited by 197
Human Diabetes Associated with a Mutation in the Tyrosine Kinase Domain of the Insulin Receptor
Odawara, M., Kadowaki, T., Yamamoto, R., Shibasaki, Y., Tobe, K., Accili, D., Bevins, C., Mikami, Y., Matsuura, N., Akanuma, Y., et al. (1989) · Science · doi:10.1126/science.2544998 · Cited by 191
Phosphorylation of Protein Kinase C-α on Serine 657 Controls the Accumulation of Active Enzyme and Contributes to Its Phosphatase-resistant State
Bornancin, F., & Parker, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3544 · Cited by 191
Targeting of Protein Kinase Cα to Caveolae
Mineo, C., Ying, Y.-S., Chapline, C., Jaken, S., & Anderson, R. G. W. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.3.601 · Cited by 186
Ceramide Recruits and Activates Protein Kinase C ζ (PKCζ) within Structured Membrane Microdomains
Fox, T. E., Houck, K. L., O'Neill, S. M., Nagarajan, M., Stover, T. C., Pomianowski, P. T., Unal, O., Yun, J. K., Naides, S. J., & Kester, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700082200 · Cited by 185
Binding Specificity for RACK1 Resides in the V5 Region of βII Protein Kinase C
Stebbins, E. G., & Mochly-Rosen, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101044200 · Cited by 183
Targeting Protein Kinase C Activity Reporter to Discrete Intracellular Regions Reveals Spatiotemporal Differences in Agonist-dependent Signaling
Gallegos, L. L., Kunkel, M. T., & Newton, A. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603741200 · Cited by 183
Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Cα
Bornancin, F., & Parker, P. J. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70678-7 · Cited by 177
Nitric Oxide (NO) Induces Nitration of Protein Kinase Cε (PKCε), Facilitating PKCε Translocation via Enhanced PKCε-RACK2 Interactions
Balafanova, Z., Bolli, R., Zhang, J., Zheng, Y., Pass, J. M., Bhatnagar, A., Tang, X.-L., Wang, O., Cardwell, E., & Ping, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112451200 · Cited by 175
Mammalian TOR Controls One of Two Kinase Pathways Acting upon nPKCδ and nPKCε
Parekh, D., Ziegler, W., Yonezawa, K., Hara, K., & Parker, P. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34758 · Cited by 174
Ceramide-induced Translocation of Protein Kinase C-δ and -ϵ to the Cytosol
Sawai, H., Okazaki, T., Takeda, Y., Tashima, M., Sawada, H., Okuma, M., Kishi, S., Umehara, H., & Domae, N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2452 · Cited by 172
Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
Maeda, Y. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5982 · Cited by 172
Regulation of novel protein kinase C ε by phosphorylation
Cenni, V., Döppler, H. R., Sonnenburg, E. D., Maraldi, N. M., Newton, A. C., & Toker, A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630537 · Cited by 171
Identification of Chelerythrine as an Inhibitor of BclXL Function
Chan, S.-L., Lee, M. C., Tan, K. O., Yang, L.-K., Lee, A. S. Y., Flotow, H., Fu, N. Y., Butler, M. S., Soejarto, D. D., Buss, A. D., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300138200 · Cited by 162
A Single Residue in the C1 Domain Sensitizes Novel Protein Kinase C Isoforms to Cellular Diacylglycerol Production
Dries, D. R., Gallegos, L. L., & Newton, A. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c600268200 · Cited by 159
Structure of the protein kinase Cβ phospholipid-binding C2 domain complexed with Ca2+
Sutton, R. B., & Sprang, S. R. (1998) · Structure · doi:10.1016/s0969-2126(98)00139-7 · Cited by 158
PKCϵ controls the traffic of β1 integrins in motile cells
Ivaska, J., Whelan, R. D. H., Watson, R., & Parker, P. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf371 · Cited by 156
Phosphorylation or Glutamic Acid Substitution at Protein Kinase C Sites on Cardiac Troponin I Differentially Depress Myofilament Tension and Shortening Velocity
Burkart, E. M., Sumandea, M. P., Kobayashi, T., Nili, M., Martin, A. F., Homsher, E. E., & Solaro, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210712200 · Cited by 156
Mechanism of Diacylglycerol-induced Membrane Targeting and Activation of Protein Kinase Cθ
Melowic, H. R., Stahelin, R. V., Blatner, N. R., Tian, W., Hayashi, K., Altman, A., & Cho, W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700119200 · Cited by 155
Protein kinase Cδ is responsible for constitutive and DNA damage‐induced phosphorylation of Rad9
Yoshida, K., Wang, H., Miki, Y., & Kufe, D. W. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg134 · Cited by 153
Phosphorylation at Conserved Carboxyl-terminal Hydrophobic Motif Regulates the Catalytic and Regulatory Domains of Protein Kinase C
Edwards, A., & Newton, A. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.18382 · Cited by 150
Activated Protein Kinase C Isoforms Target to Cardiomyocyte Caveolae
Rybin, V. O., Xu, X., & Steinberg, S. F. (1999) · Circulation Research · doi:10.1161/01.res.84.9.980 · Cited by 147
Self-citation
Catalytic Domain Crystal Structure of Protein Kinase C-θ (PKCθ)
Xu, Z., Chaudhary, D., Olland, S., Wolfrom, S., Czerwiński, R., Malakian, K., Lin, L., Stahl, M., Joseph‐McCarthy, D., Benander, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409216200 · Cited by 147
The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
Gonfloni, S., Williams, J. C., Hattula, K., Weijland, A., Wierenga, R. K., & Superti‐Furga, G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.24.7261 · Cited by 146
Activation of Acid Sphingomyelinase by Protein Kinase Cδ-mediated Phosphorylation
Zeidan, Y. H., & Hannun, Y. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609424200 · Cited by 146
Phosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutants
Skaggs, B. J., Gorre, M. E., Ryvkin, A., Burgess, M. R., Xie, Y., Han, Y., Komisopoulou, E., Brown, L. M., Loo, J. A., Landaw, E. M., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609239103 · Cited by 142
Localization, Anchoring, and Functions of Protein Kinase C Isozymes in the Heart
Mackay, K., & Mochly‐Rosen, D. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1400 · Cited by 141
Interaction of fascin and protein kinase Cα: a novel intersection in cell adhesion and motility
Anilkumar, N., Parsons, M., Monk, R. J., Ng, T., & Adams, J. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg521 · Cited by 139
Activation Mechanisms of Conventional Protein Kinase C Isoforms Are Determined by the Ligand Affinity and Conformational Flexibility of Their C1 Domains
Ananthanarayanan, B., Stahelin, R. V., Digman, M. A., & Cho, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307853200 · Cited by 134
The Turn Motif Is a Phosphorylation Switch That Regulates the Binding of Hsp70 to Protein Kinase C
Gao, T., & Newton, A. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204335200 · Cited by 134
Protein kinase C epsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi function.
Lehel, C., Oláh, Z., Jakab, G., & Anderson, W. B. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1406 · Cited by 133
Solution structure of a cysteine rich domain of rat protein kinase C
Hommel, U., Zurini, M. G. M., & Luyten, M. A. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0694-383 · Cited by 133
Protein Kinase C-δ Is a Negative Regulator of Antigen-Induced Mast Cell Degranulation
Leitges, M., Gimborn, K., Elis, W., Kalesnikoff, J., Hughes, M. R., Krystal, G., & Huber, M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.3970-3980.2002 · Cited by 131
Regulation of Protein Kinase Cθ Function during T Cell Activation by Lck-mediated Tyrosine Phosphorylation
Liu, Y., Witte, S., Liu, Y., Doyle, M., Elly, C., & Altman, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3603 · Cited by 129
Protein Kinase C βII Specifically Binds to and Is Activated by F-actin
Blobe, G. C., Stribling, D. S., Fabbro, D., Stabel, S., & Hannun, Y. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15823 · Cited by 128
Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction
Liu, Y., Graham, C., Li, A., et al. (2002) · Biochemical Journal · doi:10.1042/bj3610255 · Cited by 128
Mechanism of Diacylglycerol-induced Membrane Targeting and Activation of Protein Kinase Cδ
Stahelin, R. V., Digman, M. A., Medkova, M., Ananthanarayanan, B., Rafter, J. D., Melowic, H. R., & Cho, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403191200 · Cited by 128
PKCζ at the crossroad of NF-κB and Jak1/Stat6 signaling pathways
Moscat, J., Rennert, P. D., & Díaz-Meco, M. T. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401823 · Cited by 127
Carboxyl-terminal Phosphorylation Regulates the Function and Subcellular Localization of Protein Kinase C βII
Edwards, A., Faux, M. C., Scott, J. D., & Newton, A. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6461 · Cited by 127
The Molecular Basis of Differential Subcellular Localization of C2 Domains of Protein Kinase C-α and Group IVa Cytosolic Phospholipase A2
Stahelin, R. V., Rafter, J. D., Das, S., & Cho, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212864200 · Cited by 126
NMR Structure of a Protein Kinase C-γ Phorbol-Binding Domain and Study of Protein−Lipid Micelle Interactions
Xu, R. X., Pawełczyk, T., Xia, T.-H., & Brown, S. C. (1997) · Biochemistry · doi:10.1021/bi970833a · Cited by 125
Structure of the Catalytic Domain of Human Protein Kinase C β II Complexed with a Bisindolylmaleimide Inhibitor
Grodsky, N. B., Li, Y., Bouzida, D., Love, R. A., Jensen, J. R., Nodes, B. R., Nonomiya, J., & Grant, S. K. (2006) · Biochemistry · doi:10.1021/bi061128h · Cited by 122
PKCε, Via its Regulatory Domain and Independently of its Catalytic Domain, Induces Neurite-like Processes in Neuroblastoma Cells
Zeidman, R., Löfgren, B., Påhlman, S., & Larsson, C. U. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.4.713 · Cited by 122
Increased Membrane Affinity of the C1 Domain of Protein Kinase Cδ Compensates for the Lack of Involvement of Its C2 Domain in Membrane Recruitment
Giorgione, J. R., Lin, J., McCammon, J. A., & Newton, A. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510251200 · Cited by 122
Oxidative Activation of Protein Kinase Cγ through the C1 Domain
Lin, D., & Takemoto, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407762200 · Cited by 120
Chelerythrine Rapidly Induces Apoptosis through Generation of Reactive Oxygen Species in Cardiac Myocytes
Yamamoto, S., Seta, K., Morisco, C., Vatner, S. F., & Sadoshima, J. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1446 · Cited by 119
Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes
Doble, B. W., Dang, X., Ping, P., Fandrich, R. R., Nickel, B. E., Jin, Y., Cattini, P. A., & Kardami, E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00889 · Cited by 119
The Phosphoinositide-dependent Kinase, PDK-1, Phosphorylates Conventional Protein Kinase C Isozymes by a Mechanism That Is Independent of Phosphoinositide 3-Kinase
Sonnenburg, E. D., Gao, T., & Newton, A. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107416200 · Cited by 117
Selective Ceramide Binding to Protein Kinase C-α and -δ Isoenzymes in Renal Mesangial Cells
Huwiler, A., Fabbro, D., & Pfeilschifter, J. M. (1998) · Biochemistry · doi:10.1021/bi981401i · Cited by 117
Phosphorylation of the Catalytic Subunit of Protein Kinase A
Moore, M. J., Kanter, J. R., Jones, K., & Taylor, S. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204970200 · Cited by 116
Mutagenesis of the C2 Domain of Protein Kinase C-α
Medkova, M., & Cho, W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17544 · Cited by 115
Molecular Analysis of the Interactions between Protein Kinase C-ε and Filamentous Actin
Prekeris, R., Hernandez, R. M., Mayhew, M. W., White, M. K., & Terrian, D. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26790 · Cited by 115
p73β Is Regulated by Protein Kinase Cδ Catalytic Fragment Generated in the Apoptotic Response to DNA Damage
Ren, J., Datta, R., Shioya, H., Li, Y., Oki, E., Biedermann, V., Bharti, A. K., & Kufe, D. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110667200 · Cited by 114
Crystal structure of the C2 domain from protein kinase C-δ
Pappa, H. S., Murray‐Rust, J., Dekker, L. V., Parker, P. J., & McDonald, N. Q. (1998) · Structure · doi:10.1016/s0969-2126(98)00090-2 · Cited by 114
Diacylglycerol-induced Membrane Targeting and Activation of Protein Kinase Cϵ
Stahelin, R. V., Digman, M. A., Medkova, M., Ananthanarayanan, B., Melowic, H. R., Rafter, J. D., & Cho, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411285200 · Cited by 113
Phosphorylation of Protein Kinase Cδ on Distinct Tyrosine Residues Regulates Specific Cellular Functions
Kronfeld, I., Kazimirsky, G., Lorenzo, P. S., Garfield, S. H., Blumberg, P. M., & Brodie, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005991200 · Cited by 113
Rapamycin-sensitive phosphorylation of PKC on a carboxy-terminal site by an atypical PKC complex.
Ziegler, W., Parekh, D., Good, J. A. L., Whelan, R. D. H., Kelly, J., Frech, M., Hemmings, B., & Parker, P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80236-x · Cited by 113
Cross-regulation of Novel Protein Kinase C (PKC) Isoform Function in Cardiomyocytes
Rybin, V. O., Sabri, A., Short, J., Braz, J. C., Molkentin, J. D., & Steinberg, S. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212644200 · Cited by 112
Self-citation
Specific Translocation of Protein Kinase Cα to the Plasma Membrane Requires Both Ca 2+ and PIP 2 Recognition by Its C2 Domain
Evans, J. H., Murray, D., Leslie, C. C., & Falke, J. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0499 · Cited by 112
The Carboxyl Terminus of Protein Kinase C Provides a Switch to Regulate Its Interaction with the Phosphoinositide-dependent Kinase, PDK-1
Gao, T., Toker, A., & Newton, A. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101357200 · Cited by 109
Targeting of the c-Abl Tyrosine Kinase to Mitochondria in the Necrotic Cell Death Response to Oxidative Stress
Kumar, S., Bharti, A. K., Mishra, N. C., Raina, D., Kharbanda, S. M., Saxena, S. P., & Kufe, D. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101414200 · Cited by 108
Protein Kinase C-ε Regulates the Apoptosis and Survival of Glioma Cells
Okhrimenko, H., Lü, W., Xiang, C., Hamburger, N., Kazimirsky, G., & Brodie, C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1064 · Cited by 108
The gatekeeper residue controls autoactivation of ERK2 via a pathway of intramolecular connectivity
Emrick, M. A., Lee, T., Starkey, P. J., Mumby, M. C., Resing, K. A., & Ahn, N. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608849103 · Cited by 108
Phosphorylation of Protein Kinase Cδ (PKCδ) at Threonine 505 Is Not a Prerequisite for Enzymatic Activity
Stempka, L., Girod, A., Müller, H., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6805 · Cited by 107
Regulation of exocytosis by protein kinase C
Morgan, A., Burgoyne, R. D., Barclay, J. W., Craig, T. J., Prescott, G. R., Ciufo, L. F., Evans, G. J., & Graham, M. E. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051341 · Cited by 107
Ceramide-induced Apoptosis by Translocation, Phosphorylation, and Activation of Protein Kinase Cδ in the Golgi Complex
Kajimoto, T., Shirai, Y., Sakai, N., Yamamoto, T., Matsuzaki, H., Kikkawa, U., & Saito, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312350200 · Cited by 107
Preservation of Base-line Hemodynamic Function and Loss of Inducible Cardioprotection in Adult Mice Lacking Protein Kinase Cϵ
Gray, M. O., Zhou, H.-Z., Schafhalter-Zoppoth, I., Zhu, P., Mochly‐Rosen, D., & Messing, R. O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311459200 · Cited by 105
Structure of the C2 domain from novel protein kinase Cϵ. A membrane binding model for Ca2+-independent C2 domains
Ochoa, W. F., García-García, J., Fita, I., Corbalán‐García, S., Verdaguer, N., & Gómez-Fernández, J. C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4910 · Cited by 104
Diacylglycerol kinase δ regulates protein kinase C and epidermal growth factor receptor signaling
Crotty, T. M., Cai, J., Sakane, F., Taketomi, A., Prescott, S. M., & Topham, M. K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604104103 · Cited by 102
Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-Δ with Src family kinases in the RBL-2H3 mast cell line: regulation of Src family kinase activity by protein kinase C-δ
Song, J. S., Swann, P. G., Szállási, Z., Blank, U., Blumberg, P. M., & Rivera, J. (1998) · Oncogene · doi:10.1038/sj.onc.1201886 · Cited by 101
Association of diacylglycerol kinase ζ with protein kinase C α
Luo, B., Prescott, S. M., & Topham, M. K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208120 · Cited by 101
A New Phosphatidylinositol 4,5-Bisphosphate-binding Site Located in the C2 Domain of Protein Kinase Cα
Corbalán‐García, S., García-García, J., Rodríguez-Alfaro, J. A., & Gómez-Fernández, J. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209385200 · Cited by 99
Centrosomal Anchoring of Protein Kinase C βII by Pericentrin Controls Microtubule Organization, Spindle Function, and Cytokinesis
Chen, D., Purohit, A., Halilovic, E., Doxsey, S., & Newton, A. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311196200 · Cited by 96
Crystal Structure of the Catalytic Domain of Human Atypical Protein Kinase C-iota Reveals Interaction Mode of Phosphorylation Site in Turn Motif
Messerschmidt, A., Macieira, S., Velarde, M., et al. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.060 · Cited by 96
Nerve Growth Factor Stimulates Multisite Tyrosine Phosphorylation and Activation of the Atypical Protein Kinase C's via a src Kinase Pathway
Wooten, M. W., Vandenplas, M., Seibenhener, M., Geetha, T., & Diaz-Meco, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8414-8427.2001 · Cited by 95
Protein kinase Cα actively downregulates through caveolae-dependent traffic to an endosomal compartment
Prévostel, C., Vallentin, A., BRESSION, D., & Parker, P. J. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.14.2575 · Cited by 95
Regulation of Alternative Splicing of Protein Kinase Cβ by Insulin
Chalfant, C. E., Mischak, H., Watson, J. E., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13326 · Cited by 92
Cardiac-Specific Overexpression of Diacylglycerol Kinase ζ Prevents Gq Protein-Coupled Receptor Agonist-Induced Cardiac Hypertrophy in Transgenic Mice
Arimoto, T., Takeishi, Y., Takahashi, H., Shishido, T., Niizeki, T., Koyama, Y., Shiga, R., Nozaki, N., Nakajima, O., Nishimaru, K., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.560771 · Cited by 91
The Simultaneous Production of Phosphatidic Acid and Diacylglycerol Is Essential for the Translocation of Protein Kinase Cϵ to the Plasma Membrane in RBL-2H3 Cells
López-Andreo, M. J., Gómez-Fernández, J. C., & Corbalán‐García, S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-05-0295 · Cited by 90
Protein Kinase Cγ Regulation of Gap Junction Activity through Caveolin-1–Containing Lipid Rafts
Lin, D., Zhou, J., Zelenka, P. S., & Takemoto, D. J. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0296 · Cited by 88
Increased Collagen Deposition and Diastolic Dysfunction but Preserved Myocardial Hypertrophy After Pressure Overload in Mice Lacking PKCε
Klein, G. G., Schaefer, A., Hilfiker‐Kleiner, D., Oppermann, D., Shukla, P. C., Guba‐Quint, A., Podewski, E., Hilfiker, A., Schröder, F., Leitges, M., et al. (2005) · Circulation Research · doi:10.1161/01.res.0000161999.86198.1e · Cited by 88
Importance of C1B Domain for Lipid Messenger-induced Targeting of Protein Kinase C
Kashiwagi, K., Shirai, Y., Kuriyama, M., Sakai, N., & Saito, N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111761200 · Cited by 83
Physiological Phosphorylation of Protein Kinase A at Thr-197 Is by a Protein Kinase A Kinase
Cauthron, R. D., Carter, K. B., Liauw, S., & Steinberg, R. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1416 · Cited by 83
Consequences of Lysine 72 Mutation on the Phosphorylation and Activation State of cAMP-dependent Kinase
Iyer, G. H., Moore, M. J., & Taylor, S. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407586200 · Cited by 83
Regulation of Receptor-mediated Protein Kinase C Membrane Trafficking by Autophosphorylation
Feng, X., Becker, K. P., Stribling, S., Peters, K. G., & Hannun, Y. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.22.17024 · Cited by 81
Requirements of Protein Kinase Cδ for Catalytic Function
Stempka, L., Schnölzer, M., Radke, S., Rincke, G., Marks, F., & Gschwendt, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8886 · Cited by 80
Src Family Kinases Phosphorylate Protein Kinase C δ on Tyrosine Residues and Modify the Neoplastic Phenotype of Skin Keratinocytes
Joseloff, E., Cataisson, C., Aamodt, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111618200 · Cited by 80
Protein Kinase Cα Phosphorylates and Negatively Regulates Diacylglycerol Kinase ζ
Luo, B., Prescott, S. M., & Topham, M. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307153200 · Cited by 79
Regulated Binding of the Protein Kinase C Substrate GAP-43 to the V0/C2 Region of Protein Kinase C-δ
Dekker, L. V., & Parker, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12747 · Cited by 77
Regulation of p53 by Activated Protein Kinase C-δ during Nitric Oxide-induced Dopaminergic Cell Death
Lee, S., Kim, D., Choi, B., Ha, H., & Kim, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509509200 · Cited by 77
An Essential Role for Autophosphorylation in the Dissociation of Activated Protein Kinase C from the Plasma Membrane
Feng, X., & Hannun, Y. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26870 · Cited by 77
The Lipophilicity of Phorbol Esters as a Critical Factor in Determining the Pattern of Translocation of Protein Kinase C δ Fused to Green Fluorescent Protein
Wang, Q. J., Fang, T.-W., Fenick, D. J., Garfield, S. H., Bienfait, B., Márquez, V. E., & Blumberg, P. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12136 · Cited by 75
Identification of Serine 643 of Protein Kinase C-δ as an Important Autophosphorylation Site for Its Enzymatic Activity
Li, W., Zhang, J., Bottaro, D. P., Li, W., & Pierce, J. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24550 · Cited by 75
Ca2+ Differentially Regulates Conventional Protein Kinase Cs' Membrane Interaction and Activation
Keranen, L. M., & Newton, A. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25959 · Cited by 73
Mechanisms of Regulation of Phospholipase D1 by Protein Kinase Cα
Hu, T., & Exton, J. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210093200 · Cited by 73
Development of a Rapid Approach to Identification of Tyrosine Phosphorylation Sites: Application to PKCδ Phosphorylated upon Activation of the High Affinity Receptor for IgE in Rat Basophilic Leukemia Cells
Szállási, Z., Denning, M. F., Chang, E., Rivera, J., Yuspa, S. H., Lehel, C., Oláh, Z., Anderson, W. B., & Blumberg, P. M. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2370 · Cited by 72
A Ras activation pathway dependent on Syk phosphorylation of protein kinase C
Kawakami, Y., Kitaura, J., Yao, L., McHenry, R. W., Kawakami, Y., Newton, A. C., Kang, S., Kato, R. M., Leitges, M., Rawlings, D. J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633695100 · Cited by 72
Sphingosine-dependent Protein Kinase-1, Directed to 14-3-3, Is Identified as the Kinase Domain of Protein Kinase Cδ
Hamaguchi, A., Suzuki, É., Murayama, K., Fujimura, T., Hikita, T., Iwabuchi, K., Handa, K., Withers, D. A., Masters, S. C., Fu, H., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305294200 · Cited by 72
Regulation of Protein Kinase C βII by Its C2 Domain
Edwards, A., & Newton, A. C. (1997) · Biochemistry · doi:10.1021/bi9718752 · Cited by 72
Protein Kinase C β/Early Growth Response-1 Pathway
Yan, S., Harja, E., Andrassy, M., Fujita, T., & Schmidt, A. M. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2006.05.063 · Cited by 71
A conserved helix motif complements the protein kinase core.
Véron, M., Radzio-Andzelm, E., Tsigelny, I. F., Eyck, L. F. T., & Taylor, S. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10618 · Cited by 71
The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
GARCIA-PARAMIO, P., Cabrerizo, Y., Bornancin, F., & Parker, P. J. (1998) · Biochemical Journal · doi:10.1042/bj3330631 · Cited by 71
p32 (gC1qBP) Is a General Protein Kinase C (PKC)-binding Protein
Robles‐Flores, M., Rendon‐Huerta, E. P., González-Aguilar, H., Mendoza‐Hernández, G., Islas, S., Mendoza, V., Ponce-Castañeda, M. V., González‐Mariscal, L., & López‐Casillas, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109333200 · Cited by 70
Tyrosine Phosphorylation Modifies Protein Kinase C δ-dependent Phosphorylation of Cardiac Troponin I*
Sumandea, M., Rybin, V., Hinken, A. C., Wang, C.-J., Kobayashi, T., Harleton, E., Sievert, G., Balke, C., Feinmark, S. J., Solaro, R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802396200 · Cited by 69
Self-citation
Peptides Derived from the C2 Domain of Protein Kinase Cϵ (ϵPKC) Modulate ϵPKC Activity and Identify Potential Protein-Protein Interaction Surfaces
Brandman, R., Disatnik, M., Churchill, E. N., & Mochly‐Rosen, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608521200 · Cited by 69
Nuclear Import and Export Signals Enable Rapid Nucleocytoplasmic Shuttling of the Atypical Protein Kinase C λ
Perander, M., Bjørkøy, G., & Johansen, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010356200 · Cited by 64
Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface
Herberg, F. W., Zimmermann, B., McGlone, M. L., & Taylor, S. S. (1997) · Protein Science · doi:10.1002/pro.5560060306 · Cited by 63
cPKC-dependent Sequestration of Membrane-recycling Components in a Subset of Recycling Endosomes
Becker, K. P., & Hannun, Y. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305228200 · Cited by 62
Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C
CHAUHAN, R., & Mande, S. C. (2002) · Biochemical Journal · doi:10.1042/bj20020545 · Cited by 62
Roles of Tyrosine Phosphorylation and Cleavage of Protein Kinase Cδ in Its Protective Effect Against Tumor Necrosis Factor-related Apoptosis Inducing Ligand-induced Apoptosis
Okhrimenko, H., Lü, W., Xiang, C., Ju, D., Blumberg, P. M., Gomel, R., Kazimirsky, G., & Brodie, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501374200 · Cited by 61
Identification of Tyrosine 187 as a Protein Kinase C-δ Phosphorylation Site
Li, W., Li, W., Chen, X.-H., Kelley, C. A., Alimandi, M., Zhang, J., Chen, Q., Bottaro, D. P., & Pierce, J. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.26404 · Cited by 60
Allosteric Network of cAMP-dependent Protein Kinase Revealed by Mutation of Tyr204 in the P+1 Loop
Yang, J., Garrod, S. M., Deal, M. S., Anand, G. S., Woods, V. L., & Taylor, S. S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.030 · Cited by 60
The Origin of C1A-C2 Interdomain Interactions in Protein Kinase Cα
Stahelin, R. V., Wang, J., Blatner, N. R., Rafter, J. D., Murray, D., & Cho, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506224200 · Cited by 59
Peroxynitrite-Induced Tyrosine Nitration and Inhibition of Protein Kinase C
Knapp, L. T., Kanterewicz, B. I., Hayes, E. L., & Klann, E. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5448 · Cited by 57
Critical role of novel Thr‐219 autophosphorylation for the cellular function of PKCθ in T lymphocytes
Thuille, N., Heit, I., Fresser, F., Krumböck, N., Bauer, B., Leuthäusser, S., Dammeier, S., Graham, C., Copeland, T. D., Shaw, S., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600856 · Cited by 57
The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain
Imai, S.-I., Kai, M., Yamada, K., Kanoh, H., & Sakane, F. (2004) · Biochemical Journal · doi:10.1042/bj20040681 · Cited by 56
Regulation of PKCα Activity by C1-C2 Domain Interactions
Slater, S. J., Seiz, J. L., Cook, A. C., Buzas, C. J., Malinowski, S. A., Kershner, J. L., Stagliano, B. A., & Stubbs, C. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112207200 · Cited by 55
A Critical Role of Protein Kinase Cδ Activation Loop Phosphorylation in Formyl-Methionyl-Leucyl-Phenylalanine-Induced Phosphorylation of p47phox and Rapid Activation of Nicotinamide Adenine Dinucleotide Phosphate Oxidase
Cheng, N., He, R. L., Tian, J., Dinauer, M. C., & Ye, R. D. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7720 · Cited by 54
Dynamic Sequestration of the Recycling Compartment by Classical Protein Kinase C
Idkowiak‐Baldys, J., Becker, K. P., Kitatani, K., & Hannun, Y. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512540200 · Cited by 53
Unique Structural and Functional Properties of the ATP-binding Domain of Atypical Protein Kinase C-ι
Spitaler, M., Villunger, A., Grunicke, H. H., & Überall, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002742200 · Cited by 53
Identification of ChChd3 as a Novel Substrate of the cAMP-dependent Protein Kinase (PKA) Using an Analog-sensitive Catalytic Subunit
Schauble, S., King, C. C., Darshi, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609221200 · Cited by 51
Effects on Ligand Interaction and Membrane Translocation of the Positively Charged Arginine Residues Situated along the C1 Domain Binding Cleft in the Atypical Protein Kinase C Isoforms
Pu, Y., Peach, M. L., Garfield, S. H., Wincovitch, S., Márquez, V. E., & Blumberg, P. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606560200 · Cited by 49
Identification of an Amino Acid Residue in the Protein Kinase C C1b Domain Crucial for Its Localization to the Golgi Network
Schultz, A., Ling, M., & Larsson, C. U. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313017200 · Cited by 49
A Chemical Genetic Approach for the Identifi cation of Direct Substrates of Protein Kinases
Shah, K., & Shokat, K. M. (2003) · Humana Press eBooks · doi:10.1385/1-59259-397-6:253 · Cited by 49
Phosphorylation and Up-regulation of Diacylglycerol Kinase γ via Its Interaction with Protein Kinase Cγ
Yamaguchi, Y., Shirai, Y., Matsubara, T., Sanse, K., Kuriyama, M., Oshiro, N., Yoshino, K., Yonezawa, K., Ono, Y., & Saito, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606992200 · Cited by 48
Mapping of a Molecular Determinant for Protein Kinase C βII Isozyme Function
Gökmen‐Polar, Y., & Fields, A. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20261 · Cited by 47
Independence of Protein Kinase C-δ Activity from Activation Loop Phosphorylation
Liu, Y., Belkina, N. V., Graham, C., & Shaw, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600508200 · Cited by 45
Analysis by Fluorescence Resonance Energy Transfer of the Interaction between Ligands and Protein Kinase Cδ in the Intact Cell
Braun, D. C., Garfield, S. H., & Blumberg, P. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413896200 · Cited by 42
Protein Kinase C Isoform-specific Differences in the Spatial-Temporal Regulation and Decoding of Metabotropic Glutamate Receptor1a-stimulated Second Messenger Responses
Babwah, A. V., Dale, L. B., & Ferguson, S. S. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211053200 · Cited by 40
Proteolytic Activation of Protein Kinase Cα by Peroxynitrite in Stimulating Cytosolic Phospholipase A2 in Pulmonary Endothelium: Involvement of a Pertussis Toxin Sensitive Protein
Chakraborti, T., Das, S. K., & Chakraborti, S. (2005) · Biochemistry · doi:10.1021/bi0477889 · Cited by 40
The Roles of Protein Kinase C βI and βII in Vascular Smooth Muscle Cell Proliferation
Yamamoto, M., Acevedo-Duncan, M. E., Chalfant, C. E., Patel, N. A., Watson, J. E., & Cooper, D. R. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.3999 · Cited by 40
The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCδ and the regulation of cell apoptosis
Lu, W., Lee, H.-K., Xiang, C., Finniss, S., & Brodie, C. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.06.015 · Cited by 39
Rottlerin-Independent Attenuation of Pervanadate-Induced Tyrosine Phosphorylation Events by Protein Kinase C-δ in Hemopoietic Cells
Leitges, M., Elis, W., Gimborn, K., & Huber, M. (2001) · Laboratory Investigation · doi:10.1038/labinvest.3780321 · Cited by 38
Mechanism of Inhibition of Sequestration of Protein Kinase C α/βII by Ceramide
Kitatani, K., Idkowiak‐Baldys, J., & Hannun, Y. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609162200 · Cited by 37
Invariant Leu Preceding Turn Motif Phosphorylation Site Controls the Interaction of Protein Kinase C with Hsp70
Gao, T., & Newton, A. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604076200 · Cited by 37
Novel Protein Kinase C .DELTA. Isoform Insensitive to Caspase-3.
Sakurai, Y., Onishi, Y., Tanimoto, Y., & Kizaki, H. (2001) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.24.973 · Cited by 37
Effects of bisindolylmaleimide PKC inhibitors on p90RSK activity in vitro and in adult ventricular myocytes
Roberts, N. A., Haworth, R. S., & Avkiran, M. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706210 · Cited by 36
Effect of a tyrosine 155 to phenylalanine mutation of protein kinase Cdelta on the proliferative and tumorigenic properties of NIH 3T3 fibroblasts
Acs, P. I. (2000) · Carcinogenesis · doi:10.1093/carcin/21.5.887 · Cited by 36
Isoenzyme-specific Translocation of Protein Kinase C (PKC)βII and not PKCβI to a Juxtanuclear Subset of Recycling Endosomes
Becker, K. P., & Hannun, Y. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400770200 · Cited by 35
Protein Kinase Cα Translocates to the Perinuclear Region to Activate Phospholipase D1
Hu, T., & Exton, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402372200 · Cited by 35
Inhibition of Gap Junction Activity through the Release of the C1B Domain of Protein Kinase Cγ (PKCγ) from 14-3-3
Nguyen, T., Takemoto, L., & Takemoto, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403040200 · Cited by 33

Reactive Oxygen Species in Inflammation and Tissue Injury
Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028
Signaling in Muscle Contraction
Kuo, I. Y., & Ehrlich, B. E. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006023 · Cited by 424
DAG tales: the multiple faces of diacylglycerol—stereochemistry, metabolism, and signaling
Eichmann, T. O., & Lass, A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1982-3 · Cited by 314
Apolipoprotein E Regulates the Integrity of Tight Junctions in an Isoform-dependent Manner in an in Vitro Blood-Brain Barrier Model
Nishitsuji, K., Hosono, T., Nakamura, T., Bu, G., & Michikawa, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225532 · Cited by 275

See all 872

Authors: Steinberg, S. F.
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 2008-10
Volume: 88
Issue: 4
Pages: 1341-1378
ISSN: 0031-9333 (ISSN-L)
1522-1210
DOI: 10.1152/physrev.00034.2007
OpenAlex: W1998349282
Cited by: 872
References: 212
FWCI: 2.36
Type: journal article
Language: en
Open access: green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Structural Basis of Protein Kinase C Isoform Function

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources