Cited by 375Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsSphingolipid Metabolism and Signaling

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Taxonomy and function of C1 protein kinase C homology domains

Open access

Hurley, James H., Newton, Alexandra C., Parker, Peter J., Blumberg, Peter M., Nishizuka, Yasutomi·1997·Protein Science

DOI 10.1002/pro.5560060228PMC PMC2143645

Open this paper in CoChat — free account Open PDF

Abstract

C1 domains are compact α/β structural units of about 50 amino acids which tightly bind two zinc ions. These domains were first discovered as the loci of phorbol ester and diacylglycerol binding to conventional protein kinase C isozymes, which contain two C1 domains (CIA and C1B) in their N‐terminal regulatory regions. We present a comprehensive list of 54 C1 domains occurring singly or doubly in 34 different proteins. Many C1 domains and C1 domain‐containing proteins bind phorbol esters, but many others do not. By combining analysis of 54 C1 domain sequences with information from previously reported solution and crystal structure determinations and site‐directed mutagenesis, profiles are derived and used to classify C1 domains. Twenty‐six C1 domains fit the profile for phorbol‐ester binding and are termed “typical.” Twenty‐eight other domains fit the profile for the overall C1 domain fold but do not fit the profile for phorbol ester binding, and are termed “atypical.” Proteins containing typical C1 domains are predicted to be regulated by diacylglycerol, whereas those containing only atypical domains are not.

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 · 10.1002/pro.5560060228

Cites

30 of 30 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.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

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

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

Protein kinase C - a question of specificity
Dekker, L. V., & Parker, P. J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90038-8 · Cited by 934
Self-citation
The small GTP‐binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.
Ishizaki, T., Maekawa, M., Fujisawa, K., Okawa, K., Iwamatsu, A., Fujita, A., Watanabe, N., Saito, Y., Kakizuka, A., Morii, N., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00539.x · Cited by 887
THE PROTEIN KINASE C FAMILY: HETEROGENEITY AND ITS IMPLICATIONS
Kikkawa, U., Kishimoto, A., & Nishizuka, Y. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.000335 · Cited by 741
Self-citation
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
Self-citation
Lipid activation of protein kinase C.
Bell, R. M., & Burns, D. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67698-2 · Cited by 555
[9] Profile analysis
Gribskov, M., Lothy, R., & Eisenberg, D. S. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)83011-w · Cited by 469
Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase.
Lozano, J., Berra, E., Municio, M. M., Díaz-Meco, M. T., Dominguez, I. M., Sanz, L., & Moscat, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32152-x · Cited by 465
Phorbol ester binding to protein kinase C requires a cysteine-rich zinc-finger-like sequence.
Ono, Y., Fujii, T., Igarashi, K., Kuno, T., Tanaka, C., Kikkawa, U., & Nishizuka, Y. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.4868 · Cited by 437
Self-citation
Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain.
Valverde, Á. M., Sinnett‐Smith, J. W., Lint, J. V., & Rozengurt, E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8572 · Cited by 416
Raf-1 Kinase Possesses Distinct Binding Domains for Phosphatidylserine and Phosphatidic Acid
Ghosh, S., Strum, J. C., Sciorra, V. A., Daniel, L. W., & Bell, R. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8472 · Cited by 415

Flagged first, then by citations

Show all 30 references

Sorted by citations

Items 101–200 of 375

Toward the identification of selective modulators of protein kinase C (PKC) isozymes
Shindo, M., Irie, K., Nakahara, A., Ohigashi, H., Konishi, H., Kikkawa, U., Fukuda, H., & Wender, P. A. (2001) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(01)00100-6 · Cited by 79
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
The Cysteine-Rich Regions of the Regulatory Domains of Raf and Protein Kinase C as Retinoid Receptors
Hoyos, B. E., Imam, A., Chua, R. A., Swenson, C. D., Tong, G., Levi, E., Noy, N., & Hämmerling, U. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.6.835 · Cited by 79
Chapter 1 Functional roles of lipids in membranes
Dowhan, W., & Bogdanov, M. V. (2002) · New comprehensive biochemistry · doi:10.1016/s0167-7306(02)36003-4 · 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
Self-citation
Deletion of a novel protein kinase with PX and FYVE‐related domains increases the rate of differentiation of Trypanosoma brucei
Vassella, E., Krämer, R., Turner, C. M. R., Wankell, M., Modes, C., van den Bogaard, M., & Boshart, M. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02471.x · Cited by 74
Differential subcellular targeting and activity-dependent subcellular localization of diacylglycerol kinase isozymes in transfected cells
Kobayashi, N., Hozumi, Y., Ito, T., Hosoya, T., Kondo, H., & Goto, K. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.05.002 · Cited by 76
Pharmacology of the receptors for the phorbol ester tumor promoters
Kazanietz, M. G., Caloca, M. J., Eroles, P., Fujii, T., García‐Bermejo, L., Reilly, M. P., & Wang, H. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00470-6 · Cited by 72
Where do substrates of diacylglycerol kinases come from? Diacylglycerol kinases utilize diacylglycerol species supplied from phosphatidylinositol turnover-independent pathways
Sakane, F., Mizuno, S., Takahashi, D., & Sakai, H. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.09.003 · Cited by 71
Synthesis and Phorbol Ester Binding of the Cysteine-rich Domains of Diacylglycerol Kinase (DGK) Isozymes
Shindo, M., Irie, K., Masuda, A., Ohigashi, H., Shirai, Y., Miyasaka, K., & Saito, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300400200 · Cited by 70
Mitogenic signaling of Ras is regulated by differential interaction with Raf isozymes
Weber, C. K., Slupsky, J. R., Herrmann, C., Schuler, M., Rapp, U. R., & Block, C. (2000) · Oncogene · doi:10.1038/sj.onc.1203261 · Cited by 70
Regulation of Neurite Outgrowth in N1E-115 Cells through PDZ-Mediated Recruitment of Diacylglycerol Kinase ζ
Yakubchyk, Y., Abramovici, H., Maillet, J., Daher, E., Obagi, C., Parks, R. J., Topham, M. K., & Gee, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7289-7302.2005 · Cited by 70
Phorbol Esters and Related Analogs Regulate the Subcellular Localization of β2-Chimaerin, a Non-protein Kinase C Phorbol Ester Receptor
Caloca, M. J., Wang, H., deLemos, A. S., Wang, S., & Kazanietz, M. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011368200 · Cited by 70
New Era of Diacylglycerol Kinase, Phosphatidic Acid and Phosphatidic Acid-Binding Protein
Sakane, F., Hoshino, F., & Murakami, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186794 · Cited by 74
Protein Kinase C: One Pathway towards the Eradication of Latent HIV-1 Reservoirs
McKernan, L. N., Momjian, D., & Kulkosky, J. (2012) · Advances in Virology · doi:10.1155/2012/805347 · Cited by 72
Protein kinase C and phospholipase C: bilayer interactions and regulation
Hurley, J. H., & Grobler, J. A. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80122-4 · Cited by 68
Self-citation
The Role and Mechanism of Diacylglycerol-Protein Kinase C1 Signaling in Melanogenesis by Cryptococcus neoformans
Heung, L. J., Kaiser, A. E., Luberto, C., & Poeta, M. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503404200 · Cited by 68
A Protein Map and Its Application
Yau, S. S. ‐., Yu, C., & He, R. L. (2008) · DNA and Cell Biology · doi:10.1089/dna.2007.0676 · Cited by 66
Dissecting functions of the retinoblastoma tumor suppressor and the related pocket proteins by integrating genetic, cell biology, and electrophoretic techniques
Hansen, K. H., Lukas, J., Holm, K., Kjerulff, A. A., & Bártek, J. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19990201)20:2 · Cited by 8
Allosteric Regulation of Protein Kinase PKCζ by the N-Terminal C1 Domain and Small Compounds to the PIF-Pocket
Lopez-Garcia, L. A., Schulze, J. O., Fröhner, W., Zhang, H., Süß, E., Weber, N., Navratil, J., Amon, S., Hindie, V., Zeuzem, S., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.08.010 · Cited by 65
The protein kinase C orthologue PkcA plays a role in cell wall integrity and polarized growth in Aspergillus nidulans
Teepe, A. G., Loprete, D. M., He, Z., Hoggard, T., & Hill, T. W. (2006) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2006.10.001 · Cited by 65
RASSF1A gene inactivation in non‐small cell lung cancer and its clinical implication
Endoh, H., Yatabe, Y., Shimizu, S., Tajima, K., Kuwano, H., Takahashi, T., & Mitsudomi, T. (2003) · International Journal of Cancer · doi:10.1002/ijc.11184 · Cited by 65
Dissimilar phorbol ester binding properties of the individual cysteine‐rich motifs of protein kinase D
Iglesias, T., Matthews, S. A., & Rozengurt, E. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01189-2 · Cited by 62
Phorbol Ester-regulated Oligomerization of Diacylglycerol Kinase δ Linked to Its Phosphorylation and Translocation
Imai, S.-I., Sakane, F., & Kanoh, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202035200 · Cited by 61
Diacylglycerol kinase control of protein kinase C
Mérida, I., Arranz‐Nicolás, J., Rodríguez‐Rodríguez, C., & Ávila‐Flores, A. (2019) · Biochemical Journal · doi:10.1042/bcj20180620 · Cited by 61
Structural anatomy of Protein Kinase C C1 domain interactions with diacylglycerol and other agonists
Katti, S. S., Krieger, I. V., Ann, J., Lee, J., Sacchettini, J. C., & Igumenova, T. I. (2022) · Nature Communications · doi:10.1038/s41467-022-30389-2 · Cited by 60
Regulation of protein kinases by lipids
Leonard, T. A., & Hurley, J. H. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.07.006 · Cited by 62
Self-citation
Intramolecular Occlusion of the Diacylglycerol-Binding Site in the C1 Domain of Munc13-1,
Shen, N., Guryev, O. L., & Rizo, J. (2004) · Biochemistry · doi:10.1021/bi0476127 · Cited by 60
Mechanism of Persistent Protein Kinase D1 Translocation and Activation
Oancea, E., Bezzerides, V. J., Greka, A., & Clapham, D. E. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00087-x · Cited by 59
Diacylglycerol Kinase γ Serves as an Upstream Suppressor of Rac1 and Lamellipodium Formation
Tsushima, S., Kai, M., Yamada, K., Imai, S.-I., Houkin, K., Kanoh, H., & Sakane, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314031200 · Cited by 60
Regulation of Diacylglycerol Kinase α by Phosphoinositide 3-Kinase Lipid Products
Ciprés, A., Carrasco, S., Merino, E., Díaz-Flores, E., Krishna, U. M., Falck, J. R., Martínez‐A, C., & Mérida, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305635200 · Cited by 61
The Aspergillus fumigatus pkcAG579R Mutant Is Defective in the Activation of the Cell Wall Integrity Pathway but Is Dispensable for Virulence in a Neutropenic Mouse Infection Model
Rocha, M. C., de Godoy, K. F., de Castro, P. A., Hori, J. I., Bom, V. L. P., Brown, N. A., da Cunha, A. F., Goldman, G. H., & Malavazi, I. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135195 · Cited by 59
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
Diacylglycerol kinase-α phosphorylation by Src on Y335 is required for activation, membrane recruitment and Hgf-induced cell motility
Baldanzi, G., Cutrupi, S., Chianale, F., Gnocchi, V. F., Rainero, E., Porporato, P. E., Filigheddu, N., BLITTERSWIJK, W. J. V., Parolini, O., Bussolino, F., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1210717 · Cited by 56
Activation of c-Raf Kinase by Ultraviolet Light
Hoyos, B., Imam, A., Korichneva, I., Levi, E., Chua, R., & Hammerling, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110750200 · Cited by 55
Evolution, biochemistry and genetics of protein kinase C in fungi
Schmitz, H., & Heinisch, J. J. (2003) · Current Genetics · doi:10.1007/s00294-003-0403-6 · Cited by 54
Protein space: A natural method for realizing the nature of protein universe
Yu, C., Deng, M., Cheng, S.-Y., Yau, S.-C., He, R. L., & Yau, S. S.-T. (2012) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2012.11.005 · Cited by 53
Differential membrane binding and diacylglycerol recognition by C1 domains of RasGRPs
Johnson, J. E., Goulding, R. E., Ding, Z., Partovi, A., Anthony, K., Beaulieu, N., Tazmini, G., Cornell, R. B., & Kay, R. J. (2007) · Biochemical Journal · doi:10.1042/bj20070294 · Cited by 53
PKC‐dependent signalling mechanisms in differentiated smooth muscle
Morgan, K. G., & Leinweber (1998) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.1998.00445.x · Cited by 52
Recent progress on type II diacylglycerol kinases: the physiological functions of diacylglycerol kinase , and and their involvement in disease
Sakai, H., & Sakane, F. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs104 · Cited by 53
Diacylglycerol Kinase-ε: Properties and Biological Roles
Epand, R. M., So, V., Jennings, W., Khadka, B., Gupta, R. S., & Lemaire, M. J. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00112 · Cited by 51
A Ceramide-binding C1 Domain Mediates Kinase Suppressor of Ras Membrane Translocation
Yin, X., Zafrullah, M., Lee, H., Haimovitz‐Friedman, A., FUKS, Z. Y., & Kolesnick, R. (2009) · Cellular Physiology and Biochemistry · doi:10.1159/000233248 · Cited by 50
The Role of PKA, CaMKII, and PKC in Avoidance Conditioning: Permissive or Instructive?
Shobe, J. L. (2002) · Neurobiology of Learning and Memory · doi:10.1006/nlme.2001.4022 · Cited by 50
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
Both the Catalytic and Regulatory Domains of Protein Kinase C Chimeras Modulate the Proliferative Properties of NIH 3T3 Cells
Acs, P. I., Wang, Q. J., Bögi, K., Marquez, A. M., Lorenzo, P. S., Bı́ró, T., Szállási, Z., Mushinski, J. F., & Blumberg, P. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28793 · Cited by 49
Self-citation
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 48
Self-citation
Diacylglycerol kinases in the regulation of dendritic spines
Kim, K., Yang, J., & Kim, E. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06499.x · Cited by 51
A Domain with Homology to Neuronal Calcium Sensors Is Required for Calcium-dependent Activation of Diacylglycerol Kinase α
Jiang, Y., Qian, W., Hawes, J. W., & Walsh, J. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004914200 · Cited by 48
Protein kinase D activation by deletion of its cysteine‐rich motifs
Iglesias, T., & Rozengurt, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00772-3 · Cited by 48
Mechanoregulation of BK channel activity in the mammalian cortical collecting duct: role of protein kinases A and C
Liu, W., Wei, Y., Sun, P., Wang, W., Kleyman, T. R., & Satlin, L. M. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90685.2008 · Cited by 46
Role of the Diacylglycerol Kinase α-Conserved Domains in Membrane Targeting in Intact T Cells
Merino, E., Sanjuán, M. A. F., Moraga, I., Ciprés, A., & Mérida, I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702085200 · Cited by 47
Lipid Signaling in Pathogenic Fungi
Rhome, R. M., & Poeta, M. D. (2009) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073431 · Cited by 44
Farnesol‐mediated inhibition of Candida albicans yeast growth and rescue by a diacylglycerol analogue
Uppuluri, P., Mekala, S., & Chaffin, W. L. (2007) · Yeast · doi:10.1002/yea.1501 · Cited by 45
Atypical protein kinase C in cell motility
Xiao, H., & Liu, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1192-1 · Cited by 50
β-Adrenergic Receptors Activate Exchange Protein Directly Activated by cAMP (Epac), Translocate Munc13-1, and Enhance the Rab3A-RIM1α Interaction to Potentiate Glutamate Release at Cerebrocortical Nerve Terminals
Ferrero, J. J., Alvarez, A. M., Ramírez‐Franco, J., Godino, M. D. C., Bartolomé‐Martín, D., Aguado, C., Torres, M., Luján, R., Ciruela, F., & Sánchez‐Prieto, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463877 · Cited by 46
Establishment of a binding assay for protein kinase C isozymes using synthetic C1 peptides and development of new medicinal leads with protein kinase C isozyme and C1 domain selectivity
Irie, K., Nakahara, A., Nakagawa, Y., Ohigashi, H., Shindo, M., Fukuda, H., Konishi, H., Kikkawa, U., Kashiwagi, K., & Saito, N. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00196-1 · Cited by 46
Synthesis and Biological Activities of Simplified Analogs of the Natural PKC Ligands, Bryostatin‐1 and Aplysiatoxin
Irie, K., & Yanagita, R. C. (2014) · The Chemical Record · doi:10.1002/tcr.201300036 · Cited by 45
Single-Molecule Studies Reveal a Hidden Key Step in the Activation Mechanism of Membrane-Bound Protein Kinase C-α
Ziemba, B. P., Li, J., Landgraf, K. E., Knight, J. D., Voth, G. A., & Falke, J. J. (2014) · Biochemistry · doi:10.1021/bi4016082 · Cited by 47
Immunocytochemical localization of a neuron-specific diacylglycerol kinase β and γ in the developing rat brain
Adachi, N., Oyasu, M., Taniguchi, T., Yamaguchi, Y., Takenaka, R., Shirai, Y., & Saito, N. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.06.007 · Cited by 45
Toward the development of new medicinal leads with selectivity for protein kinase C isozymes
Irie, K., Nakagawa, Y., & Ohigashi, H. (2005) · The Chemical Record · doi:10.1002/tcr.20044 · Cited by 43
Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family
Chen, J., Deng, F., Li, J., & Wang, Q. J. (2008) · Biochemical Journal · doi:10.1042/bj20071334 · Cited by 43
The ubiquitous phosphoinositides
Parker, P. J. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320893 · Cited by 43
Self-citation
New diagnostic method for Alzheimer’s disease based on the toxic conformation theory of amyloid β
Irie, K. (2019) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2019.1667222 · Cited by 41
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
Self-citation
Role of ceramide in apoptosis and development of insulin resistance
Kuzmenko, D. I., & Klimenteva, T. K. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916090017 · Cited by 41
Diacylglycerol Kinase γ Is One of the Specific Receptors of Tumor-Promoting Phorbol Esters
Shindo, M., Irie, K., Ohigashi, H., Kuriyama, M., & Saito, N. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5935 · Cited by 41
Iridals Are a Novel Class of Ligands for Phorbol Ester Receptors with Modest Selectivity for the RasGRP Receptor Subfamily
Shao, L., Lewin, N. E., Lorenzo, P. S., Hu, Z., Enyedy, I. J., Garfield, S. H., Stone, J. C., Marner, F., Blumberg, P. M., & Wang, S. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010258f · Cited by 40
Self-citation
Tracking Diacylglycerol and Phosphatidic Acid Pools in Budding Yeast
Ganesan, S., Shabits, B. N., & Zaremberg, V. (2015) · Lipid Insights · doi:10.4137/lpi.s31781 · Cited by 39
Lipid Messenger, Diacylglycerol, and its Regulator, Diacylglycerol Kinase, in Cells, Organs, and Animals: History and Perspective
Goto, K., Hozumi, Y., Nakano, T., Saino‐Saito, S., & Martelli, A. M. (2008) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.214.199 · Cited by 40
The Catalytic Domain of Protein Kinase C Chimeras Modulates the Affinity and Targeting of Phorbol Ester-induced Translocation
Acs, P. I., Bögi, K., Lorenzo, P. S., Marquez, A. M., Bı́ró, T., Szállási, Z., & Blumberg, P. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22148 · Cited by 39
Self-citation
Novel Features of DAG-Activated PKC Isozymes Reveal a Conserved 3-D Architecture
Lučić, I., Truebestein, L., & Leonard, T. A. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.11.001 · Cited by 39
Diacylglycerol kinases in membrane trafficking
Xie, S., Naslavsky, N., & Caplan, S. (2015) · Cellular Logistics · doi:10.1080/21592799.2015.1078431 · Cited by 36
Enantioselective syntheses of decursinol angelate and decursin
Lim, J., Kim, I. H., Kim, H. H., Ahn, K., & Han, H. (2001) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)00642-6 · 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
Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species
Kamiya, Y., Mizuno, S., Komenoi, S., Sakai, H., & Sakane, F. (2016) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2016.07.017 · Cited by 34
Subcellular Localization Relevance and Cancer-Associated Mechanisms of Diacylglycerol Kinases
Fazio, A., Obeng, E. O., Rusciano, I., Marvi, M. V., Zoli, M., Mongiorgi, S., Ramazzotti, G., Follo, M. Y., McCubrey, J. A., Cocco, L., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155297 · Cited by 34
Role and Mechanism of PKC-δ for Cardiovascular Disease: Current Status and Perspective
Miao, L., Pan, D., Shi, J., Du, J., Chen, P., Gao, J., Yu, Y., Shi, D., & Guo, M. H. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.816369 · Cited by 36
Retinol as electron carrier in redox signaling, a new frontier in vitamin A research.
Hämmerling, U. (2016) · PubMed · doi:10.3978/j.issn.2304-3881.2016.01.02 · Cited by 37
Characterization of the Interaction of Phorbol Esters with the C1 Domain of MRCK (Myotonic Dystrophy Kinase-related Cdc42 Binding Kinase) α/β
Choi, S. H., Czifra, G., Kedei, N., Lewin, N. E., Lázár, J., Pu, Y., Márquez, V. E., & Blumberg, P. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707463200 · Cited by 33
Self-citation
Interactions of Protein Kinase C-α C1A and C1B Domains with Membranes: A Combined Computational and Experimental Study
Li, J., Ziemba, B. P., Falke, J. J., & Voth, G. A. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505369r · Cited by 33
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
Functional implications of the diacylglycerol kinase family
Goto, K., & Kondo, H. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.007 · Cited by 33
Depression of Type I Diacylglycerol Kinases in Pancreatic β-Cells From Male Mice Results in Impaired Insulin Secretion
Kaneko, Y. K., Kobayashi, Y., Motoki, K., Nakata, K., Miyagawa, S., Yamamoto, M., Hayashi, D., Shirai, Y., Sakane, F., & Ishikawa, T. (2013) · Endocrinology · doi:10.1210/en.2013-1356 · Cited by 32
The Implications for Cells of the Lipid Switches Driven by Protein–Membrane Interactions and the Development of Membrane Lipid Therapy
Torres, M., Rosselló, C. A., Fernández‐García, P., Lladó, V., Kakhlon, O., & Escribá, P. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072322 · Cited by 35
Diacylglycerol kinase ζ: At the crossroads of lipid signaling and protein complex organization
Rincón, E., Gharbi, S., Santos-Mendoza, T., & Mérida, I. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.10.001 · Cited by 32
Tumor promoter binding of the protein kinase C C1 homology domain peptides of RasGRPs, chimaerins, and Unc13s
Irie, K., Masuda, A., Shindo, M., Nakagawa, Y., & Ohigashi, H. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.07.008 · Cited by 32
Differential Effect of Bryostatin 1 and Phorbol 12-Myristate 13-Acetate on HOP-92 Cell Proliferation Is Mediated by Down-regulation of Protein Kinase Cδ
Choi, S. H., Hyman, T., & Blumberg, P. M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4177 · Cited by 32
Self-citation
Role of phorbol ester localization in determining protein kinase C or RasGRP3 translocation: Real-time analysis using fluorescent ligands and proteins
Braun, D. C., Cao, Y., Wang, S., Garfield, S. H., Hur, G. M., & Blumberg, P. M. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.141.4.1 · Cited by 32
Self-citation
Inhibition of Membrane Lipid-independent Protein Kinase Cα Activity by Phorbol Esters, Diacylglycerols, and Bryostatin-1
Slater, S. J., Taddeo, F. J., Mazurek, A., Stagliano, B. A., Milano, S. K., Kelly, M. B., Ho, C., & Stubbs, C. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.23160 · Cited by 32
Comparison of the roles of the C1a and C1b domains of protein kinase C alpha in ligand induced translocation in NIH 3T3 cells
Bögi, K., Lorenzo, P. S., Acs, P. I., Szállási, Z., Wagner, G. S., & Blumberg, P. M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00927-8 · Cited by 32
Self-citation
Inhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR Signaling
Kluba, M., Engelborghs, Y., Hofkens, J., & Mizuno, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139971 · Cited by 31
New Bivalent PKC Ligands Linked by a Carbon Spacer: Enhancement in Binding Affinity
Sridhar, J., Wei, Z.-L., Nowak, I., Lewin, N. E., Ayres, J. A., Pearce, L. V., Blumberg, P. M., & Kozikowski, A. P. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0302041 · Cited by 31
Self-citation
Protein Kinase D Interacts with Golgi via Its Cysteine-Rich Domain
Rey, O., & Rozengurt, E. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5530 · Cited by 30
Lipid second messengers derived from glycerolipids and sphingolipids, and their role in smooth muscle function*
Ohanian, J., Liu, G., Ohanian, V., & Heagerty, A. M. (1998) · Acta Physiologica Scandinavica · doi:10.1111/j.1365-201x.1998.tb10703.x · Cited by 30
Differential roles of the tandem C1 domains of protein kinase C delta in the biphasic down-regulation induced by bryostatin 1.
Lorenzo, P. S., Bögi, K., Hughes, K., Beheshti, M., Bhattacharyya, D., Garfield, S. H., Pettit, G. R., & Blumberg, P. M. (1999) · PubMed · Cited by 30
Self-citation
Expression and Localization of Type II Diacylglycerol Kinase Isozymes δ and η in the Developing Mouse Brain
Usuki, T., Sakai, H., Shionoya, T., Sato, N., & Sakane, F. (2014) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155414559130 · Cited by 28
Differential Regulation of Gene Expression in Lung Cancer Cells by Diacyglycerol-Lactones and a Phorbol Ester Via Selective Activation of Protein Kinase C Isozymes
Cooke, M., Casado‐Medrano, V., Ann, J., Lee, J., Blumberg, P. M., Abba, M. C., & Kazanietz, M. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-42581-4 · Cited by 28
Self-citation
Probing the Determinants of Diacylglycerol Binding Affinity in the C1B Domain of Protein Kinase Cα
Stewart, M. D., Morgan, B. R., Massi, F., & Igumenova, T. I. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.020 · Cited by 28
Domain shuffling as a tool for investigation of protein function: substitution of the cysteine-rich region of Raf kinase and PKC η for that of yeast Pkc1p
Schmitz, H., Jöckel, J., Block, C., & Heinisch, J. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4848 · Cited by 28
Lipid metabolism inCryptococcus neoformans
Shea, J. M., Henry, J. L., & Poeta, M. D. (2006) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2006.00080.x · Cited by 27

Authors: Hurley, J. H., Newton, A. C., Parker, P. J., Blumberg, P. M., & Nishizuka, Y.
Affiliations: National Institutes of Health (US)
University of California San Diego (US)
Biosignal Research Center, Kobe University (JP)
Corresponding author: Hurley, James H.
ORCID: Hurley, James H.
Newton, Alexandra C.
Parker, Peter J.
Blumberg, Peter M.
Venue: Protein Science
Publisher: Wiley
Published: 1997-02
Volume: 6
Issue: 2
Pages: 477-480
ISSN: 0961-8368 (ISSN-L)
1469-896X
DOI: 10.1002/pro.5560060228
PMC: PMC2143645
OpenAlex: W2010994547
Cited by: 362
References: 30
Citations by year: 2026: 3 · 2025: 10 · 2024: 3 · 2023: 4 · 2022: 2 · 2021: 10 · 2020: 5 · 2019: 12 · 2018: 4 · 2017: 11 · 2016: 8 · 2015: 13 · 2014: 16 · 2013: 7 · 2012: 16
FWCI: 7.11
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4351 d)
Locations: Protein Science (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords: C1 domain, protein kinase C, phorbol ester binding, zinc-binding domain, protein domain classification
MeSH terms: Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Protein Kinase C, Sequence Homology, Amino Acid

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

Taxonomy and function of C1 protein kinase C homology domains

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks