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Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3
Open accessAbstract
The c-Jun NH(2)-terminal kinase (JNK) group of mitogen-activated protein kinases (MAPKs) is activated in response to the treatment of cells with inflammatory cytokines and by exposure to environmental stress. JNK activation is mediated by a protein kinase cascade composed of a MAPK kinase and a MAPK kinase kinase. Here we describe the molecular cloning of a putative molecular scaffold protein, JIP3, that binds the protein kinase components of a JNK signaling module and facilitates JNK activation in cultured cells. JIP3 is expressed in the brain and at lower levels in the heart and other tissues. Immunofluorescence analysis demonstrated that JIP3 was present in the cytoplasm and accumulated in the growth cones of developing neurites. JIP3 is a member of a novel class of putative MAPK scaffold proteins that may regulate signal transduction by the JNK pathway.
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“The JIPs display a highly polarized subcellular localization at the tips of neuronal cell processes and in extended projections from the surface of insulinoma cells (Meyer et al. 1999; Yasuda et al. 1999; Kelkar et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Kelkar et al. 2000
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“JIP-3 (also known as JSAP) can form oligomeric complexes with itself and JIP-2 but has no sequence relationship to JIP-1 or JIP-2 (Ito et al. 1999; Kelkar et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Kelkar et al. 2000
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BackgroundInfluentialKinesin superfamily motor proteins and intracellular transport
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Protein–protein interactions define specificity in signal transductionPreprint
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“In particular, several proteins have been identified that bind members of the Jnk MAPK pathway and potentiate Jnk activation (Yasuda et al. 1999; Kelkar et al. 2000).”
BackgroundThe role of ABA and MAPK signaling pathways in plant abiotic stress responses
Danquah, A., Zelicourt, A. D., Colcombet, J., & Heribert Hirt, A. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2013.09.006 · Cited by 757
“conserved in all eukaryotic organisms, and have been found in plants, yeast, fungi, insects, nematodes and mammals (Hamel et al., 2012; Kelkar et al., 2000).”
BackgroundCargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
Verhey, K. J., Meyer, D., Deehan, R., Blenis, J., Schnapp, B. J., Rapoport, T. A., & Margolis, B. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.959 · Cited by 609
“6 B) or in COS cells (data not shown), or the localization of endogenous JIP-3 in neuronal cells (Kelkar et al., 2000).”
BackgroundMethodInfluentialUses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases
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Mixed-lineage kinase control of JNK and p38 MAPK pathways
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JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships
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“The sequence similarity of the C-terminal halves of JIP3 and JIP4 to the Rho-GAP domains of several ARHGAP proteins suggests that they might possess a GTPase activator ability toward Rho family small G-proteins (such as Rac1 or Cdc42).”
BackgroundInfluentialIntracellular Transport and Kinesin Superfamily Proteins, KIFs: Structure, Function, and Dynamics
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From JNK to Pay Dirt: Jun Kinases, their Biochemistry, Physiology and Clinical Importance
Karin, M., & Gallagher, E. D. (2005) · IUBMB Life · doi:10.1080/15216540500097111 · Cited by 414
“Several different JNK scaffolding molecules have now been identified, including: b -arrestin-2 ( 62 ), CRK2 ( 63 ), Filamin ( 64 ), IKAP ( 65 ), JIP1 ( 66 ), JIP2 ( 67 ), JIP3 ( 68, 69 ), and JIP4 ( 70 ).”
MethodKinesin-Dependent Axonal Transport Is Mediated by the Sunday Driver (SYD) Protein
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“Interaction We thank Charles Zuker and Edmund Koundakjian (UCSD) for donat- of a mitogen-activated protein kinase signaling module with the ing the Drosophila EMS mutant lines, MaryAnn Martin and Bill Sax- neuronal protein JIP3.”
BackgroundMethodInfluentialDynamic Aspects of CNS Synapse Formation
McAllister, A. K. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.112830 · Cited by 368
“JIP proteins organize components of JNK signaling pathways into functional modules (Davis 2000, Kelkar et al. 2000) and bind these JNK signaling complexes to vesicular cargo (Byrd et al. 2001, Goldstein 2001, Verhey et al. 2001).”
BackgroundDual Leucine Zipper Kinase Is Required for Retrograde Injury Signaling and Axonal Regeneration
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“Hence, JIP3 not only serves as a scaffold for JNK pathway kinases (Kelkar et al., 2000) but is itself regulated by the function of those kinases.”
Molecular recognitions in the MAP kinase cascades
Tanoue, T., & Nishida, E. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00112-2 · Cited by 324
Sunday Driver links axonal transport to damage signaling
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“Syd and JNK3 have been shown to interact in vitro, when isolated from cotransfected cells (Ito et al., 1999; Kelkar et al., 2000).”
InfluentialSakurai‐Yageta, M., Recchi, C., Dez, G. L., Sibarita, J., Daviet, L., Camonis, J., D’Souza‐Schorey, C., & Chavrier, P. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709076 · Cited by 307
“S2 a, available at http://www.jcb.org/cgi/content/full/ jcb.200709076/DC1 ; Kelkar et al., 2000 ).”
Scaffold proteins of MAP-kinase modules
Dhanasekaran, D. N., Kashef, K., Lee, C. M., Xu, H., & Reddy, E. P. (2007) · Oncogene · doi:10.1038/sj.onc.1210411 · Cited by 288
“, 1999), MLK3 (Kelkar et al., 2000), or activator of S phase kinase (ASK1) (Matsuura et al.”
BackgroundInfluentialTargeting the JNK MAPK cascade for inhibition: basic science and therapeutic potential
Bogoyevitch, M. A., Boehm, I., Oakley, A. J., Ketterman, A. J., & Barr, R. K. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.016 · Cited by 270
MAPK signaling pathways in the regulation of hematopoiesis
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“MORG1 ERK Raf-1, B-Raf, MEK, ERK [14] Paxillin ERK MEK, ERK [15] MP1 ERK MEK1, ERK1 [16] MEKK1 ERK Raf-1, MEK1, ERK2 [17, 18] -arrestin-1 ERK Raf-1, MEK1, ERK2 [19] -arrestin-2 JNK Raf-1, MEK1, ERK2 [20] JNK ASK1, MKK4, JNK3 [21] JIP1 JNK MLK2/3, DLK, MKK7, JNK1/2 [22] JIP2 JNK MLK2/3, DLK, MKK7, JNK1/2 [23, 24] p38 M…”
Requirement of the JIP1 scaffold protein for stress-induced JNK activation
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“JIP1, JIP2, and JIP3 antibodies have been described (Yasuda et al. 1999; Kelkar et al. 2000).”
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UNC-16, a JNK-Signaling Scaffold Protein, Regulates Vesicle Transport in C. elegans
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Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity
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Akt1 Regulates a JNK Scaffold during Excitotoxic Apoptosis
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“The oligos do not correspond to the recently reported human JIP2 (Yasuda et al., 1999) and JIP3 (Kelkar et al., 2000), which probably represent additional families of JIPs.”
BackgroundRegulatory mechanisms of mitogen-activated kinase signaling
Zhang, Y., & Dong, C. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7012-3 · Cited by 188
Matsuda, S., Yasukawa, T., Homma, Y., Ito, Y., Niikura, T., Hiraki, T., Hirai, S., Ohno, S., Kita, Y. A., Kawasumi, M., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-17-06597.2001 · Cited by 184
Bardwell, A. J., Flatauer, L. J., Matsukuma, K. E., Thorner, J. W., & Bardwell, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010271200 · Cited by 177
Kelkar, N., Standen, C. L., & Davis, R. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2733-2743.2005 · Cited by 157
“JIP3, and KLC were described previously (13, 34).”
BackgroundInfluentialThe JIP family of MAPK scaffold proteins
Whitmarsh, A. J. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340828 · Cited by 169
Cliffe, A. R., Arbuckle, J. H., Vogel, J. L., Geden, M. J., Rothbart, S. B., Cusack, C. L., Strahl, B. D., Kristie, T. M., & Deshmukh, M. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.11.007 · Cited by 158
“As DLK and JIP3 are expressed almost exclusively in neurons (Hirai et al., 2005; Kelkar et al., 2000), targeting them would be an effective mechanism to prevent HSV reactivation in response to multiple triggers.”
BackgroundScheinfeld, M. H., Roncarati, R., Vito, P., Lopez, P., Abdallah, M., & D'adamio, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108357200 · Cited by 160
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ARF6–JIP3/4 regulate endosomal tubules for MT1-MMP exocytosis in cancer invasion
Marchesin, V., Castro-Castro, A., Lodillinsky, C., Castagnino, A., Cyrta, J., Bonsang-Kitzis, H., Fuhrmann, L., Irondelle, M., Infante, E., Montagnac, G., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201506002 · Cited by 160
“The N-terminal region of JIP3 and JIP4 contains two leucine zipper (LZI and LZII) domains known to mediate dimerization of the proteins (Kelkar et al., 2000; Nguyen et al., 2005; Isabet et al., 2009).”
The bottleneck of JNK signaling: Molecular and functional characteristics of MKK4 and MKK7
Haeusgen, W., Herdegen, T., & Waetzig, V. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.008 · Cited by 151
AKAP-Lbc Nucleates a Protein Kinase D Activation Scaffold
Carnegie, G. K., Smith, F. D., McConnachie, G., Langeberg, L. K., & Scott, J. D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.015 · Cited by 148
Mixed-Lineage Kinases: A Target for the Prevention of Neurodegeneration
Wang, L. H., Besirli, C. G., & Johnson, E. M. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121840 · Cited by 145
“Finally, scaffolding proteins, such as JIP1 and JIP3, interact with specific members of the MLK, MKK, and JNK kinase families, thus providing another level of regulation of JNK pathway activation (26, 27).”
BackgroundDrerup, C. M., & Nechiporuk, A. V. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003303 · Cited by 145
“During axon extension (30 hpf), Jip3-mCherry localized to the neuronal cell body and axon growth cones (Figure 1J, 1K), similar to Jip3 localization in cultured neurons [27].”
BackgroundJLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors
Lee, C. M., Onésime, D., Reddy, C. D., Dhanasekaran, N., & Reddy, E. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232310199 · Cited by 139
Strength in diversity: Understanding the pathways to herpes simplex virus reactivation
Suzich, J. B., & Cliffe, A. R. (2018) · Virology · doi:10.1016/j.virol.2018.07.011 · Cited by 144
“Highly expressed in neurons (Hirai et al., 2005; Kelkar et al., 2000), DLK is a key candidate for therapies that counteract neurodegeneration and may also be an ideal target to prevent HSV reactivation.”
BackgroundPrinciples of cargo attachment to cytoplasmic motor proteins
Kamal, A., & Goldstein, L. S. B. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(01)00295-2 · Cited by 134
Waetzig, V., Zhao, Y., & Herdegen, T. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.08.002 · Cited by 130
Taru, H., Iijima, K., Hase, M., Kirino, Y., Yagi, Y., & Suzuki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108372200 · Cited by 128
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“In mammals, four JIP proteins that activate the p38 MAPK pathway have been identified, JIP1 (14), JIP2 (15), JIP3 (16, 17), and JIP4 (18), whereas A.”
BackgroundRegulation of MAP kinases by docking domains
Enslen, H., & Davis, R. J. (2001) · Biology of the Cell · doi:10.1016/s0248-4900(01)01156-x · Cited by 124
“MP1 binds specifically ERK1 and MEK1 (Schaeffer et al., 1998), JIP proteins binds the MAPKKK MLKs, MKK7 and JNK1/2 (Kelkar et al., 2000; Whitmarsh et al., 1998; Yasuda et al., 1999) and -arrestin2 is a scaffold for both the ERK and JNK pathways (Luttrell et al., 2001; McDonald et al., 2000).”
BackgroundVerhey, K. J., & Rapoport, T. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01931-4 · Cited by 115
Identification of NPM-ALK interacting proteins by tandem mass spectrometry
Crockett, D. K., Lin, Z., Elenitoba‐Johnson, K. S. J., & Lim, M. S. (2004) · Oncogene · doi:10.1038/sj.onc.1207398 · Cited by 113
Muresan, Z. L., & Mureşan, V. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502043 · Cited by 112
“JIP constructs (pcMV-FLAG-JIP-1, pcDNA3-FLAG-JIP-2, and pcDNA3-FLAG-JIP-3) were obtained from R. Davis (University of Massachusetts Medical School, Howard Hughes Medical Institute, Worcester, MA; Whitmarsh et al., 1998; Yasuda et al., 1999; Kelkar et al., 2000).”
MethodSignaling Complexes: Junctions on the Intracellular Information Super Highway
Smith, F. D., & Scott, J. D. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00646-7 · Cited by 112
The JNK-interacting Protein-1 Scaffold Protein Targets MAPK Phosphatase-7 to Dephosphorylate JNK
Willoughby, E. A., Perkins, G. R., Collins, M. K., & Whitmarsh, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207324200 · Cited by 109
Nihalani, D., Meyer, D., Pajni, S., & Holzman, L. B. (2001) · The EMBO Journal · doi:10.1093/emboj/20.13.3447 · Cited by 107
MAP Kinase Modules: Many Roads Home
Raman, M., & Cobb, M. H. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.053 · Cited by 107
Sunday Driver/JIP3 binds kinesin heavy chain directly and enhances its motility
Sun, F., Zhu, C., Dixit, R., & Cavalli, V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.229 · Cited by 103
“…in a genetic screen for axonal transport mutants and was shown to interact directly with KLC (Bowman et al, 2000). syd is a member of the JIP family of proteins, which interact with the c-Jun N-terminal kinase (JNK), and is thus also known as JIP3 (Kelkar et al, 2000) or JSAP1 (Ito et al, 1999).”
BackgroundInfluentialScaffold proteins in MAP kinase signaling: more than simple passive activating platforms
Dard, N., & Peter, M. (2006) · BioEssays · doi:10.1002/bies.20351 · Cited by 106
“This finding is consistent with the observed accumulation of JIP scaffolds in growth cones at the tips of extendedneurites,((32,33,48)) andwith impaired neurite outgrowth after inhibition of JNK activity.”
A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria
Wiltshire, C. J., Matsushita, M., Tsukada, S., Gillespie, D. A., & May, G. (2002) · Biochemical Journal · doi:10.1042/bj20020553 · Cited by 103
Neisch, A. L., Neufeld, T. P., & Hays, T. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201606082 · Cited by 87
“Scaffolding proteins can provide an additional level of regulation through their association with posttranslational protein modifiers, such as kinases and phosphatases (Yasuda et al., 1999; Kelkar et al., 2000; Willoughby et al., 2003; Horiuchi et al., 2007).”
BackgroundDual leucine zipper kinase is required for excitotoxicity-induced neuronal degeneration
Pozniak, C. D., Ghosh, A. S., Gogineni, A., Hanson, J. E., Lee, S.-H., Larson, J. L., Solanoy, H. O., Bustos, D. J., Li, H., Ngu, H., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20122832 · Cited by 107
“…a recent mass spectrometry–based study examining JIP3-interacting proteins identified >100 direct and indirect interactors but no MAP kinases (Abe et al., 2009), despite several studies confirming that these proteins indeed interact (Kelkar et al., 2000; Cavalli et al., 2005; Ghosh et al., 2011).”
BackgroundMiura, E., Fukaya, M., Sato, T., Sugihara, K., Asano, M., Yoshioka, K., & Watanabe, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03835.x · Cited by 97
“1999), and that JIP3/JSAP1 is degraded by caspase 3 in PC12 cells by nerve growth factor (NGF) depletion (Kelkar et al. 2000).”
BackgroundResultInfluentialNerve Growth Factor, Neural Stem Cells and Alzheimer’s Disease
Heese, K., Low, J. W., & Inoue, N. (2006) · Neurosignals · doi:10.1159/000094383 · Cited by 97
Phosphorylation-dependent Scaffolding Role of JSAP1/JIP3 in the ASK1-JNK Signaling Pathway
Matsuura, H., Nishitoh, H., Takeda, K., Matsuzawa, A., Amagasa, T., Ito, M., Yoshioka, K., & Ichijo, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202004200 · Cited by 10
Matsuda, S., Matsuda, Y., & D'adamio, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304379200 · Cited by 97
Matsuguchi, T., Masuda, A., Sugimoto, K., Nagai, Y., & Yoshikai, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg438 · Cited by 95
Wasserman, T., Cohen‐Katsenelson, K., Daniliuc, S., Hasin, T., Choder, M., & Aronheim, A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-06-0512 · Cited by 97
“These results are in accordance with previous reports showing the JIP 1-3 proteins are expressed at low levels in nonneuronal tissues (Yasuda et al., 1999; Kelkar et al., 2000).”
ResultGuan, Q.-H., Pei, D., Zong, Y.-Y., Xu, T., & Zhang, G.-Y. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.11.067 · Cited by 90
Whisenant, T. C., Ho, D. T., Benz, R. W., Rogers, J. S., Kaake, R. M., Gordon, E. A., Huang, L., Baldi, P., & Bardwell, L. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000908 · Cited by 96
“To evaluate the utility of an HMM-based approach for finding novel D-sites, a list of 20 proteins containing functionally verified JNK-docking sites was compiled from our own results and the work of many others [17,18,44,45,46,47,48,49,50,51,52,53,54,55,56] (Fig.”
BackgroundSize control: the developmental physiology of body and organ size regulation
Gokhale, R. H., & Shingleton, A. W. (2015) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.181 · Cited by 93
Huang, S.-H., Duan, S., Sun, T., Wang, J., Zhao, L., Geng, Z., Yan, J., Sun, H., & Chen, Z.-Y. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0436-11.2011 · Cited by 93
“JIP3 was originally identified as a JNK-binding protein and functions as a scaffold protein to trigger specific JNK signaling modules (Ito et al., 1999; Kelkar et al., 2000).”
BackgroundGindhart, J. G., Chen, J., Faulkner, M., Gandhi, R., Doerner, K., Wisniewski, T., & Nandlestadt, A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0800 · Cited by 90
“Posttranslational modification of UNC-76 by PKC could regulate UNC-76 binding to KHC, or UNC-76 could recruit regulatory proteins or cargos to the kinesin tail domain, as has been suggested for the KLC-binding scaffold proteins JIP1, JIP2, and JIP3/JSAP1 (SYD), which bind kinesin and members of the JNK signaling casca…”
Diverse Roles of JNK and MKK Pathways in the Brain
Yamasaki, T., Kawasaki, H., & Nishina, H. (2012) · Journal of Signal Transduction · doi:10.1155/2012/459265 · Cited by 90
“Phenotypic differences between knockouts of MKK4 and MKK7 have also been observed, suggesting that the JNK signaling pathway in the brain has a complex nature and is intricately regulated.”
BackgroundDynamic gene expression during the onset of myoblast differentiation in vitro
Delgado, I. J., Huang, X., Jones, S. E., Zhang, L., Hatcher, R. J., Gao, B., & Zhang, P. (2003) · Genomics · doi:10.1016/s0888-7543(03)00104-6 · Cited by 88
Jagadish, N., Rana, R., Selvi, R., Mishra, D., Garg, M., Yadav, S., Herr, J. C., Okumura, K., Hasegawa, A., Koyama, K., et al. (2005) · Biochemical Journal · doi:10.1042/bj20041577 · Cited by 87
Nihalani, D., Wong, H. N., & Holzman, L. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304212200 · Cited by 85
Taru, H., Kirino, Y., & Suzuki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203713200 · Cited by 85
Kelkar, N., Delmotte, M.-H., Weston, C. R., Barrett, T., Sheppard, B. J., Flavell, R. A., & Davis, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1733944100 · Cited by 83
Trafficking of signaling modules by kinesin motors
Schnapp, B. J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00488 · Cited by 82
“Through its interactions with clathrin and specific receptor-ligand complexes (Pearse, 1988), AP-1 coordinates the formation of specific vesicle populations at the Golgi apparatus and the plasma membrane (reviewed in Kirchhausen, 2002).”
BackgroundMuresan, Z. L., & Mureşan, V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0152-05.2005 · Cited by 81
“However, the JNK scaffolding protein, JIP-3, is structurally distinct from JIP-1 and JIP-2 and does not contain a PTB domain (Kelkar et al., 2000).”
BackgroundMethodInfluentialJNK3 as Therapeutic Target and Biomarker in Neurodegenerative and Neurodevelopmental Brain Diseases
Musi, C. A., Agrò, G., Santarella, F., Iervasi, E., & Borsello, T. (2020) · Cells · doi:10.3390/cells9102190 · Cited by 78
“In addition, JIP-3 itself is a JNK target, since it can be phosphorylated only by JNK and not by p38 and ERK [61].”
BackgroundDocking Interactions in the c-Jun N-terminal Kinase Pathway
Mooney, L. M., & Whitmarsh, A. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311841200 · Cited by 73
Autoinhibition of Mixed Lineage Kinase 3 through Its Src Homology 3 Domain
Zhang, H., & Gallo, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107176200 · Cited by 76
Molecular Mechanisms of Neurodegeneration in Spinal Muscular Atrophy
Ahmad, S., Bhatia, K., Kannan, A., & Gangwani, L. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s33122 · Cited by 78
Pin1 Mediates Neural-Specific Activation of the Mitochondrial Apoptotic Machinery
Becker, E. B. E., & Bonni, A. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.034 · Cited by 76
Ca2 dynamics in synaptosomes isolated from the squid optic lobe
Benech, J. C., Lima, P. A., Sotelo, J. R., & Brown, E. R. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20001215)62:6 · Cited by 10
The role of scaffold proteins in JNK signalling
Engström, W., Ward, A., & Moorwood, K. (2009) · Cell Proliferation · doi:10.1111/j.1365-2184.2009.00654.x · Cited by 73
Scaffold Proteins in Mammalian MAP Kinase Cascades
Yoshioka, K. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh079 · Cited by 73
“Transfection experiments suggest that JSAP1 may coordinate several distinct JNK signaling modules, containing ASK1, MEKK1, and MLK3 as the MAP3K, and enhance the MAP3Kinduced activation of JNK (18, 19, 21).”
BackgroundSong, J. J., & Lee, Y. J. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502070 · Cited by 73
“JIP1 scaffold facilitates JNK activation in an MLK-MKK7–dependent manner (Dickens et al., 1997; Whitmarsh et al., 1998; Yasuda et al., 1999; Kelkar et al., 2000).”
BackgroundOlsten, M. E. K., Canton, D. A., Zhang, C., Walton, P. A., & Litchfield, D. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407628200 · Cited by 72
Myers, K. R., Wang, G., Sheng, Y., Conger, K. K., Casanova, J. E., & Zhu, J. J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1942-12.2012 · Cited by 74
“These results are consistent with previous observations that Arf6 can signal downstream via a neuronal scaffolding protein JIP3 (Montagnac et al., 2009; Suzuki et al., 2010), and that JIP3 regulates JNK signaling(Kelkar et al., 2000; Ongusaha et al., 2008).”
BackgroundResultSpecific Modulation of Astrocyte Inflammation by Inhibition of Mixed Lineage Kinases with CEP-1347
Falsig, J., Pörzgen, P., Lotharius, J., & Leist, M. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.4.2762 · Cited by 71
Metadata
- Authors
- Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Davis, Roger J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-02-01
- Volume
- 20
- Issue
- 3
- Pages
- 1030-1043
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC85220
- OpenAlex
- W2147103035
- Cited by
- 281
- References
- 71
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 7 · 2021: 5 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 10 · 2016: 7 · 2015: 9 · 2014: 8 · 2013: 7 · 2012: 6
- FWCI
- 8.62
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute
- 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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- JIP3, JNK, c-Jun NH2-terminal kinase, MAPK signaling, MAPK kinase, MAPK kinase kinase, growth cones, neurite development, signal transduction regulation, brain expression
- MeSH terms
- Aging, Amino Acid Sequence, Animals, Brain, Cells, Cultured, Cloning, Molecular, Enzyme Activation, Female, Embryonic and Fetal Development, Male, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Recombinant Proteins, Signal Transduction, Gene Library, Sequence Alignment, Sequence Homology, Amino Acid, Gene Expression Regulation, Developmental, Protein Isoforms, Mitogen-Activated Protein Kinases, MAP Kinase Kinase Kinases, JNK Mitogen-Activated Protein Kinases, Adaptor Proteins, Signal Transducing, Mice
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