Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

Kelkar, Nyaya; Gupta, Shashi; Dickens, Martin; Davis, Roger J.

doi:10.1128/mcb.20.3.1030-1043.2000

Cited by 281Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

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Kelkar, Nyaya, Gupta, Shashi, Dickens, Martin, Davis, Roger J.·2000·Molecular and Cellular Biology

DOI 10.1128/mcb.20.3.1030-1043.2000PMC PMC85220

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Abstract

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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JIPs display a highly polarized subcellular localization at the tips of neuronal cell processes and in extended projections from the surface of insulinoma cells.
“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
JIP-3 can form oligomeric complexes with itself and JIP-2 but has no sequence relationship to JIP-1 or JIP-2.
“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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BackgroundResultInfluential
Abscisic Acid and Abiotic Stress Tolerance in Crop Plants
Sah, S. K., Reddy, K. R., & Li, J. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00571 · Cited by 1,350 · see citing works
Molecular motors and mechanisms of directional transport in neurons
Hirokawa, N., & Takemura, R. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1624 · Cited by 830 · see citing works
“JIPs are abundant at the tips of neuronal processes and synaptic junctions, where the plus ends of microtubules are foun”
Background
MAP Kinases
Chen, Z., Gibson, T. B., Robinson, F. L., Silvestro, L., Pearson, G. W., Xu, B.-E., Wright, A., Vanderbilt, C. A., & Cobb, M. H. (2001) · Chemical Reviews · doi:10.1021/cr000241p · Cited by 789 · see citing works
Regulation of MAP Kinase Signaling Modules by Scaffold Proteins in Mammals
Morrison, D. K., & Davis, R. J. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111401.091942 · Cited by 787 · see citing works
Protein–protein interactions define specificity in signal transductionPreprint
Pawson, T. J., & Nash, P. (2000) · Genes & Development · doi:10.1101/gad.14.9.1027 · Cited by 775 · see citing works
“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).”
Background
The 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 · see citing works
“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).”
Background
Cargo 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 · see citing works
“6 B) or in COS cells (data not shown), or the localization of endogenous JIP-3 in neuronal cells (Kelkar et al., 2000).”
BackgroundMethodInfluential
Uses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases
Bogoyevitch, M. A., & Kobe, B. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00025-06 · Cited by 572 · see citing works
Mixed-lineage kinase control of JNK and p38 MAPK pathways
Gallo, K. A., & Johnson, G. L. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm906 · Cited by 572 · see citing works
JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships
Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 524 · see citing works
“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).”
BackgroundInfluential
Intracellular Transport and Kinesin Superfamily Proteins, KIFs: Structure, Function, and Dynamics
Hirokawa, N., & Noda, Y. (2008) · Physiological Reviews · doi:10.1152/physrev.00023.2007 · Cited by 510 · see citing works
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 · see citing works
“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 ).”
Method
Kinesin-Dependent Axonal Transport Is Mediated by the Sunday Driver (SYD) Protein
Bowman, A. B., Kamal, A., Ritchings, B. W., Philp, A. V., McGrail, M. A., Gindhart, J. G., & Goldstein, L. S. B. (2000) · Cell · doi:10.1016/s0092-8674(00)00162-8 · Cited by 331 · see citing works
“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.”
BackgroundMethodInfluential
Dynamic Aspects of CNS Synapse Formation
McAllister, A. K. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.112830 · Cited by 368 · see citing works
“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).”
Background
Dual Leucine Zipper Kinase Is Required for Retrograde Injury Signaling and Axonal Regeneration
Shin, J. E., Cho, Y., Beirowski, B., Milbrandt, J., Cavalli, V., & DiAntonio, A. (2012) · Neuron · doi:10.1016/j.neuron.2012.04.028 · Cited by 323 · see citing works
“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 318 · see citing works
Sunday Driver links axonal transport to damage signaling
Cavalli, V., Kujala, P., Klumperman, J., & Goldstein, L. S. B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410136 · Cited by 315 · see citing works
“Syd and JNK3 have been shown to interact in vitro, when isolated from cotransfected cells (Ito et al., 1999; Kelkar et al., 2000).”
Influential
The interaction of IQGAP1 with the exocyst complex is required for tumor cell invasion downstream of Cdc42 and RhoA
Sakurai‐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 · see citing works
“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 · see citing works
“, 1999), MLK3 (Kelkar et al., 2000), or activator of S phase kinase (ASK1) (Matsuura et al.”
BackgroundInfluential
Targeting 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 268 · see citing works
MAPK signaling pathways in the regulation of hematopoiesis
Geest, C. R., & Coffer, P. J. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0209097 · Cited by 261 · see citing works
“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
Whitmarsh, A. J., Kuan, C.-Y., Kennedy, N. J., Kelkar, N., Haydar, T. F., Mordes, J. P., Appel, M., Rossini, A. A., Jones, S. N., Flavell, R. A., et al. (2001) · Genes & Development · doi:10.1101/gad.922801 · Cited by 238 · see citing works
“JIP1, JIP2, and JIP3 antibodies have been described (Yasuda et al. 1999; Kelkar et al. 2000).”
BackgroundMethodResultInfluential
Ceramide Directly Activates Protein Kinase C ζ to Regulate a Stress-activated Protein Kinase Signaling Complex
Bourbon, N. A., Yun, J. K., & KESTER, M. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007346200 · Cited by 234 · see citing works
UNC-16, a JNK-Signaling Scaffold Protein, Regulates Vesicle Transport in C. elegans
Byrd, D. T., Kawasaki, M., Walcoff, M., Hisamoto, N., Matsumoto, K., & Jin, Y. (2001) · Neuron · doi:10.1016/s0896-6273(01)00532-3 · Cited by 234 · see citing works
Dynein activators and adaptors at a glance
Olenick, M. A., & Holzbaur, E. L. F. (2019) · Journal of Cell Science · doi:10.1242/jcs.227132 · Cited by 218 · see citing works
Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity
Barr, R. K., Kendrick, T. S., & Bogoyevitch, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107565200 · Cited by 211 · see citing works
Akt1 Regulates a JNK Scaffold during Excitotoxic Apoptosis
Kim, A. H., Yano, H., Cho, H., Meyer, D. J., Monks, B. R., Margolis, B. L., Birnbaum, M. J., & Chao, M. V. (2002) · Neuron · doi:10.1016/s0896-6273(02)00821-8 · Cited by 206 · see citing works
ARF6 Interacts with JIP4 to Control a Motor Switch Mechanism Regulating Endosome Traffic in Cytokinesis
Montagnac, G., Sibarita, J., Loubéry, S., Daviet, L., Romao, M., Raposo, G., & Chavrier, P. (2009) · Current Biology · doi:10.1016/j.cub.2008.12.043 · Cited by 203 · see citing works
Kinesin molecular motors: Transport pathways, receptors, and human disease
Goldstein, L. S. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111145298 · Cited by 202 · see citing works
Dual Roles for c-Jun N-Terminal Kinase in Developmental and Stress Responses in Cerebellar Granule Neurons
Coffey, E. T., Hongisto, V., Dickens, M., Davis, R. J., & Courtney, M. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-20-07602.2000 · Cited by 191 · see citing works
“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.”
Background
Regulatory 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 187 · see citing works
c-Jun N-Terminal Kinase (JNK)-Interacting Protein-1b/Islet-Brain-1 Scaffolds Alzheimer's Amyloid Precursor Protein with JNK
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 · see citing works
A Conserved Docking Site in MEKs Mediates High-affinity Binding to MAP Kinases and Cooperates with a Scaffold Protein to Enhance Signal Transmission
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 · see citing works
Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways
Kelkar, N., Standen, C. L., & Davis, R. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2733-2743.2005 · Cited by 171 · see citing works
“JIP3, and KLC were described previously (13, 34).”
BackgroundInfluential
The JIP family of MAPK scaffold proteins
Whitmarsh, A. J. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340828 · Cited by 169 · see citing works
Neuronal Stress Pathway Mediating a Histone Methyl/Phospho Switch Is Required for Herpes Simplex Virus Reactivation
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 161 · see citing works
“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.”
Background
Jun NH2-terminal Kinase (JNK) Interacting Protein 1 (JIP1) Binds the Cytoplasmic Domain of the Alzheimer's β-Amyloid Precursor Protein (APP)
Scheinfeld, 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 158 · see citing works
A Scaffold Protein JIP-1b Enhances Amyloid Precursor Protein Phosphorylation by JNK and Its Association with Kinesin Light Chain 1
Inomata, H., Nakamura, Y., Hayakawa, A., Takata, H., Suzuki, T., Miyazawa, K., & Kitamura, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212160200 · Cited by 158 · see citing works
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) · The Journal of Cell Biology · doi:10.1083/jcb.201506002 · Cited by 149 · see citing works
“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 149 · see citing works
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 · see citing works
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 · see citing works
“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).”
Background
JNK-Interacting Protein 3 Mediates the Retrograde Transport of Activated c-Jun N-Terminal Kinase and Lysosomes
Drerup, C. M., & Nechiporuk, A. V. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003303 · Cited by 144 · see citing works
“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].”
Background
JLP: 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 · see citing works
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 136 · see citing works
“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.”
Background
Principles 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 133 · see citing works
The bright side of JNKs—Multitalented mediators in neuronal sprouting, brain development and nerve fiber regeneration
Waetzig, V., Zhao, Y., & Herdegen, T. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.08.002 · Cited by 129 · see citing works
Interaction of Alzheimer's β-Amyloid Precursor Family Proteins with Scaffold Proteins of the JNK Signaling Cascade
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 · see citing works
Plasmodium falciparum evades mosquito immunity by disrupting JNK-mediated apoptosis of invaded midgut cells
Ramphul, U. N., Garver, L. S., Molina-Cruz, A., Cánepa, G. E., & Barillas-Mury, C. V. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1423586112 · Cited by 127 · see citing works
“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.”
Background
Regulation 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 · see citing works
“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).”
Background
Kinesin carries the signal
Verhey, K. J., & Rapoport, T. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01931-4 · Cited by 115 · see citing works
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 · see citing works
Coordinated transport of phosphorylated amyloid-β precursor protein and c-Jun NH2-terminal kinase–interacting protein-1
Muresan, Z. L., & Mureşan, V. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502043 · Cited by 112 · see citing works
“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).”
Method
Signaling 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 · see citing works
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 · see citing works
Mixed lineage kinase‐dependent JNK activation is governed by interactions of scaffold protein JIP with MAPK module components
Nihalani, D., Meyer, D., Pajni, S., & Holzman, L. B. (2001) · The EMBO Journal · doi:10.1093/emboj/20.13.3447 · Cited by 107 · see citing works
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 · see citing works
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 107 · see citing works
“…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).”
BackgroundInfluential
Scaffold 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 · see citing works
“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 · see citing works
A STRIPAK complex mediates axonal transport of autophagosomes and dense core vesicles through PP2A regulation
Neisch, A. L., Neufeld, T. P., & Hays, T. S. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201606082 · Cited by 103 · see citing works
“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).”
Background
Dual 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 100 · see citing works
“…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).”
Background
Expression and distribution of JNK/SAPK‐associated scaffold protein JSAP1 in developing and adult mouse brain
Miura, 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 · see citing works
“1999), and that JIP3/JSAP1 is degraded by caspase 3 in PC12 cells by nerve growth factor (NGF) depletion (Kelkar et al. 2000).”
BackgroundResultInfluential
Nerve Growth Factor, Neural Stem Cells and Alzheimer’s Disease
Heese, K., Low, J. W., & Inoue, N. (2006) · Neurosignals · doi:10.1159/000094383 · Cited by 96 · see citing works
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 · see citing works
Amyloid β Protein Precursor (AβPP), but Not AβPP-like Protein 2, Is Bridged to the Kinesin Light Chain by the Scaffold Protein JNK-interacting Protein 1
Matsuda, S., Matsuda, Y., & D'adamio, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304379200 · Cited by 93 · see citing works
JNK‐interacting protein 3 associates with Toll‐like receptor 4 and is involved in LPS‐mediated JNK activation
Matsuguchi, T., Masuda, A., Sugimoto, K., Nagai, Y., & Yoshikai, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg438 · Cited by 93 · see citing works
A Novel c-Jun N-terminal Kinase (JNK)-binding Protein WDR62 Is Recruited to Stress Granules and Mediates a Nonclassical JNK Activation
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 93 · see citing works
“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).”
Result
Neuroprotection against ischemic brain injury by a small peptide inhibitor of c-Jun N-terminal kinase (JNK) via nuclear and non-nuclear pathways
Guan, Q.-H., Pei, D., Zong, Y.-Y., Xu, T., & Zhang, G.-Y. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.11.067 · Cited by 92 · see citing works
Computational Prediction and Experimental Verification of New MAP Kinase Docking Sites and Substrates Including Gli Transcription Factors
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 91 · see citing works
“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.”
Background
Size 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 89 · see citing works
JIP3 Mediates TrkB Axonal Anterograde Transport and Enhances BDNF Signaling by Directly Bridging TrkB with Kinesin-1
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 90 · see citing works
“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).”
Background
The Kinesin-associated Protein UNC-76 Is Required for Axonal Transport in theDrosophilaNervous System
Gindhart, 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 · see citing works
“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 · see citing works
“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.”
Background
Dynamic 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 · see citing works
Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein
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 · see citing works
Recruitment of JNK to JIP1 and JNK-dependent JIP1 Phosphorylation Regulates JNK Module Dynamics and Activation
Nihalani, D., Wong, H. N., & Holzman, L. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304212200 · Cited by 85 · see citing works
Differential Roles of JIP Scaffold Proteins in the Modulation of Amyloid Precursor Protein Metabolism
Taru, H., Kirino, Y., & Suzuki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203713200 · Cited by 85 · see citing works
Morphogenesis of the telencephalic commissure requires scaffold protein JNK-interacting protein 3 (JIP3)
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 · see citing works
Trafficking of signaling modules by kinesin motors
Schnapp, B. J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00488 · Cited by 81 · see citing works
“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).”
Background
c-Jun NH2-Terminal Kinase-Interacting Protein-3 Facilitates Phosphorylation and Controls Localization of Amyloid-β Precursor Protein
Muresan, Z. L., & Mureşan, V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0152-05.2005 · Cited by 80 · see citing works
“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).”
BackgroundMethodInfluential
JNK3 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 · see citing works
“In addition, JIP-3 itself is a JNK target, since it can be phosphorylated only by JNK and not by p38 and ERK [61].”
Background
Docking 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 · see citing works
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 · see citing works
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 · see citing works
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 75 · see citing works
Neurofibromatosis type 1 I. General overview
Lakkis, M. M., & Tennekoon, G. I. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20001215)62:6 · Cited by 55 · see citing works
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 · see citing works
Scaffold Proteins in Mammalian MAP Kinase Cascades
Yoshioka, K. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh079 · Cited by 73 · see citing works
“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).”
Background
Dissociation of Akt1 from its negative regulator JIP1 is mediated through the ASK1–MEK–JNK signal transduction pathway during metabolic oxidative stress
Song, J. J., & Lee, Y. J. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502070 · Cited by 73 · see citing works
“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).”
Background
The Pleckstrin Homology Domain of CK2 Interacting Protein-1 Is Required for Interactions and Recruitment of Protein Kinase CK2 to the Plasma Membrane
Olsten, 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 · see citing works
Arf6-GEF BRAG1 Regulates JNK-Mediated Synaptic Removal of GluA1-Containing AMPA Receptors: A New Mechanism for Nonsyndromic X-Linked Mental Disorder
Myers, K. R., Wang, G., Sheng, Y., Conger, K. K., Casanova, J. E., & Zhu, J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1942-12.2012 · Cited by 70 · see citing works
“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).”
BackgroundResult
Specific 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 · see citing works

Interaction of a mitogenactivated protein kinase signaling module with the neuronal protein JIP3. Mol Cell Biol
Kelkar, N., Gupta, S., Dickens, M., Davis, R. J., Gupta, S., & Davis, R. J. (2000)
Subcellular distribution and funciton of the neuronal JNK signalling pathway scaffold protein JIP3
Caswell, P. T. (2004) · Figshare
Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways
Kelkar, N., Standen, C. L., & Davis, R. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2733-2743.2005 · Cited by 171 · see citing works
The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins
Yasuda, J., Whitmarsh, A. J., Cavanagh, J., Sharma, M., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7245 · Cited by 458 · see citing works
Colocalization and Interaction Study of Neuronal JNK3, JIP1, and β-Arrestin2 Together with PSD95
Musi, C. A., Marchini, G., Giani, A., Tomaselli, G., Priori, E. C., Colnaghi, L., & Borsello, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084113 · Cited by 7 · see citing works

Authors: Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Davis, Roger J.
ORCID: Dickens, Martin
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
DOI: 10.1128/mcb.20.3.1030-1043.2000
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

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