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

The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index, and 1 are not checked yet.

Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3

Open access

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

DOI 10.1128/mcb.20.3.1030-1043.2000PMC PMC85220

Open this paper in CoChat — free account

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.

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 · 10.1128/mcb.20.3.1030-1043.2000

Cites

71 of 72 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.

Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis
Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,273
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human
Widmann, C., Gibson, S. B., Jarpe, M. B., & Johnson, G. L. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.1.143 · Cited by 2,707
The stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
Mitogen-activated protein kinase pathways
Robinson, M. J., & Cobb, M. H. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80061-0 · Cited by 2,489
Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
Tewari, M., Quan, L. T., O’Rourke, K. M., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S., & Dixit, V. M. (1995) · Cell · doi:10.1016/0092-8674(95)90541-3 · Cited by 2,367
Caspases: Intracellular Signaling by Proteolysis
Salvesen, G. S., & Dixit, V. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80430-4 · Cited by 2,118
Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600

Flagged first, then by citations

Show all 71 references

Research works printed but not linked: 2

Ammerer G., 1994, Curr. Opin. Cell Biol., 4, 90
Sluss H. K., 1994, Mol. Cell. Biol., 14, 8376

Sorted by citations

Items 101–200 of 279

Structural Basis for Rab8a Recruitment of RILPL2 via LRRK2 Phosphorylation of Switch 2
Waschbüsch, D., Purlyte, E., Pal, P., McGrath, E., Alessi, D. R., & Khan, A. R. (2020) · Structure · doi:10.1016/j.str.2020.01.005 · Cited by 87
“Sequence numbers correspond to JIP3, the interacting partners are shown above the cartoon, and p150G refers to p150Glued.”
BackgroundInfluential
Protein Kinase C Isoforms Involved in the Transcriptional Activation of Cyclin D1 by Transforming Ha-Ras
Kampfer, S., Windegger, M., Hochholdinger, F., Schwaiger, W., Pestell, R. G., Baier, G., Grunicke, H. H., & Überall, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102047200 · Cited by 69
Arrestin-3 Binds c-Jun N-terminal Kinase 1 (JNK1) and JNK2 and Facilitates the Activation of These Ubiquitous JNK Isoforms in Cells via Scaffolding
Kook, S., Zhan, X., Kaoud, T. S., Dalby, K. N., Gurevich, V. V., & Gurevich, E. V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510412 · Cited by 74
An Organelle Gatekeeper Function for Caenorhabditis elegans UNC-16 (JIP3) at the Axon Initial Segment
Edwards, S. L., Yu, S.-C., Hoover, C. M., Phillips, B. C., Richmond, J. E., & Miller, K. G. (2013) · Genetics · doi:10.1534/genetics.112.147348 · Cited by 76
“…MAPK act in the same pathway to prevent axonal lysosome accumulation Prior studies have shown that UNC-16 and its JIP3 orthologs directly interact with multiple MAP kinase signaling proteins, including C. elegans JNK-1 (a JNK-type MAP kinase) (Ito et al. 1999; Kelkar et al. 2000; Byrd et al. 2001).”
Background
Regulation of expression and signalling modulator function of mammalian tribbles is cell-type specific
Sung, H. Y., Francis, S., Crossman, D. C., & Kiss‐Toth, E. (2005) · Immunology Letters · doi:10.1016/j.imlet.2005.11.010 · Cited by 72
Association and Regulation of Heat Shock Transcription Factor 4b with both Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Dual-Specificity Tyrosine Phosphatase DUSP26
Hu, Y., & Mivechi, N. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3282-3294.2006 · Cited by 67
JLP Associates with Kinesin Light Chain 1 through a Novel Leucine Zipper-like Domain
Nguyen, Q., Lee, C. M., Le, A., & Reddy, E. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505499200 · Cited by 62
When Worlds Collide--Trafficking in JNK
Goldstein, L. S. B. (2001) · Science · doi:10.1126/science.1059766 · Cited by 66
Sunday Driver Interacts with Two Distinct Classes of Axonal Organelles
Abe, N., Almenar‐Queralt, A., Lillo, C., Shen, Z., Lozach, J., Briggs, S. P., Williams, D. S., Goldstein, L. S. B., & Cavalli, V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035022 · Cited by 65
Regulation of Apoptotic c-Jun N-Terminal Kinase Signaling by a Stabilization-Based Feed-Forward Loop
Xu, Z., Kukekov, N. V., & Greene, L. A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.22.9949-9959.2005 · Cited by 65
“Past work indicated that UV exposure elevates endogenous JIP3 and decreases its electrophoretic mobility ( 9 ).”
Background
Genetic inhibition of JNK3 ameliorates spinal muscular atrophy
Genabai, N. K., Ahmad, S., Zhang, Z., Jiang, X., Gabaldon, C. A., & Gangwani, L. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv401 · Cited by 64
The axon guidance defect of the telencephalic commissures of the JSAP1-deficient brain was partially rescued by the transgenic expression of JIP1
Ha, H.-Y., Cho, I. H., Lee, K.-W., Lee, K.-W., Song, J.-Y., Kim, K., Yu, Y.-M., Lee, J.-K., Song, J.-S., Yang, S.-D., et al. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.09.019 · Cited by 64
Dynamic Interaction between the Dual Specificity Phosphatase MKP7 and theJNK3 Scaffold Protein β-Arrestin2
Willoughby, E. A., & Collins, M. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501926200 · Cited by 68
Co‐operative Versus Independent Transport of Different Cargoes by Kinesin‐1
Hammond, J. W., Griffin, K. M., Jih, G. T., Stuckey, J. A., & Verhey, K. J. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00722.x · Cited by 63
“Previous studies have shown that JIP1, JIP2 and JIP3 homo-oligomerize and that JIP2 can hetero-oligomerize with JIP1 and JIP3 (39,41,42).”
BackgroundMethodResultInfluential
ARL8 Relieves SKIP Autoinhibition to Enable Coupling of Lysosomes to Kinesin-1
Keren‐Kaplan, T., & Bonifacino, J. S. (2020) · Current Biology · doi:10.1016/j.cub.2020.10.071 · Cited by 59
“Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3.”
BackgroundInfluential
Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3
Cockburn, J. J. B., Hesketh, S. J., Mulhair, P. O., Thomsen, M., O’Connell, M. J., & Way, M. (2018) · Structure · doi:10.1016/j.str.2018.07.011 · Cited by 57
A JIP3-Regulated GSK3β/DCX Signaling Pathway Restricts Axon Branching
Bilimoria, P. M., de la Torre-Ubieta, L., Ikeuchi, Y., Becker, E. B. E., Reiner, O., & Bonni, A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1362-10.2010 · Cited by 56
“The JIP3associated protein kinases JNKs and focal adhesion kinase (FAK) have reported roles in axon growth (Ito et al., 1999; Kelkar et al., 2000; Takino et al., 2002; Chang et al., 2003; Rico et al., 2004; Oliva et al., 2006).”
Background
c-Jun NH2-terminal Kinase (JNK)-interacting Protein-3 (JIP3) Regulates Neuronal Axon Elongation in a Kinesin- and JNK-dependent Manner
Sun, T., Yu, N., Zhai, L., Li, N., Zhang, C., Zhou, L., Huang, Z., Jiang, X., Shen, Y., & Chen, Z.-Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464453 · Cited by 56
“JIP”ing along the axon: the complex roles of JIPs in axonal transport
Koushika, S. P. (2007) · BioEssays · doi:10.1002/bies.20695 · Cited by 56
Motor Protein Receptors
Klopfenstein, D. R., Vale, R. D., & Rogers, S. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00144-6 · Cited by 56
Scaffold Role of a Mitogen-activated Protein Kinase Phosphatase, SKRP1, for the JNK Signaling Pathway
Zama, T., Aoki, R., Kamimoto, T., Inoue, K., Ikeda, Y., & Hagiwara, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200838200 · Cited by 53
MKK7, the essential regulator of JNK signaling involved in cancer cell survival: a newly emerging anticancer therapeutic target
Park, J. G., Aziz, N., & Cho, J. Y. (2019) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835919875574 · Cited by 57
Targeting the JNK Pathway as a Therapeutic Protective Strategy for Nervous System Diseases
Bonny, C., Borsello, T., & Zine, A. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.1.57 · Cited by 54
Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases
Cason, S. E., & Holzbaur, E. L. F. (2023) · Journal of Cell Biology · doi:10.1083/jcb.202301084 · Cited by 51
“…to the brain; in contrast, the related protein JIP4 ( SPAG9 ; also known as JLP) is expressed ubiquitously (Ito et al., 1999; Jagadish et al., 2005; Kelkar et al., 2000; Platzer et al., 2019) has shown that JIP3 and JIP4 contain a structurally conserved motif in their N-termini that mediates…”
Identification of ROCK1 as an Upstream Activator of the JIP-3 to JNK Signaling Axis in Response to UVB Damage
Ongusaha, P. P., Qi, H. H., Raj, L., Kim, Y., Aaronson, S. A., Davis, R. J., Shi, Y., Liao, J. K., & Lee, S. W. (2008) · Science Signaling · doi:10.1126/scisignal.1161938 · Cited by 53
“JIP-3 is a multifunctional protein; it is a cargo adaptor protein mediating axonal transport of kinesin (5, 39, 40) and a scaffold protein for the JNK pathway (26, 41).”
Background
Protein kinases and their involvement in the cellular responses to genotoxic stress
Yang, J. J., Yu, Y., & Duerksen-Hughes, P. J. (2003) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(02)00069-8 · Cited by 53
JIP3 interacts with dynein and kinesin-1 to regulate bidirectional organelle transport
Celestino, R., Gama, J. B., Castro-Rodrigues, A. F., Barbosa, D. J., Rocha, H., d’Amico, E. A., Musacchio, A., Carvalho, A. X., Morais-Cabral, J. H., & Gassmann, R. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202110057 · Cited by 54
“…identified as a scaffolding protein that binds c-Jun N-terminal kinase (JNK) and kinesin light chain (KLC; Bowman et al., 2000; Ito et al., 1999; Kelkar et al., 2000; Verhey et al., 2001), and as the product of the sunday driver ( syd ) gene in a D. melanogaster screen for axonal transport…”
The Amyloid-β Precursor Protein Is Phosphorylated via Distinct Pathways during Differentiation, Mitosis, Stress, and Degeneration
Muresan, Z. L., & Mureşan, V. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-07-0625 · Cited by 50
“Roger Davis (University of Massachusetts Medical School, Howard Hughes Medical Institute, Worcester, MA; Kelkar et al., 2000).”
Background
A New Identity for MLK3 as an NIMA-related, Cell Cycle–regulated Kinase That Is Localized near Centrosomes and Influences Microtubule Organization
Swenson, K. I., Winkler, K. E., & Means, A. R. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-02-0115 · Cited by 49
Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates
BARDWELL, L., & SHAH, K. (2006) · Methods · doi:10.1016/j.ymeth.2006.06.008 · Cited by 46
Biological Properties of JNK3 and Its Function in Neurons, Astrocytes, Pancreatic β-Cells and Cardiovascular Cells
Nakano, R., Nakayama, T., & Sugiya, H. (2020) · Cells · doi:10.3390/cells9081802 · Cited by 48
“JNK/SAPK-associated protein 1 (JSAP-1, JIP3) is also a protein binding to JNK3 [49,50].”
Background
A Novel Dual Specificity Phosphatase SKRP1 Interacts with the MAPK Kinase MKK7 and Inactivates the JNK MAPK Pathway
Zama, T., Aoki, R., Kamimoto, T., Inoue, K., Ikeda, Y., & Hagiwara, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200837200 · Cited by 48
Regulation of Bidirectional Melanosome Transport by Organelle Bound MAP Kinase
Deacon, S. W., Nascimento, A. A. C., Serpinskaya, A. S., & Gelfand, V. I. (2005) · Current Biology · doi:10.1016/j.cub.2004.12.074 · Cited by 47
Role of the JNK-interacting protein 1/islet brain 1 in cell degeneration in Alzheimer disease and diabetes
Beeler, N., Riederer, B. M., Waeber, G., & Abderrahmani, A. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.07.006 · Cited by 51
Diverse Physiological Functions of MKK4 and MKK7 during Early Embryogenesis
Asaoka, Y., & Nishina, H. (2010) · The Journal of Biochemistry · doi:10.1093/jb/mvq098 · Cited by 46
JSAP1/JIP3 and JLP regulate kinesin-1-dependent axonal transport to prevent neuronal degeneration
Sato, T., Ishikawa, M., Mochizuki, M., Ohta, M., Ohkura, M., Nakai, J., Takamatsu, N., & Yoshioka, K. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.207 · Cited by 47
“…protein kinase-associated protein 1 (JSAP1, also known as JIP3 or Sunday Driver).4 The JIP protein family includes JIP1,5 JIP2,6 JSAP1/JIP3 (Ito et al. 1999; Kelkar et al. 2000) and JNK-associated leucine zipper protein (JLP).9 Splice variants of JLPare known as JIP4 (Kelkar et al. 2005) or SPAG9.”
Background
Alzheimers Disease - An Interactive Perspective
Heese, K., & Akatsu, H. (2006) · Current Alzheimer Research · doi:10.2174/156720506776383022 · Cited by 46
A unique set of SH3–SH3 interactions controls IB1 homodimerization
Kristensen, O., Guenat, S., Dar, I., Allaman-Pillet, N., Abderrahmani, A., Ferdaoussi, M., Roduit, R., Maurer, F., Beckmann, J. S., Kastrup, J. S., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600982 · Cited by 46
“MLK3 and MKK7, as potential partners binding to the large C-terminal part of IB1 (Kelkar et al, 2000), were assayed in the same pull-down experiments (Figure 2B).”
Background
Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators
Benoit, B., Baillet, A., & Poüs, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168375 · Cited by 45
“The related neuronal scaffolding and motor-associated protein JIP3/JSAP1 can also be phosphorylated by JNK at Thr266, Thr276, and Thr287 [120], and accumulates in the growth cone of neurites where it colocalizes with activated JNK and exocytic vesicles [121].”
Background
Use of cell-permeable peptides to prevent neuronal degeneration
Borsello, T., & Bonny, C. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.03.008 · Cited by 44
JIP3 Activates Kinesin-1 Motility to Promote Axon Elongation
Watt, D., Dixit, R., & Cavalli, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.651885 · Cited by 46
“Deletion of the KHC Binding Domain in JIP3 Has a Dominant Negative Effect—Because JIP3 can homo-oligomerize (5, 60) we next determined whether JIP3 lacking the KHC binding domain had dominant negative effects on axon morphology in a WT background.”
Background
Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions
Gindhart, J. G. (2006) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/ell002 · Cited by 42
“The SYD also provided new insights on the integration of transport and cell signalling pathways, as SYD is a scaffold protein that binds to components of the JNK signalling pathway [29, 30].”
Background
Linkers, packages and pathways: new concepts in axonal transport.
Almenar-Queralt, A., & Goldstein, L. (2001) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00248-8 · Cited by 43
Cross-talk between JIP3 and JIP1 during Glucose Deprivation
Song, J. J., & Lee, Y. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502318200 · Cited by 40
Parallel Regulation of Mitogen-activated Protein Kinase Kinase 3 (MKK3) and MKK6 in Gq-signaling Cascade
Yamauchi, J., Tsujimoto, G., Kaziro, Y., & Itoh, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011752200 · Cited by 40
Kinesin Adapter JLP Links PIKfyve to Microtubule-based Endosome-to-Trans-Golgi Network Traffic of Furin
Ikonomov, O. C., Fligger, J., Sbrissa, D., Dondapati, R., Mlak, K., Deeb, R. H., & Shisheva, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806539200 · Cited by 39
Truncation of the CNS-expressed JNK3 in a patient with a severe developmental epileptic encephalopathy
Shoichet, S. A., Duprez, L., Hagens, O., Waetzig, V., Menzel, C., Herdegen, T., Schweiger, S., Dan, B., Vamos, E., Ropers, H., et al. (2005) · Human Genetics · doi:10.1007/s00439-005-0084-y · Cited by 39
“JNK interacting protein 3 (JIP3, also known as JNK/stress activated protein kinase-associated protein 1, or JSAP1), known for its role as a JNK scaffold, exhibits predominant expression in the brain, and has particular affinity for binding to JNK3, in comparison with JNKs 1 and 2 (Ito et al. 1999; Kelkar et al. 2000).”
Background
Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin
d’Amico, E. A., Ud Din Ahmad, M., Cmentowski, V., Girbig, M., Müller, F., Wohlgemuth, S., Brockmeyer, A., Maffini, S., Janning, P., Vetter, I. R., et al. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202206131 · Cited by 34
“We only present predictions of dimers here, as there is experimental evidence for several of them that their active conformation is the dimer (Isabet et al., 2009; Kelkar et al., 2000; Lee et al., 2018; Urnavicius et al., 2018; Urnavicius et al., 2015; Wu et al., 2005).”
Isoforms of JSAP1 scaffold protein generated through alternative splicing
Ito, M., Akechi, M., Hirose, R., Ichimura, M., Takamatsu, N., Xu, P., Nakabeppu, Y., Shiba, T., Yamamoto, K.-I., & Yoshioka, K. (2000) · Gene · doi:10.1016/s0378-1119(00)00335-8 · Cited by 38
Ablation of the scaffold protein JLP causes reduced fertility in male mice
Iwanaga, A., Wang, G., Davaakhuu, G., Sato, T., Tuvshintugs, B., Shimizu, K., Takumi, K., Hayashi, M., Akashi, T., Fuse, H., et al. (2008) · Transgenic Research · doi:10.1007/s11248-008-9191-6 · Cited by 38
“JLP, which is expressed fairly ubiquitously, shares significant sequence identity with JNK/stressactivated protein kinase-associated protein 1 [JSAP1, or JNK-interacting protein 3 (JIP3)], a scaffold protein for JNK cascades (Ito et al. 1999; Ito et al. 2000; Kelkar et al. 2000 ).”
Background
Palmitoyl Acyltransferase zD17 Mediates Neuronal Responses in Acute Ischemic Brain Injury by Regulating JNK Activation in a Signaling Module
Yang, G., & Cynader, M. S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2510-11.2011 · Cited by 38
Mixed lineage kinases (MLKs): a role in dendritic cells, inflammation and immunity?
Handley, M. E., Rasaiyaah, J., Chain, B., & Katz, D. R. (2007) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2007.00531.x · Cited by 37
“Stimulation results in recruitment of JNK to the scaffold protein (Kelkar et al. 2000; Nihalani et al. 2001), and JNK recruitment coincides with decreased affinity of JIP for DLK.”
Background
Syd/JIP3 and JNK Signaling Are Required for Myonuclear Positioning and Muscle Function
Schulman, V. K., Folker, E. S., Rosen, J. N., & Baylies, M. K. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004880 · Cited by 36
“1A, purple) [40], which mediates binding to JNK/p-JNK [39] and facilitates JNKdependent phosphorylation of Syd/JIP3 [47].”
Influential
Genome-Wide Identification and Analysis of MKK and MAPK Gene Families in Brassica Species and Response to Stress in Brassica napus
Wang, Z., Wan, Y., Meng, X., Zhang, X., Yao, M., Wen-Jie, M. I. U., Zhu, D., Yuan, D., Lu, K., Li, J., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020544 · Cited by 35
The transport of Staufen2‐containing ribonucleoprotein complexes involves kinesin motor protein and is modulated by mitogen‐activated protein kinase pathway
Jeong, J., Nam, Y., Kim, S., Kim, E., Jeong, J., & Kim, H. K. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04697.x · Cited by 35
“The Sunday driver protein (JIP3/JSAP1), which is a linker protein for the kinesin-vesicular cargos such as organelles or small vesicles, is a scaffold protein of c-jun N-terminal kinase, a member of the MAP kinase group (Kelkar et al. 2000).”
Background
Repression of phospho‐JNK and infarct volume in ischemic brain of JIP1‐deficient mice
Im, J., Lee, K., Kim, M. H., Lee, S. H., Ha, H., Cho, I. J., Kim, D., Yu, M. S., Kim, J., Lee, J., et al. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10761 · Cited by 35
“Expression levels of other JNKinteracting scaffold proteins, JIP2 and JSAP1/JIP3 (Ito et al., 1999; Yasuda et al., 1999; Kelkar et al., 2000), were not altered in jip1 / mice (Fig.”
Background
Copy Number Variations in Amyotrophic Lateral Sclerosis: Piecing the Mosaic Tiles Together through a Systems Biology Approach
Morello, G., Guarnaccia, M., Spampinato, A. G., Cognata, V. L., D’Agata, V., & Cavallaro, S. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0393-x · Cited by 36
“cellular events, including growth control, apoptosis, and axonal transport [161].”
Sin1 binds to both ATF‐2 and p38 and enhances ATF‐2‐dependent transcription in an SAPK signaling pathway
Makino, C., Sano, Y., Shinagawa, T., Millar, J. B. A., & Ishii, S. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.01016.x · Cited by 34
In Vitro Development of Mouse Embryonic Stem Cells Lacking JNK/Stress-activated Protein Kinase-associated Protein 1 (JSAP1) Scaffold Protein Revealed Its Requirement during Early Embryonic Neurogenesis
Xu, P., Yoshioka, K., Yoshimura, D., Tominaga, Y., Nishioka, T., Ito, M., & Nakabeppu, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307888200 · Cited by 34
A Scaffold Protein in the c-Jun NH2-terminal Kinase Signaling Pathways Suppresses the Extracellular Signal-regulated Kinase Signaling Pathways
Kuboki, Y., Ito, M., Takamatsu, N., Yamamoto, K.-I., Shiba, T., & Yoshioka, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000403200 · Cited by 34
Identification of castration‐resistant prostate cancer‐related hub genes using weighted gene co‐expression network analysis
Cheng, Y., Li, L., Qin, Z., Li, X., & Qi, F. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15432 · Cited by 33
The scaffold protein JIP3 functions as a downstream effector of the small GTPase ARF6 to regulate neurite morphogenesis of cortical neurons
Suzuki, A., Arikawa, C., Kuwahara, Y., Itoh, K., Watanabe, M., Watanabe, H., Suzuki, T., Funakoshi, Y., Hasegawa, H., & Kanaho, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.020 · Cited by 32
“As JIP3 is specifically expressed in neurons [9], we speculated that ARF6/JIP3 signaling couples to neurite morphogenesis.”
Background
Identification of a Specific Domain Responsible for JNK2α2 Autophosphorylation
Cui, J., Holgado-Madruga, M., Su, W., Tsuiki, H., Wedegaertner, P., & Wong, A. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412165200 · Cited by 31
JIP3 links lysosome transport to regulation of multiple components of the axonal cytoskeleton
Rafiq, N. M., Lyons, L. L., Gowrishankar, S., Camilli, P. V. D., & Ferguson, S. M. (2022) · Communications Biology · doi:10.1038/s42003-021-02945-x · Cited by 30
“In addition to interactions with motors, JIP3 (and JIP4) also intersect with signaling in the JNK pathway by acting as a scaffold that regulates the subcellular position and activity of DLK and JNK (Drerup and Nechiporuk, 2013; Ghosh et al., 2011; Kelkar et al., 2000; Kulkarni et al., 2019).”
Background
Podocyte Injury Induces Nuclear Translocation of WTIP via Microtubule-dependent Transport
Kim, J. H., Konieczkowski, M., Mukherjee, A., Schechtman, S., Khan, S., Schelling, J. R., Ross, M. D., Bruggeman, L. A., & Sedor, J. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061671 · Cited by 30
Scaffold protein JSAP1 is transported to growth cones of neurites independent of JNK signaling pathways in PC12h cells
Sato, S., Ito, M., Ito, T., & Yoshioka, K. (2004) · Gene · doi:10.1016/j.gene.2003.12.034 · Cited by 29
Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif
Vilela, F., Velours, C., Chenon, M., Nicaise, M., Campanacci, V., Thureau, A., Pylypenko, O., Andréani, J., Llinas, P., & Ménétrey, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-52537-3 · Cited by 26
Identification of a Novel Actin-Binding Domain within the Rho Guanine Nucleotide Exchange Factor TEM4
Mitin, N., Rossman, K. L., & Der, C. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041876 · Cited by 29
“Interestingly, while the C-terminus of TEM4 was not required for subcellular localization, it is homologous to a region found in JSAP-1/JIP-3, a known scaffold for the c-Jun N-terminal kinase pathway [58,59].”
Background
JIP1 regulates neuronal apoptosis in response to stress
Dong, Z., Zhou, L., Villar, K. D., Ghanevati, M., Tashjian, V. S., & Miller, C. A. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.10.039 · Cited by 28
Detailed gene copy number and RNA expression analysis of the 17q12–23 region in primary breast cancers
Willis, S. N., Hutchins, A., Hammet, F., Ciciulla, J., Soo, W. K., White, D. J., van der Spek, P. J., Henderson, M. A., Gish, K., Venter, D. J., et al. (2003) · Genes Chromosomes and Cancer · doi:10.1002/gcc.10138 · Cited by 28
“The JIP3 proteins are molecular scaffolds believed to increase MLK3-induced JNK activation, thereby impacting on MAPK pathway signaling, with consequent widespread effects on morphogenesis, mitogenesis, and apoptosis (Kelkar et al., 2000).”
Background
Toll-like receptor pathway gene expression is associated with human immunodeficiency virus–associated neurodegeneration
Salaria, S., Badkoobehi, H., Rockenstein, E. M., Crews, L. A., Chana, G., Masliah, E., Everall, I., & the HNRC Group (2007) · Journal of NeuroVirology · doi:10.1080/13550280701558616 · Cited by 27
“However, it is unclear whether this change in gene expression relates directly to neurodegenerative effects or is in an attempt to rectify MAPK8IP3/JIP3 protein levels, which has been observed in the neuronal cytoplasm and growth cones of developing dendrites ( Kelkar et al, 2000 ).”
Background
Formin-induced actin cables are required for polarized recruitment of the Ste5 scaffold and high level activation of MAPK Fus3
Qi, M., & Elion, E. A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02418 · Cited by 27
“MAPK scaffolds can be asymmetrically enriched at plasma membrane sites, suggesting their localization may be sensitive to spatial cues of cell polarity and they, in turn, may influence cell polarity (Mahanty et al., 1999; Kelkar et al., 2000; Muller et al., 2001; Ge et al., 2003).”
Background
Activation of ASK1, downstream MAPKK and MAPK isoforms during cardiac ischaemia
Harding, S. J., Browne, G. J., Miller, B. W., Prigent, S. A., & Dickens, M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.06.005 · Cited by 26
DUSP1 regulates apoptosis and cell migration, but not the JIP1-protected cytokine response, during Respiratory Syncytial Virus and Sendai Virus infection
Robitaille, A. C., Caron, E., Zucchini, N., Mukawera, E., Adam, D., Mariani, M. K., Gélinas, A., Fortin, A., Brochiero, E., & Grandvaux, N. (2017) · Scientific Reports · doi:10.1038/s41598-017-17689-0 · Cited by 26
Expression of JNK cascade scaffold protein JSAP1 in the mouse nervous system
Akechi, M., Ito, M., Uemura, K., Takamatsu, N., Yamashita, S., Uchiyama, K., Yoshioka, K., & Shiba, T. (2001) · Neuroscience Research · doi:10.1016/s0168-0102(01)00194-8 · Cited by 26
Identification and Analysis of a Novel Dimerization Domain Shared by Various Members of c-Jun N-terminal Kinase (JNK) Scaffold Proteins
Cohen‐Katsenelson, K., Wasserman, T., Darlyuk‐Saadon, I., Rabner, A., Glaser, F., & Aronheim, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422055 · Cited by 24
Sperm associated antigen 9 (SPAG9): a new member of c-Jun NH2-terminal kinase (JNK) interacting protein exclusively expressed in testis
Jagadish, N., Rana, R., Mishra, D., Kumar, M., & Suri, A. (2005) · The Keio Journal of Medicine · doi:10.2302/kjm.54.66 · Cited by 25
Reverse Two-hybrid Screening Identifies Residues of JNK Required for Interaction with the Kinase Interaction Motif of JNK-interacting Protein-1
Barr, R. K., Hopkins, R. M., Watt, P. M., & Bogoyevitch, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405900200 · Cited by 25
Differential regulation of M3/6 (DUSP8) signaling complexes in response to arsenite-induced oxidative stress
Oehrl, W., Cotsiki, M., & Panayotou, G. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.010 · Cited by 25
The WW domain of the scaffolding protein IQGAP1 is neither necessary nor sufficient for binding to the MAPKs ERK1 and ERK2
Bardwell, A. J., Lagunes, L., Zebarjedi, R., & Bardwell, L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767087 · Cited by 24
Intrinsic disorder in proteins associated with oxidative stress-induced JNK signaling
Gehi, B. R., Gadhave, K., Uversky, V. N., & Giri, R. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04230-4 · Cited by 25
“JIP3 binds to the MLK3-MKK7-JNK signaling module and activates JNK signaling [110].”
Background
Positive regulation of ASK1-mediated c-Jun NH2-terminal kinase signaling pathway by the WD-repeat protein Gemin5
Kim, E. K., Noh, K. T., Yoon, J.-H., Cho, J.-H., Yoon, K.-W., Dreyfuss, G., & Choi, E.-J. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402157 · Cited by 23
The scaffold protein JSAP1 regulates proliferation and differentiation of cerebellar granule cell precursors by modulating JNK signaling
Sato, T., Torashima, T., Sugihara, K., Hirai, H., Asano, M., & Yoshioka, K. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.08.003 · Cited by 21
Pre-synaptic TrkB in basolateral amygdala neurons mediates BDNF signaling transmission in memory extinction
Li, Y., Wang, D., Li, Y., Chu, H., Zhang, L., Hou, M., Jiang, X., Chen, Z.-Y., Su, B., & Sun, T. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.302 · Cited by 20
Emerging role of the Jun N‐terminal kinase interactome in human health
Guo, X., An, S., Yang, Y., Liu, Y., Hao, Q., Tang, T., & Xu, T. (2018) · Cell Biology International · doi:10.1002/cbin.10948 · Cited by 19
“The third member of JIP family, JIP3 (also referred to as JSAP1), is structurally unrelated to JIP1/2 (Ito et al., 1999; Kelkar et al., 2000) and is abundantly expressed in the brain and nervous system (Ito et al., 1999; Yasuda et al., 1999; Akechi et al., 2001).”
Background
The assembly of POSH-JNK regulates Xenopus anterior neural development
Kim, G., Park, E., & Han, J. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.07.033 · Cited by 19
“…CrkII (Girardin and Yaniv, 2001), Filamin (Marti et al., 1997), IKAP (Holmberg et al., 2002), JNK interacting proteins (JIPs) (Ito et al., 1999; Kelkar et al., 2000; Lee et al., 2002; Whitmarsh et al., 1998; Yasuda et al., 1999), SKRP1/MKPX phosphatases (Chen et al., 2002; Zama et al., 2002),…”
Background
Regulation of stress-associated scaffold proteins JIP1 and JIP3 on the c-Jun NH2-terminal kinase in ischemia–reperfusion
Xu, B., Zhou, Y., Karmin, O., Choy, P. C., Pierce, G. N., & Siow, Y. L. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y10-088 · Cited by 18
“JIP1 is clearly distinct from JIP3 in structure (Whitmarsh et al. 1998; Ito et al. 2000; Kelkar et al. 2000).”
Background
Disassembly of the JIP1/JNK molecular scaffold by caspase-3-mediated cleavage of JIP1 during apoptosis
Vaishnav, M., MacFarlane, M., & Dickens, M. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.01.011 · Cited by 18
“Thus the JIP proteins are able to bind MLK3, MKK7 and JNK in a manner which may facilitate JNK signalling and activation [32,33,39,40].”
BackgroundInfluential
Effects of JIP3 on epileptic seizures: Evidence from temporal lobe epilepsy patients, kainic-induced acute seizures and pentylenetetrazole-induced kindled seizures
Wang, Z., Chen, Y., Lu, Y., Chen, X., Cheng, L., Mi, X., Xu, X. Y., Deng, W., Zhang, Y., Wang, N., et al. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.05.008 · Cited by 18
Impaired activation of AP-1 and altered expression of constituent proteins in rat adrenal during ageing
Medicherla, R., Leers‐Sucheta, S., Luo, Y., & Azhar, S. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00258-5 · Cited by 18
Differential effects of ischemia and reperfusion on c-Jun N-terminal kinase isoform protein and activity
Shackelford, D. A., & Yeh, R. Y. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00245-5 · Cited by 18
Discovering autoinhibition as a design principle for the control of biological mechanisms
Bollhagen, A., & Bechtel, W. (2022) · Studies in History and Philosophy of Science Part A · doi:10.1016/j.shpsa.2022.08.008 · Cited by 17
Doublecortin and JIP3 are neural-specific counteracting regulators of dynein-mediated retrograde trafficking
(2022) · doi:10.7554/elife.82218 · Cited by 17
The Scaffold Protein c-Jun NH2-Terminal Kinase-associated Leucine Zipper Protein Regulates Cell Migration through Interaction with the G Protein G 13
Davaakhuu, G., Tuvshintugs, B., Endo, Y., Takino, T., Sato, H., Murakami, S., & Yoshioka, K. (2008) · The Journal of Biochemistry · doi:10.1093/jb/mvn123 · Cited by 17
Phosphorylation‐dependent binding of human transcription factor MOK2 to lamin A/C
Harper, M., Tillit, J., Kress, M., & Ernoult‐Lange, M. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07032.x · Cited by 17
The JNK signalling transduction pathway in the brain
Antoniou, X. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/528 · Cited by 16
Label-free quantitative proteomics of rat hypothalamus under fever induced by LPS and PGE2
Firmino, M., Weis, S. N., de Souza, J. M. F., Gomes, B. R. B., Mól, A. R., Mortari, M. R., de Souza, G. E. P., Coca, G. C., Williams, T. C. R., Fontes, W., et al. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.07.018 · Cited by 16
Signal Transduction Cross Talk Mediated by Jun N-Terminal Kinase-Interacting Protein and Insulin Receptor Substrate Scaffold Protein Complexes
Standen, C. L., Kennedy, N. J., Flavell, R. A., & Davis, R. J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00155-09 · Cited by 15
“(Sigma), JIP1 and JIP2 (31), JIP3 (15), JIP4 (16), JNK1/2 (Pharmingen), phos-”
Influential
Neural-specific ablation of the scaffold protein JSAP1 in mice causes neonatal death
Iwanaga, A., Sato, T., Sugihara, K., Hirao, A., Takakura, N., Okamoto, H., Asano, M., & Yoshioka, K. (2009) · Kanazawa University Repository for Academic Resources (DSpace) (Kanazawa University) · Cited by 14
A subdomain of MEKK1 that is critical for binding to MKK4
Tu, Z., Mooney, S. M., & Lee, F. S. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00056-6 · Cited by 14

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

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

Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3

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