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Cited by 126Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesAxon Guidance and Neuronal Signaling

Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons

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Meyer, Debra, Liu, Albert, Margolis, Ben·1999·Journal of Biological Chemistry
DOI 10.1074/jbc.274.49.35113
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Abstract

c-Jun amino-terminal kinase (JNK) interacting protein-1 (JIP-1) was originally identified as a cytoplasmic inhibitor of JNK. More recently, JIP-1 was proposed to function as a scaffold protein by complexing specific components of the JNK signaling pathway, namely JNK, mitogen-activated protein kinase kinase 7, and mixed lineage kinase 3. We have identified the human homologue of JIP-1 that contains a phosphotyrosine binding (PTB) domain in addition to a JNK binding domain and an Src homology 3 domain. To identify binding targets for the hJIP-1 PTB domain, a mouse embryo cDNA library was screened using the yeast two-hybrid system. One clone encoded a 191-amino acid region of the neuronal protein rhoGEF, an exchange factor for rhoA. Overexpression of rhoGEF promotes cytoskeletal rearrangement and cell rounding in NIE-115 neuronal cells. The interaction of JIP-1 with rhoGEF was confirmed by coimmunoprecipitation of these proteins from lysates of transiently transfected HEK 293 cells. Using glutathione S-transferase rhoGEF fusion proteins containing deletion or point mutations, we identified a putative PTB binding site within rhoGEF. This binding site does not contain tyrosine, indicating that the JIP PTB domain, like that of Xll alpha and Numb, binds independently of phosphotyrosine. Several forms of endogenous JIP-1 protein can be detected in neuronal cell lines. Indirect immunofluorescence analysis localized endogenous JIP-1 to the tip of the neurites in differentiated NIE-115 and PC12 cells. The interaction of JIP-1 with rhoGEF and its subcellular localization suggests that JIP-1 may function to specifically localize a signaling complex in neuronal cells.

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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 Meyer et al. 1999

  • JIP-1 and JIP-2 interact with rhoGEF and with the cell surface receptor for Reelin, ApoER2.

    “JIP-1 and JIP-2 have additionally been found to interact with rhoGEF (Meyer et al. 1999) and with the cell surface receptor for Reelin, ApoER2 (Stockinger et al. 2000).”

    From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Meyer et al. 1999

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Authors
Meyer, D., Liu, A., & Margolis, B.
Affiliations
Howard Hughes Medical Institute (US)
Corresponding author
Margolis, Ben
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-12
Volume
274
Issue
49
Pages
35113-35118
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.274.49.35113
OpenAlex
W2045929031
Cited by
126
References
37
Citations by year
2026: 1 · 2025: 1 · 2023: 1 · 2022: 3 · 2021: 1 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 6 · 2013: 1 · 2012: 2
FWCI
4.82
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
Keywords
JIP1, RhoA, phosphotyrosine binding domain, protein-protein interaction, scaffold proteins, JNK signaling, neuronal differentiation, cytoskeletal rearrangement, PC12 cells, MAPKAPK7, MKK3
MeSH terms
Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Cell Line, Humans, Molecular Sequence Data, Neurons, Precipitin Tests, Tyrosine, Immunoblotting, Signal Transduction, Sequence Homology, Amino Acid, Fluorescent Antibody Technique, Indirect, Guanine Nucleotide Exchange Factors, Two-Hybrid System Techniques, Adaptor Proteins, Signal Transducing, Mice, Rho Guanine Nucleotide Exchange Factors

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