PMID- 10574993
OWN - NLM
STAT- MEDLINE
DCOM- 20000203
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 49
DP  - 1999 Dec 3
TI  - Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF
      and its localization in differentiated neurons.
PG  - 35113-8
AB  - 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.
FAU - Meyer, D
AU  - Meyer D
AD  - Howard Hughes Medical Institute, University of Michigan Medical School, Ann
      Arbor, Michigan 48109, USA.
FAU - Liu, A
AU  - Liu A
FAU - Margolis, B
AU  - Margolis B
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (MAPK8IP1 protein, human)
RN  - 0 (Mapk8ip protein, mouse)
RN  - 0 (Rho Guanine Nucleotide Exchange Factors)
RN  - 42HK56048U (Tyrosine)
SB  - IM
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Carrier Proteins/biosynthesis/*metabolism
MH  - Cell Line
MH  - Fluorescent Antibody Technique, Indirect
MH  - Guanine Nucleotide Exchange Factors/biosynthesis/*metabolism
MH  - Humans
MH  - Immunoblotting
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neurons/*metabolism
MH  - Precipitin Tests
MH  - Rho Guanine Nucleotide Exchange Factors
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Two-Hybrid System Techniques
MH  - Tyrosine/metabolism
EDAT- 1999/11/27 00:00
MHDA- 1999/11/27 00:01
CRDT- 1999/11/27 00:00
PHST- 1999/11/27 00:00 [pubmed]
PHST- 1999/11/27 00:01 [medline]
PHST- 1999/11/27 00:00 [entrez]
AID - 10.1074/jbc.274.49.35113 [doi]
AID - S0021-9258(19)53436-6 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 3;274(49):35113-8. doi: 10.1074/jbc.274.49.35113.