PMID- 10318831
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20191210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 20
DP  - 1999 May 14
TI  - A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF.
PG  - 14137-46
AB  - M-SemF is a membrane-associated, neurally enriched member of the semaphorin
      family of axon guidance signals. We considered whether the cytoplasmic domain of 
      M-SemF might possess a signaling function and/or might control the distribution
      of M-SemF on the cell surface. We identify a PDZ-containing neural protein as an 
      M-SemF cytoplasmic domain-associated protein (SEMCAP-1). SEMCAP-2 is a closely
      related nonneuronal protein. SEMCAP-1 has recently also been identified as GIPC, 
      by virtue of its interaction with the RGS protein GAIP in vitro (De Vries, L.,
      Lou, X., Zhao, G., Zheng, B., and Farquhar, M. G. (1998) Proc. Natl. Acad. Sci.
      U. S. A. 95, 12340-12345). Expression studies support the notion that
      SEMCAP-1(GIPC) interacts with M-SemF, but not GAIP, in brain. Lung SEMCAP-2 and
      SEMCAP-1(GIPC) are potential partners for both GAIP and M-SemF. The protein
      interaction requires the single PDZ domain of SEMCAP-1(GIPC) and the
      carboxyl-terminal four residues of M-SemF, ESSV. While SEMCAP-1(GIPC) also
      interacts with SemC, it does not interact with other proteins containing a class 
      I PDZ binding motif, nor does M-SemF interact with other class I PDZ proteins.
      Co-expression of SEMCAP-1(GIPC) induces the redistribution of dispersed M-SemF
      into detergent-resistant aggregates in HEK293 cells. Thus, SEMCAP-1(GIPC) appears
      to regulate the subcellular distribution of M-SemF in brain, and SEMCAPs could
      link M-SemF to G protein signal transduction pathways.
FAU - Wang, L H
AU  - Wang LH
AD  - Department of Neurology, Yale University School of Medicine, New Haven,
      Connecticut 06520, USA.
FAU - Kalb, R G
AU  - Kalb RG
FAU - Strittmatter, S M
AU  - Strittmatter SM
LA  - eng
GR  - NS29837/NS/NINDS NIH HHS/United States
GR  - NS33020/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
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 (GIPC1 protein, human)
RN  - 0 (Gipc1 protein, mouse)
RN  - 0 (Gipc2 protein, mouse)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Growth Factors)
RN  - 0 (Neuropeptides)
RN  - 0 (Phosphoproteins)
RN  - 0 (RGS Proteins)
RN  - 0 (Sema4c protein, mouse)
RN  - 0 (Semaphorins)
RN  - 0 (regulator of G-protein signalling 19)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/metabolism
MH  - Carrier Proteins/*metabolism
MH  - Cell Line
MH  - Fluorescent Antibody Technique, Indirect
MH  - Humans
MH  - Lung/metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nerve Growth Factors/*metabolism
MH  - Neuropeptides/*metabolism
MH  - Phosphoproteins/metabolism
MH  - RGS Proteins
MH  - Rabbits
MH  - *Semaphorins
MH  - Signal Transduction
EDAT- 1999/05/13 00:00
MHDA- 1999/05/13 00:01
CRDT- 1999/05/13 00:00
PHST- 1999/05/13 00:00 [pubmed]
PHST- 1999/05/13 00:01 [medline]
PHST- 1999/05/13 00:00 [entrez]
AID - 10.1074/jbc.274.20.14137 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 14;274(20):14137-46. doi: 10.1074/jbc.274.20.14137.