PMID- 10414980
OWN - NLM
STAT- MEDLINE
DCOM- 19990816
LR  - 20191210
IS  - 0270-6474 (Print)
IS  - 0270-6474 (Linking)
VI  - 19
IP  - 15
DP  - 1999 Aug 1
TI  - Cloning and characterization of neuropilin-1-interacting protein: a
      PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic
      domain of neuropilin-1.
PG  - 6519-27
AB  - Neuropilin-1 (Npn-1), a receptor for semaphorin III, mediates the guidance of
      growth cones on extending neurites. The molecular mechanism of Npn-1 signaling
      remains unclear. We have used a yeast two-hybrid system to isolate a protein that
      interacts with the cytoplasmic domain of Npn-1. This Npn-1-interacting protein
      (NIP) contains a central PSD-95/Dlg/ZO-1 (PDZ) domain and a C-terminal acyl
      carrier protein domain. The physiological interaction of Npn-1 and NIP is
      supported by co-immunoprecipitation of these two proteins in extracts from a
      heterologous expression system and from a native tissue. The C-terminal three
      amino acids of Npn-1 (S-E-A-COOH), which is conserved from Xenopus to human, is
      responsible for interaction with the PDZ domain-containing C-terminal two-thirds 
      of NIP. NIP as well as Npn-1 are broadly expressed in mice as assayed by Northern
      and Western analysis. Immunohistochemistry and in situ hybridization experiments 
      revealed that NIP expression overlaps with that of Npn-1. NIP has been
      independently cloned as RGS-GAIP-interacting protein (GIPC), where it was
      identified by virtue of its interaction with the C terminus of RGS-GAIP and
      suggested to participate in clathrin-coated vesicular trafficking. We suggest
      that NIP and GIPC may participate in regulation of Npn-1-mediated signaling as a 
      molecular adapter that couples Npn-1 to membrane trafficking machinery in the
      dynamic axon growth cone.
FAU - Cai, H
AU  - Cai H
AD  - Howard Hughes Medical Institutes, The Johns Hopkins University School of
      Medicine, Baltimore, Maryland 21205, USA.
FAU - Reed, R R
AU  - Reed RR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for
      Neuroscience
JID - 8102140
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (GIPC1 protein, human)
RN  - 0 (Gipc1 protein, mouse)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Neuropeptides)
RN  - 144713-63-3 (Neuropilin-1)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence/genetics
MH  - Animals
MH  - Axons/metabolism
MH  - Carrier Proteins/*genetics/metabolism/*physiology
MH  - Cell Line
MH  - Central Nervous System/metabolism
MH  - *Cloning, Molecular
MH  - Humans
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Nerve Endings/metabolism
MH  - Nerve Tissue Proteins/*genetics/*physiology
MH  - Neuropeptides/*genetics/metabolism/*physiology
MH  - Neuropilin-1
MH  - Olfactory Pathways/metabolism
MH  - Peripheral Nerves/metabolism
MH  - Precipitin Tests
MH  - Sequence Homology, Amino Acid
PMC - PMC6782790
EDAT- 1999/07/22 00:00
MHDA- 1999/07/22 00:01
CRDT- 1999/07/22 00:00
PHST- 1999/07/22 00:00 [pubmed]
PHST- 1999/07/22 00:01 [medline]
PHST- 1999/07/22 00:00 [entrez]
PST - ppublish
SO  - J Neurosci. 1999 Aug 1;19(15):6519-27.