PMID- 10520994
OWN - NLM
STAT- MEDLINE
DCOM- 19991025
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 99
IP  - 1
DP  - 1999 Oct 1
TI  - Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.
PG  - 59-69
AB  - Class 1 and 3 semaphorins repulse axons but bind to different cell surface
      proteins. We find that the two known semaphorin-binding proteins, plexin 1 (Plex 
      1) and neuropilin-1 (NP-1), form a stable complex. Plex 1 alone does not bind
      semaphorin-3A (Sema3A), but the NP-1/Plex 1 complex has a higher affinity for
      Sema3A than does NP-1 alone. While Sema3A binding to NP-1 does not alter
      nonneuronal cell morphology, Sema3A interaction with NP-1/Plex 1 complexes
      induces adherent cells to round up. Expression of a dominant-negative Plex 1 in
      sensory neurons blocks Sema3A-induced growth cone collapse. Sema3A treatment
      leads to the redistribution of growth cone NP-1 and plexin into clusters. Thus,
      physiologic Sema3A receptors consist of NP-1/plexin complexes.
FAU - Takahashi, T
AU  - Takahashi T
AD  - Department of Neurology, Yale University School of Medicine, New Haven,
      Connecticut 06510, USA.
FAU - Fournier, A
AU  - Fournier A
FAU - Nakamura, F
AU  - Nakamura F
FAU - Wang, L H
AU  - Wang LH
FAU - Murakami, Y
AU  - Murakami Y
FAU - Kalb, R G
AU  - Kalb RG
FAU - Fujisawa, H
AU  - Fujisawa H
FAU - Strittmatter, S M
AU  - Strittmatter SM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (PLXNA1 protein, human)
RN  - 0 (Receptors, Cell Surface)
RN  - 144713-63-3 (Neuropilin-1)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Ganglia, Spinal/cytology
MH  - Gene Expression/physiology
MH  - Growth Cones/chemistry/metabolism
MH  - Humans
MH  - Kidney/cytology
MH  - Multigene Family
MH  - Nerve Tissue Proteins/chemistry/genetics/*metabolism
MH  - Neurons/chemistry/cytology/ultrastructure
MH  - Neuropilin-1
MH  - Protein Binding/physiology
MH  - Protein Structure, Tertiary
MH  - Receptors, Cell Surface/chemistry/genetics/*metabolism
MH  - Signal Transduction/physiology
MH  - Solubility
MH  - Transfection
EDAT- 1999/10/16 00:00
MHDA- 1999/10/16 00:01
CRDT- 1999/10/16 00:00
PHST- 1999/10/16 00:00 [pubmed]
PHST- 1999/10/16 00:01 [medline]
PHST- 1999/10/16 00:00 [entrez]
AID - S0092-8674(00)80062-8 [pii]
AID - 10.1016/s0092-8674(00)80062-8 [doi]
PST - ppublish
SO  - Cell. 1999 Oct 1;99(1):59-69. doi: 10.1016/s0092-8674(00)80062-8.