Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors

Takuya Takahashi; Alyson Fournier; Fumio Nakamura; Li Hsien Wang; Yasunori Murakami; Robert G. Kalb; Hajime Fujisawa; Stephen M. Strittmatter

doi:10.1016/S0092-8674(00)80062-8

Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors

Takuya Takahashi, Alyson Fournier, Fumio Nakamura, Li Hsien Wang, Yasunori Murakami, Robert G. Kalb, Hajime Fujisawa, Stephen M. Strittmatter^*

^*Corresponding author for this work

Neurology

Research output: Contribution to journal › Article › peer-review

661 Scopus citations

Abstract

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 I 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.

Original language	English (US)
Pages (from-to)	59-69
Number of pages	11
Journal	Cell
Volume	99
Issue number	1
DOIs	https://doi.org/10.1016/S0092-8674(00)80062-8
State	Published - Oct 1 1999

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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@article{df954cdf9b094999b385d2f800fb284c,

title = "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors",

abstract = "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 I 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.",

author = "Takuya Takahashi and Alyson Fournier and Fumio Nakamura and Wang, {Li Hsien} and Yasunori Murakami and Kalb, {Robert G.} and Hajime Fujisawa and Strittmatter, {Stephen M.}",

note = "Funding Information: We thank M. Tessier-Lavigne for providing the AP-Sema3F expression vector. This work was supported by grants to S. M. S. from the National Institutes of Health and the American Paralysis Association. S. M. S. is a John Merck Scholar in the Biology of Developmental Disorders in Children and an Investigator of the Patrick and Catherine Weldon Donaghue Medical Research Foundation. A. F. is supported by a FCAR research fellowship. F. N. is supported by a research fellowship from the Spinal Cord Research Fund of the Paralyzed Veterans of America.",

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AU - Takahashi, Takuya

AU - Fournier, Alyson

AU - Nakamura, Fumio

AU - Wang, Li Hsien

AU - Murakami, Yasunori

AU - Kalb, Robert G.

AU - Fujisawa, Hajime

AU - Strittmatter, Stephen M.

N1 - Funding Information: We thank M. Tessier-Lavigne for providing the AP-Sema3F expression vector. This work was supported by grants to S. M. S. from the National Institutes of Health and the American Paralysis Association. S. M. S. is a John Merck Scholar in the Biology of Developmental Disorders in Children and an Investigator of the Patrick and Catherine Weldon Donaghue Medical Research Foundation. A. F. is supported by a FCAR research fellowship. F. N. is supported by a research fellowship from the Spinal Cord Research Fund of the Paralyzed Veterans of America.

PY - 1999/10/1

Y1 - 1999/10/1

N2 - 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 I 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.

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 I 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.

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