Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity
Neuropilins bind secreted members of the semaphorin family of proteins. Neuropilin-1 is a receptor for Sema III. Here, we show that neuropilin-2 is a receptor for the secreted semaphorin Sema IV and acts selectively to mediate repulsive guidance events in discrete populations of neurons. neuropilin-...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 1998-11, Vol.21 (5), p.1079-1092 |
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| container_title | Neuron (Cambridge, Mass.) |
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| creator | Giger, R J Urquhart, E R Gillespie, S K Levengood, D V Ginty, D D Kolodkin, A L |
| description | Neuropilins bind secreted members of the semaphorin family of proteins. Neuropilin-1 is a receptor for Sema III. Here, we show that neuropilin-2 is a receptor for the secreted semaphorin Sema IV and acts selectively to mediate repulsive guidance events in discrete populations of neurons. neuropilin-2 and semaIV are expressed in strikingly complementary patterns during neurodevelopment. The extracellular complement-binding (CUB) and coagulation factor domains of neuropilin-2 confer specificity to the Sema IV repulsive response, and these domains of neuropilin-1 are necessary and sufficient for binding of the Sema III semaphorin (sema) domain. The coagulation factor domains alone are necessary and sufficient for binding of the Sema III immunoglobulin- (Ig-) basic domain and the unrelated ligand, vascular endothelial growth factor (VEGF). Lastly, neuropilin-1 can homomultimerize and form heteromultimers with neuropilin-2. These results provide insight into how interactions between neuropilins and secreted semaphorins function to coordinate repulsive axon guidance during neurodevelopment. |
| doi_str_mv | 10.1016/S0896-6273(00)80625-X |
| format | Article |
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Neuropilin-1 is a receptor for Sema III. Here, we show that neuropilin-2 is a receptor for the secreted semaphorin Sema IV and acts selectively to mediate repulsive guidance events in discrete populations of neurons. neuropilin-2 and semaIV are expressed in strikingly complementary patterns during neurodevelopment. The extracellular complement-binding (CUB) and coagulation factor domains of neuropilin-2 confer specificity to the Sema IV repulsive response, and these domains of neuropilin-1 are necessary and sufficient for binding of the Sema III semaphorin (sema) domain. The coagulation factor domains alone are necessary and sufficient for binding of the Sema III immunoglobulin- (Ig-) basic domain and the unrelated ligand, vascular endothelial growth factor (VEGF). Lastly, neuropilin-1 can homomultimerize and form heteromultimers with neuropilin-2. 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These results provide insight into how interactions between neuropilins and secreted semaphorins function to coordinate repulsive axon guidance during neurodevelopment.</description><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Coculture Techniques</subject><subject>Embryo, Mammalian</subject><subject>Ganglia, Spinal - cytology</subject><subject>Ganglia, Sympathetic - cytology</subject><subject>Glycoproteins - physiology</subject><subject>Humans</subject><subject>Nerve Growth Factors - metabolism</subject><subject>Nerve Growth Factors - physiology</subject><subject>Nerve Tissue Proteins - biosynthesis</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Neurons - metabolism</subject><subject>neuropilin 2</subject><subject>Neuropilin-1</subject><subject>Rats</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - physiology</subject><subject>semaphorin IV</subject><subject>Semaphorin-3A</subject><subject>Superior Cervical Ganglion - chemistry</subject><subject>Superior Cervical Ganglion - cytology</subject><issn>0896-6273</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctOwzAQRb0AlVL4hEpeIVgE7Di2Y3YI8ahUwYKHurMcx6ZGaRxsZ9G_J32oYsdiZqTRvXekOQBMMbrGCLObN1QKlrGck0uErkrEcpotjsD4sD4BpzF-I4QLKvAIjERJWcHIGKQX0wffuca1WQ5dhAoGo02XfIB2qGhWqlv64Fo4-7yFro3ua5mGmTxMSwNjCr1OfVANrFQc_N7-CehbnZxvoWprGDujnXXapfUZOLaqieZ8Pyfg4_Hh_f45m78-ze7v5pkuSJGyvCCK1HVFa1pgXHNcKqG51gJrwa2thk5VXZWEI8VFji3NrdC1qBRhPFeUTMDFLrcL_qc3McmVi9o0jWqN76NkApUUc_avEPMCoaLkg5DuhDr4GIOxsgtupcJaYiQ3KOQWhdz8XCIktyjkYvBN9wf6amXqg2vPgfwCeYiItg</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Giger, R J</creator><creator>Urquhart, E R</creator><creator>Gillespie, S K</creator><creator>Levengood, D V</creator><creator>Ginty, D D</creator><creator>Kolodkin, A L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity</title><author>Giger, R J ; Urquhart, E R ; Gillespie, S K ; Levengood, D V ; Ginty, D D ; Kolodkin, A L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-243a3ddb5d5411d718a9c7cc91c97ffbc975adb8370a7921f52f9cd9ba3672a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Coculture Techniques</topic><topic>Embryo, Mammalian</topic><topic>Ganglia, Spinal - cytology</topic><topic>Ganglia, Sympathetic - cytology</topic><topic>Glycoproteins - physiology</topic><topic>Humans</topic><topic>Nerve Growth Factors - metabolism</topic><topic>Nerve Growth Factors - physiology</topic><topic>Nerve Tissue Proteins - biosynthesis</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Neurons - metabolism</topic><topic>neuropilin 2</topic><topic>Neuropilin-1</topic><topic>Rats</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - physiology</topic><topic>semaphorin IV</topic><topic>Semaphorin-3A</topic><topic>Superior Cervical Ganglion - chemistry</topic><topic>Superior Cervical Ganglion - cytology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Giger, R J</creatorcontrib><creatorcontrib>Urquhart, E R</creatorcontrib><creatorcontrib>Gillespie, S K</creatorcontrib><creatorcontrib>Levengood, D V</creatorcontrib><creatorcontrib>Ginty, D D</creatorcontrib><creatorcontrib>Kolodkin, A L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuron (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giger, R J</au><au>Urquhart, E R</au><au>Gillespie, S K</au><au>Levengood, D V</au><au>Ginty, D D</au><au>Kolodkin, A L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity</atitle><jtitle>Neuron (Cambridge, Mass.)</jtitle><addtitle>Neuron</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>21</volume><issue>5</issue><spage>1079</spage><epage>1092</epage><pages>1079-1092</pages><issn>0896-6273</issn><abstract>Neuropilins bind secreted members of the semaphorin family of proteins. Neuropilin-1 is a receptor for Sema III. Here, we show that neuropilin-2 is a receptor for the secreted semaphorin Sema IV and acts selectively to mediate repulsive guidance events in discrete populations of neurons. neuropilin-2 and semaIV are expressed in strikingly complementary patterns during neurodevelopment. The extracellular complement-binding (CUB) and coagulation factor domains of neuropilin-2 confer specificity to the Sema IV repulsive response, and these domains of neuropilin-1 are necessary and sufficient for binding of the Sema III semaphorin (sema) domain. The coagulation factor domains alone are necessary and sufficient for binding of the Sema III immunoglobulin- (Ig-) basic domain and the unrelated ligand, vascular endothelial growth factor (VEGF). Lastly, neuropilin-1 can homomultimerize and form heteromultimers with neuropilin-2. 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| source | MEDLINE; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Cells, Cultured Coculture Techniques Embryo, Mammalian Ganglia, Spinal - cytology Ganglia, Sympathetic - cytology Glycoproteins - physiology Humans Nerve Growth Factors - metabolism Nerve Growth Factors - physiology Nerve Tissue Proteins - biosynthesis Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Neurons - metabolism neuropilin 2 Neuropilin-1 Rats Receptors, Cell Surface - chemistry Receptors, Cell Surface - physiology semaphorin IV Semaphorin-3A Superior Cervical Ganglion - chemistry Superior Cervical Ganglion - cytology |
| title | Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity |
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