Netrin-G1: a Novel Glycosyl Phosphatidylinositol-Linked Mammalian Netrin That Is Functionally Divergent from Classical Netrins
UNC-6/netrins compose a small phylogenetically conserved family of proteins that act as axon guidance cues. With a signal sequence trap method, we isolated a cDNA encoding a novel member of the UNC-6/netrin family, which we named netrin-G1. Unlike classical netrins, netrin-G1 consists of at least si...
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| Veröffentlicht in: | The Journal of neuroscience 2000-09, Vol.20 (17), p.6540-6550 |
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| container_title | The Journal of neuroscience |
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| creator | Nakashiba, Toshiaki Ikeda, Toshio Nishimura, Sachiko Tashiro, Kei Honjo, Tasuku Culotti, Joseph G Itohara, Shigeyoshi |
| description | UNC-6/netrins compose a small phylogenetically conserved family of proteins that act as axon guidance cues. With a signal sequence trap method, we isolated a cDNA encoding a novel member of the UNC-6/netrin family, which we named netrin-G1. Unlike classical netrins, netrin-G1 consists of at least six isoforms of which five were predominantly anchored to the plasma membrane via glycosyl phosphatidyl-inositol linkages. Netrin-G1 transcripts were first detected in midbrain and hindbrain regions by embryonic day 12 and reached highest levels at perinatal stages in various brain regions, including olfactory bulb mitral cells, thalamus, and deep cerebellar nuclei. Its expression was primarily restricted to the CNS. Interestingly, netrin-G1 proteins did not show appreciable affinity to any netrin receptor examined. Unlike netrin-1, a secreted form of netrin-G1 consistently failed to attract circumferentially growing axons from the cerebellar plate. Our findings suggest that netrin-G1 and its putative receptors have coevolved independently from the classical netrins. The expression pattern of netrin-G1 and its predicted neuronal membrane localization suggest it may also have novel signaling functions in nervous system development. |
| doi_str_mv | 10.1523/jneurosci.20-17-06540.2000 |
| format | Article |
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With a signal sequence trap method, we isolated a cDNA encoding a novel member of the UNC-6/netrin family, which we named netrin-G1. Unlike classical netrins, netrin-G1 consists of at least six isoforms of which five were predominantly anchored to the plasma membrane via glycosyl phosphatidyl-inositol linkages. Netrin-G1 transcripts were first detected in midbrain and hindbrain regions by embryonic day 12 and reached highest levels at perinatal stages in various brain regions, including olfactory bulb mitral cells, thalamus, and deep cerebellar nuclei. Its expression was primarily restricted to the CNS. Interestingly, netrin-G1 proteins did not show appreciable affinity to any netrin receptor examined. Unlike netrin-1, a secreted form of netrin-G1 consistently failed to attract circumferentially growing axons from the cerebellar plate. Our findings suggest that netrin-G1 and its putative receptors have coevolved independently from the classical netrins. The expression pattern of netrin-G1 and its predicted neuronal membrane localization suggest it may also have novel signaling functions in nervous system development.</description><identifier>ISSN: 0270-6474</identifier><identifier>EISSN: 1529-2401</identifier><identifier>DOI: 10.1523/jneurosci.20-17-06540.2000</identifier><identifier>PMID: 10964959</identifier><language>eng</language><publisher>United States: Soc Neuroscience</publisher><subject>Amino Acid Sequence ; Animals ; Axons - physiology ; Brain - physiology ; Cerebellum - physiology ; Chickens ; Cloning, Molecular ; Glycosylphosphatidylinositols - metabolism ; Male ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; netrin G1 ; Netrin Receptors ; Netrins ; Organ Specificity ; Phosphatidylinositol Diacylglycerol-Lyase ; Protein Conformation ; Receptors, Cell Surface - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment ; Sequence Homology, Amino Acid ; Type C Phospholipases - metabolism</subject><ispartof>The Journal of neuroscience, 2000-09, Vol.20 (17), p.6540-6550</ispartof><rights>Copyright © 2000 Society for Neuroscience 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c542t-11546019e20158a24b401e692b1df6cdcbdc1bbfb52950c1970d65bdcc07a1103</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772945/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772945/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10964959$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakashiba, Toshiaki</creatorcontrib><creatorcontrib>Ikeda, Toshio</creatorcontrib><creatorcontrib>Nishimura, Sachiko</creatorcontrib><creatorcontrib>Tashiro, Kei</creatorcontrib><creatorcontrib>Honjo, Tasuku</creatorcontrib><creatorcontrib>Culotti, Joseph G</creatorcontrib><creatorcontrib>Itohara, Shigeyoshi</creatorcontrib><title>Netrin-G1: a Novel Glycosyl Phosphatidylinositol-Linked Mammalian Netrin That Is Functionally Divergent from Classical Netrins</title><title>The Journal of neuroscience</title><addtitle>J Neurosci</addtitle><description>UNC-6/netrins compose a small phylogenetically conserved family of proteins that act as axon guidance cues. With a signal sequence trap method, we isolated a cDNA encoding a novel member of the UNC-6/netrin family, which we named netrin-G1. Unlike classical netrins, netrin-G1 consists of at least six isoforms of which five were predominantly anchored to the plasma membrane via glycosyl phosphatidyl-inositol linkages. Netrin-G1 transcripts were first detected in midbrain and hindbrain regions by embryonic day 12 and reached highest levels at perinatal stages in various brain regions, including olfactory bulb mitral cells, thalamus, and deep cerebellar nuclei. Its expression was primarily restricted to the CNS. Interestingly, netrin-G1 proteins did not show appreciable affinity to any netrin receptor examined. Unlike netrin-1, a secreted form of netrin-G1 consistently failed to attract circumferentially growing axons from the cerebellar plate. Our findings suggest that netrin-G1 and its putative receptors have coevolved independently from the classical netrins. The expression pattern of netrin-G1 and its predicted neuronal membrane localization suggest it may also have novel signaling functions in nervous system development.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Axons - physiology</subject><subject>Brain - physiology</subject><subject>Cerebellum - physiology</subject><subject>Chickens</subject><subject>Cloning, Molecular</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>Male</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>netrin G1</subject><subject>Netrin Receptors</subject><subject>Netrins</subject><subject>Organ Specificity</subject><subject>Phosphatidylinositol Diacylglycerol-Lyase</subject><subject>Protein Conformation</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Type C Phospholipases - metabolism</subject><issn>0270-6474</issn><issn>1529-2401</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVFv0zAUhS0EYmXwF5DFAzxl-LpOvOwBaSpbKSodgu3Zchyn9XDsYiet8rLfPpdUaDwhWbJ1_Z2je3QQegfkDHI6_XjvdB98VOaMkgx4RoqckfQm5BmaJKLMKCPwHE0I5SQrGGcn6FWM9wngBPhLdAKkLFiZlxP0sNJdMC6bwwWWeOV32uK5HZSPg8XfNz5uN7Iz9WCN89F03mZL437pGn-TbSutkQ6PDvg2gXgR8XXvVGe8k9YO-LPZ6bDWrsNN8C2eWRmjUdIeRfE1etFIG_Wb432K7q6vbmdfsuXNfDG7XGYqZ7TLAHJWECg1JZCfS8qqFFAXJa2gbgpVq6pWUFVNlcLnREHJSV3kaagIlwBkeoo-jb7bvmp1rdJGQVqxDaaVYRBeGvHvjzMbsfY7UXBOS5Yng_dHg-B_9zp2ojVRaWul076PglNKARj5LwjnhE_TSeDFCKrUZQy6-bsNEHHoWXxdXd39uPk5WwiaJlz86Vkcek7it0_zPJGOxSbgwwhszHqzN0GLmOqyCQex3-9Hw4Pf9BEiQbaP</recordid><startdate>20000901</startdate><enddate>20000901</enddate><creator>Nakashiba, Toshiaki</creator><creator>Ikeda, Toshio</creator><creator>Nishimura, Sachiko</creator><creator>Tashiro, Kei</creator><creator>Honjo, Tasuku</creator><creator>Culotti, Joseph G</creator><creator>Itohara, Shigeyoshi</creator><general>Soc Neuroscience</general><general>Society for Neuroscience</general><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><scope>5PM</scope></search><sort><creationdate>20000901</creationdate><title>Netrin-G1: a Novel Glycosyl Phosphatidylinositol-Linked Mammalian Netrin That Is Functionally Divergent from Classical Netrins</title><author>Nakashiba, Toshiaki ; Ikeda, Toshio ; Nishimura, Sachiko ; Tashiro, Kei ; Honjo, Tasuku ; Culotti, Joseph G ; Itohara, Shigeyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c542t-11546019e20158a24b401e692b1df6cdcbdc1bbfb52950c1970d65bdcc07a1103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Axons - physiology</topic><topic>Brain - physiology</topic><topic>Cerebellum - physiology</topic><topic>Chickens</topic><topic>Cloning, Molecular</topic><topic>Glycosylphosphatidylinositols - metabolism</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>netrin G1</topic><topic>Netrin Receptors</topic><topic>Netrins</topic><topic>Organ Specificity</topic><topic>Phosphatidylinositol Diacylglycerol-Lyase</topic><topic>Protein Conformation</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakashiba, Toshiaki</creatorcontrib><creatorcontrib>Ikeda, Toshio</creatorcontrib><creatorcontrib>Nishimura, Sachiko</creatorcontrib><creatorcontrib>Tashiro, Kei</creatorcontrib><creatorcontrib>Honjo, Tasuku</creatorcontrib><creatorcontrib>Culotti, Joseph G</creatorcontrib><creatorcontrib>Itohara, Shigeyoshi</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakashiba, Toshiaki</au><au>Ikeda, Toshio</au><au>Nishimura, Sachiko</au><au>Tashiro, Kei</au><au>Honjo, Tasuku</au><au>Culotti, Joseph G</au><au>Itohara, Shigeyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Netrin-G1: a Novel Glycosyl Phosphatidylinositol-Linked Mammalian Netrin That Is Functionally Divergent from Classical Netrins</atitle><jtitle>The Journal of neuroscience</jtitle><addtitle>J Neurosci</addtitle><date>2000-09-01</date><risdate>2000</risdate><volume>20</volume><issue>17</issue><spage>6540</spage><epage>6550</epage><pages>6540-6550</pages><issn>0270-6474</issn><eissn>1529-2401</eissn><abstract>UNC-6/netrins compose a small phylogenetically conserved family of proteins that act as axon guidance cues. With a signal sequence trap method, we isolated a cDNA encoding a novel member of the UNC-6/netrin family, which we named netrin-G1. Unlike classical netrins, netrin-G1 consists of at least six isoforms of which five were predominantly anchored to the plasma membrane via glycosyl phosphatidyl-inositol linkages. Netrin-G1 transcripts were first detected in midbrain and hindbrain regions by embryonic day 12 and reached highest levels at perinatal stages in various brain regions, including olfactory bulb mitral cells, thalamus, and deep cerebellar nuclei. Its expression was primarily restricted to the CNS. Interestingly, netrin-G1 proteins did not show appreciable affinity to any netrin receptor examined. Unlike netrin-1, a secreted form of netrin-G1 consistently failed to attract circumferentially growing axons from the cerebellar plate. Our findings suggest that netrin-G1 and its putative receptors have coevolved independently from the classical netrins. 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| subjects | Amino Acid Sequence Animals Axons - physiology Brain - physiology Cerebellum - physiology Chickens Cloning, Molecular Glycosylphosphatidylinositols - metabolism Male Mice Molecular Sequence Data Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism netrin G1 Netrin Receptors Netrins Organ Specificity Phosphatidylinositol Diacylglycerol-Lyase Protein Conformation Receptors, Cell Surface - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Sequence Alignment Sequence Homology, Amino Acid Type C Phospholipases - metabolism |
| title | Netrin-G1: a Novel Glycosyl Phosphatidylinositol-Linked Mammalian Netrin That Is Functionally Divergent from Classical Netrins |
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