Fray, a Drosophila Serine/Threonine Kinase Homologous to Mammalian PASK, Is Required for Axonal Ensheathment
Fray is a serine/threonine kinase expressed by the peripheral glia of Drosophila, whose function is required for normal axonal ensheathment. Null fray mutants die early in larval development and have nerves with severe swelling and axonal defasciculation. The phenotype is associated with a failure o...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 2000-12, Vol.28 (3), p.793-806 |
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| creator | Leiserson, William M. Harkins, Elizabeth W. Keshishian, Haig |
| description | Fray is a serine/threonine kinase expressed by the peripheral glia of
Drosophila, whose function is required for normal axonal ensheathment. Null
fray mutants die early in larval development and have nerves with severe swelling and axonal defasciculation. The phenotype is associated with a failure of the ensheathing glia to correctly wrap peripheral axons. When the
fray cDNA is expressed in the ensheathing glia of
fray mutants, normal nerve morphology is restored. Fray belongs to a novel family of Ser/Thr kinases, the PF kinases, whose closest relatives are the PAK kinases. Rescue of the
Drosophila mutant phenotype with PASK, the rat homolog of Fray, demonstrates a functional homology among these proteins and suggests that the Fray signaling pathway is widely conserved. |
| doi_str_mv | 10.1016/S0896-6273(00)00154-9 |
| format | Article |
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Drosophila, whose function is required for normal axonal ensheathment. Null
fray mutants die early in larval development and have nerves with severe swelling and axonal defasciculation. The phenotype is associated with a failure of the ensheathing glia to correctly wrap peripheral axons. When the
fray cDNA is expressed in the ensheathing glia of
fray mutants, normal nerve morphology is restored. Fray belongs to a novel family of Ser/Thr kinases, the PF kinases, whose closest relatives are the PAK kinases. Rescue of the
Drosophila mutant phenotype with PASK, the rat homolog of Fray, demonstrates a functional homology among these proteins and suggests that the Fray signaling pathway is widely conserved.</description><identifier>ISSN: 0896-6273</identifier><identifier>EISSN: 1097-4199</identifier><identifier>DOI: 10.1016/S0896-6273(00)00154-9</identifier><identifier>PMID: 11163267</identifier><language>eng</language><publisher>Legacy CDMS: Elsevier Inc</publisher><subject>Animals ; Axons - metabolism ; Conserved Sequence ; Drosophila ; Fray protein ; Insect Proteins - metabolism ; Larva - genetics ; Larva - growth & development ; Larva - metabolism ; Life Sciences (General) ; Molecular Sequence Data ; Mutation ; Myelin Sheath - metabolism ; Neuroglia - metabolism ; Neuroglia - pathology ; PASK protein ; Peripheral Nervous System - growth & development ; Peripheral Nervous System - metabolism ; Peripheral Nervous System - pathology ; Phenotype ; Protein-Serine-Threonine Kinases - biosynthesis ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; protein-serine/threonine kinase ; Sequence Homology, Amino Acid ; Signal Transduction - genetics ; Space life sciences ; Transfection</subject><ispartof>Neuron (Cambridge, Mass.), 2000-12, Vol.28 (3), p.793-806</ispartof><rights>2000 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-92fbb3b5db9040b550f872cf73e47a49e1ed530331306174fcdeb0104f3407ac3</citedby><cites>FETCH-LOGICAL-c526t-92fbb3b5db9040b550f872cf73e47a49e1ed530331306174fcdeb0104f3407ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0896-6273(00)00154-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,782,786,3554,27933,27934,46004</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11163267$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leiserson, William M.</creatorcontrib><creatorcontrib>Harkins, Elizabeth W.</creatorcontrib><creatorcontrib>Keshishian, Haig</creatorcontrib><title>Fray, a Drosophila Serine/Threonine Kinase Homologous to Mammalian PASK, Is Required for Axonal Ensheathment</title><title>Neuron (Cambridge, Mass.)</title><addtitle>Neuron</addtitle><description>Fray is a serine/threonine kinase expressed by the peripheral glia of
Drosophila, whose function is required for normal axonal ensheathment. Null
fray mutants die early in larval development and have nerves with severe swelling and axonal defasciculation. The phenotype is associated with a failure of the ensheathing glia to correctly wrap peripheral axons. When the
fray cDNA is expressed in the ensheathing glia of
fray mutants, normal nerve morphology is restored. Fray belongs to a novel family of Ser/Thr kinases, the PF kinases, whose closest relatives are the PAK kinases. Rescue of the
Drosophila mutant phenotype with PASK, the rat homolog of Fray, demonstrates a functional homology among these proteins and suggests that the Fray signaling pathway is widely conserved.</description><subject>Animals</subject><subject>Axons - metabolism</subject><subject>Conserved Sequence</subject><subject>Drosophila</subject><subject>Fray protein</subject><subject>Insect Proteins - metabolism</subject><subject>Larva - genetics</subject><subject>Larva - growth & development</subject><subject>Larva - metabolism</subject><subject>Life Sciences (General)</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Myelin Sheath - metabolism</subject><subject>Neuroglia - metabolism</subject><subject>Neuroglia - pathology</subject><subject>PASK protein</subject><subject>Peripheral Nervous System - growth & development</subject><subject>Peripheral Nervous System - metabolism</subject><subject>Peripheral Nervous System - pathology</subject><subject>Phenotype</subject><subject>Protein-Serine-Threonine Kinases - biosynthesis</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>protein-serine/threonine kinase</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction - genetics</subject><subject>Space life sciences</subject><subject>Transfection</subject><issn>0896-6273</issn><issn>1097-4199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EoqHwDwD5hEDq0vH6Kz5VUT9o1SIQKWfLuztLjHbt1N6g9t_jNBEce7KlecaeeV5C3jH4zICp4yXMjapUrflHgE8ATIrKPCMzBkZXghnznMz-IQfkVc6_CySkYS_JAWNM8VrpGRkukns4oo6epZjjeuUHR5eYfMDj21XCGMqNXvvgMtLLOMYh_oqbTKdIv7pxdIN3gX5fLK-P6FWmP_Bu4xN2tI-JLu5jcAM9D3mFblqNGKbX5EXvhoxv9uch-Xlxfnt6Wd18-3J1uripWlmrqTJ13zS8kV1jQEAjJfRzXbe95ii0EwYZdpID54yDYlr0bYcNMBA9F6Bdyw_Jh9276xTvNpgnO_rc4jC4gGV6q2upgCv9JMj0nEvDRQHlDmyLppywt-vkR5ceLAO7zcM-5mG3si2AfczDmtL3fv_Bphmx-9-1D6AAb3dAMexsmFK2NZStGaul2ZZPdmUsuv54TDa3HkOLXfHcTraL_okJ_gJHS6HX</recordid><startdate>20001201</startdate><enddate>20001201</enddate><creator>Leiserson, William M.</creator><creator>Harkins, Elizabeth W.</creator><creator>Keshishian, Haig</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CYE</scope><scope>CYI</scope><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>7SS</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20001201</creationdate><title>Fray, a Drosophila Serine/Threonine Kinase Homologous to Mammalian PASK, Is Required for Axonal Ensheathment</title><author>Leiserson, William M. ; Harkins, Elizabeth W. ; Keshishian, Haig</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-92fbb3b5db9040b550f872cf73e47a49e1ed530331306174fcdeb0104f3407ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Axons - metabolism</topic><topic>Conserved Sequence</topic><topic>Drosophila</topic><topic>Fray protein</topic><topic>Insect Proteins - metabolism</topic><topic>Larva - genetics</topic><topic>Larva - growth & development</topic><topic>Larva - metabolism</topic><topic>Life Sciences (General)</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Myelin Sheath - metabolism</topic><topic>Neuroglia - metabolism</topic><topic>Neuroglia - pathology</topic><topic>PASK protein</topic><topic>Peripheral Nervous System - growth & development</topic><topic>Peripheral Nervous System - metabolism</topic><topic>Peripheral Nervous System - pathology</topic><topic>Phenotype</topic><topic>Protein-Serine-Threonine Kinases - biosynthesis</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>protein-serine/threonine kinase</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction - genetics</topic><topic>Space life sciences</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leiserson, William M.</creatorcontrib><creatorcontrib>Harkins, Elizabeth W.</creatorcontrib><creatorcontrib>Keshishian, Haig</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>NASA Scientific and Technical Information</collection><collection>NASA Technical Reports Server</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuron (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leiserson, William M.</au><au>Harkins, Elizabeth W.</au><au>Keshishian, Haig</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fray, a Drosophila Serine/Threonine Kinase Homologous to Mammalian PASK, Is Required for Axonal Ensheathment</atitle><jtitle>Neuron (Cambridge, Mass.)</jtitle><addtitle>Neuron</addtitle><date>2000-12-01</date><risdate>2000</risdate><volume>28</volume><issue>3</issue><spage>793</spage><epage>806</epage><pages>793-806</pages><issn>0896-6273</issn><eissn>1097-4199</eissn><abstract>Fray is a serine/threonine kinase expressed by the peripheral glia of
Drosophila, whose function is required for normal axonal ensheathment. Null
fray mutants die early in larval development and have nerves with severe swelling and axonal defasciculation. The phenotype is associated with a failure of the ensheathing glia to correctly wrap peripheral axons. When the
fray cDNA is expressed in the ensheathing glia of
fray mutants, normal nerve morphology is restored. Fray belongs to a novel family of Ser/Thr kinases, the PF kinases, whose closest relatives are the PAK kinases. Rescue of the
Drosophila mutant phenotype with PASK, the rat homolog of Fray, demonstrates a functional homology among these proteins and suggests that the Fray signaling pathway is widely conserved.</abstract><cop>Legacy CDMS</cop><pub>Elsevier Inc</pub><pmid>11163267</pmid><doi>10.1016/S0896-6273(00)00154-9</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); NASA Technical Reports Server; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Axons - metabolism Conserved Sequence Drosophila Fray protein Insect Proteins - metabolism Larva - genetics Larva - growth & development Larva - metabolism Life Sciences (General) Molecular Sequence Data Mutation Myelin Sheath - metabolism Neuroglia - metabolism Neuroglia - pathology PASK protein Peripheral Nervous System - growth & development Peripheral Nervous System - metabolism Peripheral Nervous System - pathology Phenotype Protein-Serine-Threonine Kinases - biosynthesis Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism protein-serine/threonine kinase Sequence Homology, Amino Acid Signal Transduction - genetics Space life sciences Transfection |
| title | Fray, a Drosophila Serine/Threonine Kinase Homologous to Mammalian PASK, Is Required for Axonal Ensheathment |
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