Hedgehog Elicits Signal Transduction by Means of a Large Complex Containing the Kinesin-Related Protein Costal2
The hedgehog gene of Drosophila melanogaster encodes a secreted protein (HH) that plays a vital role in cell fate and patterning. Here we describe a protein complex that mediates signal transduction from HH. The complex includes the products of at least three genes: fused(a protein-serine/threonine...
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Veröffentlicht in: | Cell 1997-07, Vol.90 (2), p.225-234 |
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creator | Robbins, David J Nybakken, Kent E Kobayashi, Ryuji Sisson, John C Bishop, J.Michael Thérond, Pascal P |
description | The
hedgehog gene of Drosophila melanogaster encodes a secreted protein (HH) that plays a vital role in cell fate and patterning. Here we describe a protein complex that mediates signal transduction from HH. The complex includes the products of at least three genes:
fused(a protein-serine/threonine kinase),
cubitus interruptus(a transcription factor), and
costal2(a kinesin-like protein). The complex binds with great affinity to microtubules in the absence of HH, but binding is reversed by HH. Mutations in the extracatalytic domain of FU abolish both the biological function of the protein and its association with COS2. We conclude that the complex may facilitate signaling from HH by governing access of the
cubitus interruptus protein to the nucleus. |
doi_str_mv | 10.1016/S0092-8674(00)80331-1 |
format | Article |
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hedgehog gene of Drosophila melanogaster encodes a secreted protein (HH) that plays a vital role in cell fate and patterning. Here we describe a protein complex that mediates signal transduction from HH. The complex includes the products of at least three genes:
fused(a protein-serine/threonine kinase),
cubitus interruptus(a transcription factor), and
costal2(a kinesin-like protein). The complex binds with great affinity to microtubules in the absence of HH, but binding is reversed by HH. Mutations in the extracatalytic domain of FU abolish both the biological function of the protein and its association with COS2. We conclude that the complex may facilitate signaling from HH by governing access of the
cubitus interruptus protein to the nucleus.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(00)80331-1</identifier><identifier>PMID: 9244297</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Cells, Cultured ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Drosophila melanogaster ; Drosophila melanogaster - chemistry ; Drosophila melanogaster - growth & development ; Drosophila melanogaster - physiology ; Drosophila Proteins ; Embryo, Nonmammalian - chemistry ; Embryo, Nonmammalian - physiology ; Gene Expression Regulation, Developmental - physiology ; Hedgehog Proteins ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Kinesin - genetics ; Kinesin - metabolism ; Kinesin - pharmacology ; Microtubules - metabolism ; Phosphorylation ; Protein Binding - physiology ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Signal Transduction - physiology ; Transcription Factors ; Zinc Fingers - genetics</subject><ispartof>Cell, 1997-07, Vol.90 (2), p.225-234</ispartof><rights>1997 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-76f4d21ae59e97c37a6bc7890773010ff8d9e5db3eeb7d1b91961f82eb1ba9143</citedby><cites>FETCH-LOGICAL-c556t-76f4d21ae59e97c37a6bc7890773010ff8d9e5db3eeb7d1b91961f82eb1ba9143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(00)80331-1$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9244297$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Robbins, David J</creatorcontrib><creatorcontrib>Nybakken, Kent E</creatorcontrib><creatorcontrib>Kobayashi, Ryuji</creatorcontrib><creatorcontrib>Sisson, John C</creatorcontrib><creatorcontrib>Bishop, J.Michael</creatorcontrib><creatorcontrib>Thérond, Pascal P</creatorcontrib><title>Hedgehog Elicits Signal Transduction by Means of a Large Complex Containing the Kinesin-Related Protein Costal2</title><title>Cell</title><addtitle>Cell</addtitle><description>The
hedgehog gene of Drosophila melanogaster encodes a secreted protein (HH) that plays a vital role in cell fate and patterning. Here we describe a protein complex that mediates signal transduction from HH. The complex includes the products of at least three genes:
fused(a protein-serine/threonine kinase),
cubitus interruptus(a transcription factor), and
costal2(a kinesin-like protein). The complex binds with great affinity to microtubules in the absence of HH, but binding is reversed by HH. Mutations in the extracatalytic domain of FU abolish both the biological function of the protein and its association with COS2. We conclude that the complex may facilitate signaling from HH by governing access of the
cubitus interruptus protein to the nucleus.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cells, Cultured</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila melanogaster</subject><subject>Drosophila melanogaster - chemistry</subject><subject>Drosophila melanogaster - growth & development</subject><subject>Drosophila melanogaster - physiology</subject><subject>Drosophila Proteins</subject><subject>Embryo, Nonmammalian - chemistry</subject><subject>Embryo, Nonmammalian - physiology</subject><subject>Gene Expression Regulation, Developmental - physiology</subject><subject>Hedgehog Proteins</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Kinesin - genetics</subject><subject>Kinesin - metabolism</subject><subject>Kinesin - pharmacology</subject><subject>Microtubules - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding - physiology</subject><subject>Protein Structure, Tertiary</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Signal Transduction - physiology</subject><subject>Transcription Factors</subject><subject>Zinc Fingers - genetics</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS1U1C6Fn1DJJ1QOAY8Tx_EJVatCEYuo2nK2HHuSusraW9uL6L8n21312tNo9L6ZJ71HyBmwz8Cg_XLLmOJV18rmnLFPHatrqOANWQBTsmpA8iOyeEFOyLucHxhjnRDimBwr3jRcyQWJV-hGvI8jvZy89SXTWz8GM9G7ZEJ2W1t8DLR_or9w3mkcqKErk0aky7jeTPhvnqEYH3wYablH-tMHzD5UNziZgo5ep1jQhxnLxUz8PXk7mCnjh8M8JX--Xd4tr6rV7-8_lherygrRlkq2Q-M4GBQKlbS1NG1vZaeYlDUDNgydUyhcXyP20kGvQLUwdBx76I2Cpj4lH_d_Nyk-bjEXvfbZ4jSZgHGbtVTQ1hzgVRDaOW0p-AyKPWhTzDnhoDfJr0160sD0rhH93Ijexa0Z08-N6J3B2cFg26_RvVwdKpj1r3sd5zj-ekw6W4_BovMJbdEu-lcc_gOBZJr7</recordid><startdate>19970725</startdate><enddate>19970725</enddate><creator>Robbins, David J</creator><creator>Nybakken, Kent E</creator><creator>Kobayashi, Ryuji</creator><creator>Sisson, John C</creator><creator>Bishop, J.Michael</creator><creator>Thérond, Pascal P</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970725</creationdate><title>Hedgehog Elicits Signal Transduction by Means of a Large Complex Containing the Kinesin-Related Protein Costal2</title><author>Robbins, David J ; Nybakken, Kent E ; Kobayashi, Ryuji ; Sisson, John C ; Bishop, J.Michael ; Thérond, Pascal P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-76f4d21ae59e97c37a6bc7890773010ff8d9e5db3eeb7d1b91961f82eb1ba9143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cells, Cultured</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila melanogaster</topic><topic>Drosophila melanogaster - chemistry</topic><topic>Drosophila melanogaster - growth & development</topic><topic>Drosophila melanogaster - physiology</topic><topic>Drosophila Proteins</topic><topic>Embryo, Nonmammalian - chemistry</topic><topic>Embryo, Nonmammalian - physiology</topic><topic>Gene Expression Regulation, Developmental - physiology</topic><topic>Hedgehog Proteins</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Kinesin - genetics</topic><topic>Kinesin - metabolism</topic><topic>Kinesin - pharmacology</topic><topic>Microtubules - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding - physiology</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Signal Transduction - physiology</topic><topic>Transcription Factors</topic><topic>Zinc Fingers - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Robbins, David J</creatorcontrib><creatorcontrib>Nybakken, Kent E</creatorcontrib><creatorcontrib>Kobayashi, Ryuji</creatorcontrib><creatorcontrib>Sisson, John C</creatorcontrib><creatorcontrib>Bishop, J.Michael</creatorcontrib><creatorcontrib>Thérond, Pascal P</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robbins, David J</au><au>Nybakken, Kent E</au><au>Kobayashi, Ryuji</au><au>Sisson, John C</au><au>Bishop, J.Michael</au><au>Thérond, Pascal P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hedgehog Elicits Signal Transduction by Means of a Large Complex Containing the Kinesin-Related Protein Costal2</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1997-07-25</date><risdate>1997</risdate><volume>90</volume><issue>2</issue><spage>225</spage><epage>234</epage><pages>225-234</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The
hedgehog gene of Drosophila melanogaster encodes a secreted protein (HH) that plays a vital role in cell fate and patterning. Here we describe a protein complex that mediates signal transduction from HH. The complex includes the products of at least three genes:
fused(a protein-serine/threonine kinase),
cubitus interruptus(a transcription factor), and
costal2(a kinesin-like protein). The complex binds with great affinity to microtubules in the absence of HH, but binding is reversed by HH. Mutations in the extracatalytic domain of FU abolish both the biological function of the protein and its association with COS2. We conclude that the complex may facilitate signaling from HH by governing access of the
cubitus interruptus protein to the nucleus.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9244297</pmid><doi>10.1016/S0092-8674(00)80331-1</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Cells, Cultured DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Drosophila melanogaster Drosophila melanogaster - chemistry Drosophila melanogaster - growth & development Drosophila melanogaster - physiology Drosophila Proteins Embryo, Nonmammalian - chemistry Embryo, Nonmammalian - physiology Gene Expression Regulation, Developmental - physiology Hedgehog Proteins Insect Proteins - genetics Insect Proteins - metabolism Kinesin - genetics Kinesin - metabolism Kinesin - pharmacology Microtubules - metabolism Phosphorylation Protein Binding - physiology Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Signal Transduction - physiology Transcription Factors Zinc Fingers - genetics |
title | Hedgehog Elicits Signal Transduction by Means of a Large Complex Containing the Kinesin-Related Protein Costal2 |
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