Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis
Dynamin was discovered in bovine brain tissue as a nucleotide-sensitive microtubule-binding protein of relative molecular mass 100,000. It was found to cross-link microtubules into highly ordered bundles, and appeared to have a role in intermicrotubule sliding in vitro. Cloning and sequencing of rat...
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Veröffentlicht in: | Nature (London) 1991-06, Vol.351 (6327), p.583-588 |
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description | Dynamin was discovered in bovine brain tissue as a nucleotide-sensitive microtubule-binding protein of relative molecular mass 100,000. It was found to cross-link microtubules into highly ordered bundles, and appeared to have a role in intermicrotubule sliding in vitro. Cloning and sequencing of rat brain dynamin complementary DNA identified an N-terminal region of about 300 amino acids which contained the three consensus elements characteristic of GTP-binding proteins. Extensive homology was found between this domain and the mammalian Mx proteins which are involved in interferon-induced viral resistance, and with the product of the VPS1 locus in Saccharomyces cerevisiae, which has been implicated both in membrane protein sorting, and in meiotic spindle pole separation. Dynamin-containing microtubule bundles were not observed in an immunofluorescence study of cultured mammalian cells, but a role for a GTP-requiring protein in intermicrotubule sliding during mitosis in plants has been reported. We report here that Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting. |
doi_str_mv | 10.1038/351583a0 |
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It was found to cross-link microtubules into highly ordered bundles, and appeared to have a role in intermicrotubule sliding in vitro. Cloning and sequencing of rat brain dynamin complementary DNA identified an N-terminal region of about 300 amino acids which contained the three consensus elements characteristic of GTP-binding proteins. Extensive homology was found between this domain and the mammalian Mx proteins which are involved in interferon-induced viral resistance, and with the product of the VPS1 locus in Saccharomyces cerevisiae, which has been implicated both in membrane protein sorting, and in meiotic spindle pole separation. Dynamin-containing microtubule bundles were not observed in an immunofluorescence study of cultured mammalian cells, but a role for a GTP-requiring protein in intermicrotubule sliding during mitosis in plants has been reported. We report here that Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/351583a0</identifier><identifier>PMID: 1828536</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Amino acids ; Animals ; Biological and medical sciences ; Blotting, Northern ; Blotting, Western ; Ca(2+) Mg(2+)-ATPase - genetics ; Ca(2+) Mg(2+)-ATPase - immunology ; Cellular biology ; clones ; Cloning ; Cloning, Molecular ; Cross Reactions ; DNA ; DNA - genetics ; Drosophila melanogaster ; Drosophila melanogaster - genetics ; Drosophila Proteins ; Dynamins ; Endocytosis ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genes ; Mammals ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; polypeptides ; Proteins ; Rats ; RNA</subject><ispartof>Nature (London), 1991-06, Vol.351 (6327), p.583-588</ispartof><rights>1991 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. 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We report here that Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Ca(2+) Mg(2+)-ATPase - genetics</subject><subject>Ca(2+) Mg(2+)-ATPase - immunology</subject><subject>Cellular biology</subject><subject>clones</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Cross Reactions</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>Drosophila melanogaster</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins</subject><subject>Dynamins</subject><subject>Endocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genes</subject><subject>Mammals</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Hybridization</subject><subject>polypeptides</subject><subject>Proteins</subject><subject>Rats</subject><subject>RNA</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp90U1v1DAQBmALgcqyIPEHAAupwIGAHTvx5IjKp1TEAXriEE2ScesqsRc7qbT_voYsFHHg5MM8fu2ZYeyhFK-kUPBaVbICheIW20ht6kLXYG6zjRAlFAJUfZfdS-lSCFFJo4_YkYQSKlVv2PfPyzi73UjchjglHiwf9h4n5zlG4uT7MNDAuz1PF65zkV5y5G9jSGF34Ubk5-SJO38VxqvM8i3yQ-j3c0gu3Wd3LI6JHhzOLTt7_-7bycfi9MuHTydvToteg5iLHqGpSDRCdSQ7jUPXCEs9AFqN2BFo03VNpQEpk1o2g6YaS1BaDbayg9qyZ2vuLoYfC6W5nVzqaRzRU1hSC6IWxtQyw-f_hUarEhqTf7JlT_-Rl2GJPnfRlkJrBaBURi9W1Od5pEi23UU3Ydy3UrQ_19L-Xkumjw55SzfRcAPXPeT68aGOqcfRRvS9SzesMWUjf3XweHUe5yXSH_DXQ09WYDG0eB5zyNnXUkglpFEadKmuAf-wpxg</recordid><startdate>19910613</startdate><enddate>19910613</enddate><creator>Chen, M.S</creator><creator>Obar, R.A</creator><creator>Schroeder, C.C</creator><creator>Austin, T.W</creator><creator>Poodry, C.A</creator><creator>Wadsworth, S.C</creator><creator>Vallee, R.B</creator><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>19910613</creationdate><title>Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis</title><author>Chen, M.S ; 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, M.S</au><au>Obar, R.A</au><au>Schroeder, C.C</au><au>Austin, T.W</au><au>Poodry, C.A</au><au>Wadsworth, S.C</au><au>Vallee, R.B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1991-06-13</date><risdate>1991</risdate><volume>351</volume><issue>6327</issue><spage>583</spage><epage>588</epage><pages>583-588</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Dynamin was discovered in bovine brain tissue as a nucleotide-sensitive microtubule-binding protein of relative molecular mass 100,000. It was found to cross-link microtubules into highly ordered bundles, and appeared to have a role in intermicrotubule sliding in vitro. Cloning and sequencing of rat brain dynamin complementary DNA identified an N-terminal region of about 300 amino acids which contained the three consensus elements characteristic of GTP-binding proteins. Extensive homology was found between this domain and the mammalian Mx proteins which are involved in interferon-induced viral resistance, and with the product of the VPS1 locus in Saccharomyces cerevisiae, which has been implicated both in membrane protein sorting, and in meiotic spindle pole separation. Dynamin-containing microtubule bundles were not observed in an immunofluorescence study of cultured mammalian cells, but a role for a GTP-requiring protein in intermicrotubule sliding during mitosis in plants has been reported. We report here that Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>1828536</pmid><doi>10.1038/351583a0</doi><tpages>6</tpages></addata></record> |
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subjects | Amino Acid Sequence amino acid sequences Amino acids Animals Biological and medical sciences Blotting, Northern Blotting, Western Ca(2+) Mg(2+)-ATPase - genetics Ca(2+) Mg(2+)-ATPase - immunology Cellular biology clones Cloning Cloning, Molecular Cross Reactions DNA DNA - genetics Drosophila melanogaster Drosophila melanogaster - genetics Drosophila Proteins Dynamins Endocytosis Fundamental and applied biological sciences. Psychology Gene expression Genes Mammals Molecular and cellular biology Molecular genetics Molecular Sequence Data Nucleic Acid Hybridization polypeptides Proteins Rats RNA |
title | Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis |
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