Myosin V orientates the mitotic spindle in yeast
Coordination of spindle orientation with the axis of cell division is an essential process in all eukaryotes. In addition to ensuring accurate chromosomal segregation, proper spindle orientation also establishes differential cell fates and proper morphogenesis 1 . In both animal and yeast cells, thi...
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Veröffentlicht in: | Nature (London) 2000-08, Vol.406 (6799), p.1013-1015 |
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creator | Yin, Hongwei Pruyne, David Huffaker, Tim C. Bretscher, Anthony |
description | Coordination of spindle orientation with the axis of cell division is an essential process in all eukaryotes. In addition to ensuring accurate chromosomal segregation, proper spindle orientation also establishes differential cell fates and proper morphogenesis
1
. In both animal and yeast cells, this process is dependent on cytoplasmic microtubules interacting with the cortical actin-based cytoskeleton
2
,
3
,
4
,
5
, although the motive force was unknown. Here we show that yeast Myo2, a myosin V that translocates along polarized actin cables into the bud
6
, orientates the spindle early in the cell cycle by binding and polarizing the microtubule-associated protein Kar9 (refs
7
,
8
,
9
). The tail domain of Myo2 that binds Kar9 also interacts with secretory vesicles
12
and vacuolar elements
13
, making it a pivotal component of yeast cell polarization. |
doi_str_mv | 10.1038/35023024 |
format | Article |
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1
. In both animal and yeast cells, this process is dependent on cytoplasmic microtubules interacting with the cortical actin-based cytoskeleton
2
,
3
,
4
,
5
, although the motive force was unknown. Here we show that yeast Myo2, a myosin V that translocates along polarized actin cables into the bud
6
, orientates the spindle early in the cell cycle by binding and polarizing the microtubule-associated protein Kar9 (refs
7
,
8
,
9
). The tail domain of Myo2 that binds Kar9 also interacts with secretory vesicles
12
and vacuolar elements
13
, making it a pivotal component of yeast cell polarization.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/35023024</identifier><identifier>PMID: 10984058</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Actins - metabolism ; Biological and medical sciences ; Carrier Proteins - metabolism ; Carrier Proteins - physiology ; Cell Cycle ; Cell division ; Cells ; Fundamental and applied biological sciences. Psychology ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Humanities and Social Sciences ; Kar9 protein ; letter ; Medical research ; Microbiology ; Microtubule-Associated Proteins - metabolism ; Microtubules - metabolism ; multidisciplinary ; Mycology ; Myo2 protein ; Myosin Heavy Chains ; Myosin Type II ; Myosin Type V ; myosin V ; Myosins - metabolism ; Myosins - physiology ; Nuclear Proteins - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; Saccharomycetales ; Schizosaccharomyces pombe Proteins ; Science ; Science (multidisciplinary) ; Spindle Apparatus - physiology ; Two-Hybrid System Techniques ; Yeast ; Yeasts</subject><ispartof>Nature (London), 2000-08, Vol.406 (6799), p.1013-1015</ispartof><rights>Macmillan Magazines Ltd. 2000</rights><rights>2000 INIST-CNRS</rights><rights>COPYRIGHT 2000 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. Aug 31, 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c670t-cff0bfb5a2c18a5ef7c2a2fe6dfb8fed7aa83ebb1300c2b649e0ad4a0e7928053</citedby><cites>FETCH-LOGICAL-c670t-cff0bfb5a2c18a5ef7c2a2fe6dfb8fed7aa83ebb1300c2b649e0ad4a0e7928053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/35023024$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/35023024$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1498112$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10984058$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yin, Hongwei</creatorcontrib><creatorcontrib>Pruyne, David</creatorcontrib><creatorcontrib>Huffaker, Tim C.</creatorcontrib><creatorcontrib>Bretscher, Anthony</creatorcontrib><title>Myosin V orientates the mitotic spindle in yeast</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Coordination of spindle orientation with the axis of cell division is an essential process in all eukaryotes. In addition to ensuring accurate chromosomal segregation, proper spindle orientation also establishes differential cell fates and proper morphogenesis
1
. In both animal and yeast cells, this process is dependent on cytoplasmic microtubules interacting with the cortical actin-based cytoskeleton
2
,
3
,
4
,
5
, although the motive force was unknown. Here we show that yeast Myo2, a myosin V that translocates along polarized actin cables into the bud
6
, orientates the spindle early in the cell cycle by binding and polarizing the microtubule-associated protein Kar9 (refs
7
,
8
,
9
). The tail domain of Myo2 that binds Kar9 also interacts with secretory vesicles
12
and vacuolar elements
13
, making it a pivotal component of yeast cell polarization.</description><subject>Actins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - metabolism</subject><subject>Carrier Proteins - physiology</subject><subject>Cell Cycle</subject><subject>Cell division</subject><subject>Cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Growth, nutrition, metabolism, transports, enzymes. 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Anthony</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myosin V orientates the mitotic spindle in yeast</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2000-08-31</date><risdate>2000</risdate><volume>406</volume><issue>6799</issue><spage>1013</spage><epage>1015</epage><pages>1013-1015</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Coordination of spindle orientation with the axis of cell division is an essential process in all eukaryotes. In addition to ensuring accurate chromosomal segregation, proper spindle orientation also establishes differential cell fates and proper morphogenesis
1
. In both animal and yeast cells, this process is dependent on cytoplasmic microtubules interacting with the cortical actin-based cytoskeleton
2
,
3
,
4
,
5
, although the motive force was unknown. Here we show that yeast Myo2, a myosin V that translocates along polarized actin cables into the bud
6
, orientates the spindle early in the cell cycle by binding and polarizing the microtubule-associated protein Kar9 (refs
7
,
8
,
9
). The tail domain of Myo2 that binds Kar9 also interacts with secretory vesicles
12
and vacuolar elements
13
, making it a pivotal component of yeast cell polarization.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>10984058</pmid><doi>10.1038/35023024</doi><tpages>3</tpages></addata></record> |
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source | MEDLINE; SpringerLink Journals; Nature Journals Online |
subjects | Actins - metabolism Biological and medical sciences Carrier Proteins - metabolism Carrier Proteins - physiology Cell Cycle Cell division Cells Fundamental and applied biological sciences. Psychology Growth, nutrition, metabolism, transports, enzymes. Molecular biology Humanities and Social Sciences Kar9 protein letter Medical research Microbiology Microtubule-Associated Proteins - metabolism Microtubules - metabolism multidisciplinary Mycology Myo2 protein Myosin Heavy Chains Myosin Type II Myosin Type V myosin V Myosins - metabolism Myosins - physiology Nuclear Proteins - metabolism Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Saccharomycetales Schizosaccharomyces pombe Proteins Science Science (multidisciplinary) Spindle Apparatus - physiology Two-Hybrid System Techniques Yeast Yeasts |
title | Myosin V orientates the mitotic spindle in yeast |
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