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dc.contributor.authorUsui, Takeo
dc.contributor.authorMaekawa, Hiromi
dc.contributor.authorPereira, Gislene
dc.contributor.authorSchiebel, Elmar
dc.date.accessioned2009-09-22T14:59:36Z
dc.date.available2009-09-22T14:59:36Z
dc.date.issued2003-09-15
dc.identifier.citationThe XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage. 2003, 22 (18):4779-93 EMBO J.en
dc.identifier.issn0261-4189
dc.identifier.pmid12970190
dc.identifier.doi10.1093/emboj/cdg459
dc.identifier.urihttp://hdl.handle.net/10541/82123
dc.description.abstractThe yeast protein Stu2 belongs to the XMAP215 family of conserved microtubule-binding proteins which regulate microtubule plus end dynamics. XMAP215-related proteins also bind to centrosomes and spindle pole bodies (SPBs) through proteins like the mammalian transforming acidic coiled coil protein TACC or the yeast Spc72. We show that yeast Spc72 has two distinct domains involved in microtubule organization. The essential 100 N-terminal amino acids of Spc72 interact directly with the gamma-tubulin complex, and an adjacent non-essential domain of Spc72 mediates binding to Stu2. Through these domains, Spc72 brings Stu2 and the gamma-tubulin complex together into a single complex. Manipulation of Spc72-Stu2 interaction at SPBs compromises the anchorage of astral microtubules at the SPB and surprisingly also influences the dynamics of microtubule plus ends. Permanently tethering Stu2 to SPBs by fusing it to a version of Spc72 that lacks the Stu2-binding site in part complements these defects in a manner which is dependent upon the microtubule-binding domain of Stu2. Thus, the SPB-associated Spc72-Stu2 complex plays a key role in regulating microtubule properties.
dc.language.isoenen
dc.subject.meshGenotype
dc.subject.meshMicrotubule-Associated Proteins
dc.subject.meshMicrotubules
dc.subject.meshMitotic Spindle Apparatus
dc.subject.meshPolymerase Chain Reaction
dc.subject.meshProtein Binding
dc.subject.meshSaccharomyces cerevisiae
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.titleThe XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage.en
dc.typeArticleen
dc.contributor.departmentThe Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalThe EMBO Journalen
html.description.abstractThe yeast protein Stu2 belongs to the XMAP215 family of conserved microtubule-binding proteins which regulate microtubule plus end dynamics. XMAP215-related proteins also bind to centrosomes and spindle pole bodies (SPBs) through proteins like the mammalian transforming acidic coiled coil protein TACC or the yeast Spc72. We show that yeast Spc72 has two distinct domains involved in microtubule organization. The essential 100 N-terminal amino acids of Spc72 interact directly with the gamma-tubulin complex, and an adjacent non-essential domain of Spc72 mediates binding to Stu2. Through these domains, Spc72 brings Stu2 and the gamma-tubulin complex together into a single complex. Manipulation of Spc72-Stu2 interaction at SPBs compromises the anchorage of astral microtubules at the SPB and surprisingly also influences the dynamics of microtubule plus ends. Permanently tethering Stu2 to SPBs by fusing it to a version of Spc72 that lacks the Stu2-binding site in part complements these defects in a manner which is dependent upon the microtubule-binding domain of Stu2. Thus, the SPB-associated Spc72-Stu2 complex plays a key role in regulating microtubule properties.


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