The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage.
Affiliation
The Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.Issue Date
2003-09-15
Metadata
Show full item recordAbstract
The 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.Citation
The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage. 2003, 22 (18):4779-93 EMBO J.Journal
The EMBO JournalDOI
10.1093/emboj/cdg459PubMed ID
12970190Type
ArticleLanguage
enISSN
0261-4189ae974a485f413a2113503eed53cd6c53
10.1093/emboj/cdg459
Scopus Count
Collections
Related articles
- The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation.
- Authors: Gunzelmann J, Rüthnick D, Lin TC, Zhang W, Neuner A, Jäkle U, Schiebel E
- Issue date: 2018 Sep 17
- The spindle pole body component Spc97p interacts with the gamma-tubulin of Saccharomyces cerevisiae and functions in microtubule organization and spindle pole body duplication.
- Authors: Knop M, Pereira G, Geissler S, Grein K, Schiebel E
- Issue date: 1997 Apr 1
- Cortical capture of microtubules and spindle polarity in budding yeast - where's the catch?
- Authors: Huisman SM, Segal M
- Issue date: 2005 Feb 1
- Stu2 acts as a microtubule destabilizer in metaphase budding yeast spindles.
- Authors: Humphrey L, Felzer-Kim I, Joglekar AP
- Issue date: 2018 Feb 1
- Gamma-tubulin complex-mediated anchoring of spindle microtubules to spindle-pole bodies requires Msd1 in fission yeast.
- Authors: Toya M, Sato M, Haselmann U, Asakawa K, Brunner D, Antony C, Toda T
- Issue date: 2007 Jun