Article
- The EMBO Journal (2005) 24, 3000 - 3011
- doi:10.1038/sj.emboj.7600783
Published online: 18 August 2005
Subject Category:
The Bud14p–Glc7p complex functions as a cortical regulator of dynein in budding yeast
Michèle Knaus1, Elisabetta Cameroni2, Ivo Pedruzzi2,a, Kelly Tatchell3, Claudio De Virgilio2 and Matthias Peter1
- Swiss Federal Institute of Technology Zürich (ETH), Institute of Biochemistry, Zürich, Switzerland
- Department of Microbiology and Molecular Medicine, CMU, University of Geneva, Geneva, Switzerland
- Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA, USA
Correspondence to:
Claudio De Virgilio, Department of Microbiology and Molecular Medicine, CMU, University of Geneva, Geneva, Switzerland. Tel.: +41 22 379 54 95; Fax: +41 22 379 55 02; E-mail: claudio.devirgilio@medecine.unige.ch
Matthias Peter, Swiss Federal Institute of Technology Zürich (ETH), Institute of Biochemistry, ETH Hönggerberg HPM G 6.2, 8093 Zürich, Switzerland. Tel.: +41 1 632 3134; Fax: +41 1 632 1269; E-mail: matthias.peter@bc.biol.ethz.ch
aPresent address: Swiss Institute of Bioinformatics, CMU, University of Geneva, Switzerland
Received 24 May 2005; Accepted 21 July 2005
Abstract
Regulated interactions between microtubules (MTs) and the cell cortex control MT dynamics and position the mitotic spindle. In eukaryotic cells, the adenomatous polyposis coli/Kar9p and dynein/dynactin pathways are involved in guiding MT plus ends and MT sliding along the cortex, respectively. Here we identify Bud14p as a novel cortical activator of the dynein/dynactin complex in budding yeast. Bud14p accumulates at sites of polarized growth and the mother-bud neck during cytokinesis. The localization to bud and shmoo tips requires an intact actin cytoskeleton and the kelch-domain-containing proteins Kel1p and Kel2p. While cells lacking Bud14p function fail to stabilize the pre-anaphase spindle at the mother-bud neck, overexpression of Bud14p is toxic and leads to elongated astral MTs and increased dynein-dependent sliding along the cell cortex. Bud14p physically interacts with the type-I phosphatase Glc7p, and localizes Glc7p to the bud cortex. Importantly, the formation of Bud14p–Glc7p complexes is necessary to regulate MT dynamics at the cortex. Taken together, our results suggest that Bud14p functions as a regulatory subunit of the Glc7p type-I phosphatase to stabilize MT interactions specifically at sites of polarized growth.
Keywords:
- Bud14p,
- dynein,
- Glc7p,
- microtubule regulation,
- spindle orientation
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated
NEWS AND VIEWS
Centrosomes as command centres for cellular control
Nature Cell Biology News and Views (01 May 2001)
First things first: spindle orientation and mitotic progression
Nature Cell Biology News and Views (01 Oct 2002)
RESEARCH
The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage
The EMBO Journal Article (15 Sep 2003)
The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage
The EMBO Journal Article (15 Sep 2003)
