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The Bud14p–Glc7p complex functions as a cortical regulator of dynein in budding yeast
Author(s) -
Knaus Michèle,
Cameroni Elisabetta,
Pedruzzi Ivo,
Tatchell Kelly,
De Virgilio Claudio,
Peter Matthias
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600783
Subject(s) - biology , microbiology and biotechnology , dynein , cell cortex , astral microtubules , cytokinesis , dynactin , microtubule , mitosis , spindle pole body , anaphase , cytoskeleton , spindle apparatus , cell division , cell cycle , genetics , cell
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.