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PMID: 10428957 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interaction of the yeast gamma-tubulin complex-binding protein Spc72p with Kar1p is essential for microtubule function during karyogamy.

The EMBO journal ·Vol. 18 ·No. 15 ·1999-08-02 ·Pages 4180-95

Pereira G, Grueneberg U, Knop M, Schiebel E

Abstract

The spindle pole body component Kar1p has a function in nuclear fusion during conjugation, a process known as karyogamy. The molecular role of Kar1p during this process is poorly understood. Here we show that the yeast gamma-tubulin complex-binding protein Spc72p interacts directly with the N-terminal domain of Kar1p, thereby targeting the gamma-tubulin complex to the half bridge, a substructure of the spindle pole body, where it organizes microtubules. This binding of Spc72p to Kar1p has only a minor role during vegetative growth, whereas it becomes essential for karyogamy in mating cells, explaining the important role of Kar1p in this process. We also show that the localization of Spc72p within the spindle pole body changes throughout the cell cycle and even more strongly in response to mating pheromone. Taken together, these observations suggest that the relocalization of Spc72p within the spindle pole body is the 'landmark' event in the pheromone-induced reorganization of the cytoplasmic microtubules.

MeSH Terms
Fungal Proteins/metabolism Microtubules/physiology Nuclear Proteins/metabolism Protein Binding Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/growth & development,metabolism Saccharomyces cerevisiae Proteins Tubulin/metabolism
Chemicals
Fungal Proteins KAR1 protein, S cerevisiae Nuclear Proteins Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins Tubulin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pereira G
The Beatson Institute for Cancer Research, CRC Beatson Laboratories, Glasgow G61 1BD, Scotland, UK.
Grueneberg U
Knop M
Schiebel E
Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1999-08-02
Pages
4180-95
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1171495
Subset
IM
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