Home LiteratureArticle Details
PMID: 12699621 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Septins have a dual role in controlling mitotic exit in budding yeast.

Current biology : CB ·Vol. 13 ·No. 8 ·2003-04-15 ·Pages 654-8

Castillon GA, Adames NR, Rosello CH, Seidel HS, Longtine MS, Cooper JA, Heil-Chapdelaine RA

Abstract

In Saccharomyces cerevisiae, the spindle position checkpoint ensures that cells do not exit mitosis until the mitotic spindle moves into the mother/bud neck and thus guarantees that each cell receives one nucleus [1-6]. Mitotic exit is controlled by the small G protein Tem1p. Tem1p and its GTPase activating protein (GAP) Bub2p/Bfa1p are located on the daughter-bound spindle pole body. The GEF Lte1p is located in the bud. This segregation helps keep Tem1p in its inactive GDP state until the spindle enters the neck. However, the checkpoint functions without Lte1p and apparently senses cytoplasmic microtubules in the mother/bud neck [7-9]. To investigate this mechanism, we examined mutants defective for septins, which compose a ring at the neck [10]. We found that the septin mutants sep7Delta and cdc10Delta are defective in the checkpoint. When movement of the spindle into the neck was delayed, mitotic exit occurred, inappropriately leaving both nuclei in the mother. In sep7Delta and cdc10Delta mutants, Lte1p is mislocalized to the mother. In sep7Delta, but not cdc10Delta, mutants, inappropriate mitotic exit depends on Lte1p. These results suggest that septins serve as a diffusion barrier for Lte1p, and that Cdc10p is needed for the septin ring to serve as a scaffold for a putative microtubule sensor.

MeSH Terms
Cell Cycle Proteins/metabolism Cytoskeletal Proteins/metabolism,physiology Guanine Nucleotide Exchange Factors/metabolism Microscopy, Fluorescence Mitosis/physiology Monomeric GTP-Binding Proteins/metabolism Mutation/genetics,physiology Saccharomyces cerevisiae/cytology,genetics Saccharomyces cerevisiae Proteins/metabolism Spindle Apparatus/physiology
Chemicals
BUB2 protein, S cerevisiae Cell Cycle Proteins Cytoskeletal Proteins Guanine Nucleotide Exchange Factors LTE1 protein, S cerevisiae Saccharomyces cerevisiae Proteins TEM1 protein, S cerevisiae Monomeric GTP-Binding Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Castillon Guillaume A
Department of Cell Biology, Washington University, St. Louis, MO 63110, USA.
Adames Neil R
Rosello Caroline H
Seidel Hannah S
Longtine Mark S
Cooper John A
Heil-Chapdelaine Richard A
Article Info
Journal
Current biology : CB
Abbr.
Curr Biol
ISSN
0960-9822
Published
2003-04-15
Pages
654-8
Language
English
Region
England
NLM ID
9107782
Subset
IM
Grants
NIGMS NIH HHS · R01 GM047337 · United States
NIGMS NIH HHS · R01 GM047337-12S1 · United States
NIGMS NIH HHS · GM 47337 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]