Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p

被引:131
作者
Jasperson, SL
Giddings, TH
Winey, M
机构
[1] Univ Colorado, MCD Biol, Boulder, CO 80309 USA
[2] Univ Colorado, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA
关键词
D O I
10.1083/jcb.200208169
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Accurate duplication of the Saccharomyces cerevisiae spindle pole body (SPB) is required for formation of a bipolar mitotic spindle. We identified mutants in SPB assembly by screening a temperature-sensitive collection of yeast for defects in SPB incorporation of a fluorescently marked integral SPB component, Spc42p. One SPB assembly mutant contained a mutation in a previously uncharacterized open reading frame that we call MPS3 (for monopolar spindle). mps3-1 mutants arrest in mitosis with monopolar spindles at the nonpermissive temperature, suggesting a defect in SPB duplication. Execution point experiments revealed that MPS3 function is required for the first step of SPB duplication in G1. Like cells containing mutations in two other genes required for this step of SPB duplication (CDC31 and KAR1), mps3-1 mutants arrest with a single unduplicated SPB that lacks an associated half-bridge. MPS3 encodes an essential integral membrane protein that localizes to the SPB half-bridge. Genetic interactions between MPS3 and CDC31 and binding of Cdc31p to Mps3p in vitro, as well as the fact that Cdc31p localization to the SPB is partially dependent on Mps3p function, suggest that one function for Mps3p during SPB duplication is to recruit Cdc31p, the yeast centrin homologue, to the half-bridge.
引用
收藏
页码:945 / 956
页数:12
相关论文
共 50 条
[41]   Sid4p is required to localize components of the septation initiation pathway to the spindle pole body in fission yeast [J].
Chang, L ;
Gould, KL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (10) :5249-5254
[42]   Mps1p regulates meiotic spindle pole body duplication in addition to having novel roles during sporulation [J].
Straight, PD ;
Giddings, TH ;
Winey, M .
MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (10) :3525-3537
[43]   Regulation of Mob1p, an essential budding yeast protein required for completion of mitosis and spindle pole body duplication [J].
Luca, FC ;
Winey, M .
MOLECULAR BIOLOGY OF THE CELL, 1998, 9 :12A-12A
[44]   Spc98p and Spc97p of the yeast γ-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p [J].
Knop, M ;
Schiebel, E .
EMBO JOURNAL, 1997, 16 (23) :6985-6995
[45]   Nuclear inner membrane fusion facilitated by yeast Jem1p is required for spindle pole body fusion but not for the first mitotic nuclear division during yeast mating [J].
Nishikawa, Shuh-ichi ;
Hirata, Aiko ;
Endo, Toshiya .
GENES TO CELLS, 2008, 13 (11) :1185-1195
[46]   Binding of centrins and yeast calmodulin to synthetic peptides corresponding to binding sites in the spindle pole body components Kar1p and Spc110p [J].
Geier, BM ;
Wiech, H ;
Schiebel, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (45) :28366-28374
[47]   The spindle pole body component Spc98p interacts with the gamma-tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment [J].
Geissler, S ;
Pereira, G ;
Spang, A ;
Knop, M ;
Soues, S ;
Kilmartin, J ;
Schiebel, E .
EMBO JOURNAL, 1996, 15 (15) :3899-3911
[48]   The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170 [J].
Methot, N ;
Rom, E ;
Olsen, H ;
Sonenberg, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (02) :1110-1116
[49]   Fission yeast Sop2p: A novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function [J].
Balasubramanian, MK ;
Feoktistova, A ;
McCollum, D ;
Gould, KL .
EMBO JOURNAL, 1996, 15 (23) :6426-6437
[50]   The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly [J].
Niepel, M ;
Strambio-de-Castillia, C ;
Fasolo, J ;
Chait, BT ;
Rout, MP .
JOURNAL OF CELL BIOLOGY, 2005, 170 (02) :225-235