Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiae

被引:13
作者
Kosodo, Y
Imai, K
Hirata, A
Noda, Y
Takatsuki, A
Adachi, H
Yoda, K [1 ]
机构
[1] Univ Tokyo, Dept Biotechnol, Bunkyo Ku, Tokyo 1138657, Japan
[2] Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1138657, Japan
[3] RIKEN, Inst Phys & Chem Res, Wako, Saitama 3510198, Japan
关键词
multicopy suppressor; SLY1; vesicular trafficking; ER-Golgi transport; Saccharomyces cerevisiae;
D O I
10.1002/yea.747
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Saccharomyces cerevisiae Sly1 protein is a member of the Sec1/Munc18-family proteins, which are essential for vesicular trafficking, but their exact biological roles are yet to be determined. A temperature-sensitive sly1 mutant arrests the vesicular transport from the ER to Golgi compartments at 37 degrees. We screened for multicopy suppressor genes that restore the colony formation of the sly1(ts) mutant to discover functionally interacting components. The suppressor genes obtained were classified as: (1) those that encode a multifunctional suppressor, SSD1; (2) heat shock proteins, SSB1 and SSB2; (3) cell surface proteins, WSC1, WSC2 and MID2; (4) ER-Golgi transport proteins, USO1 and BET1; and (5) an as-yet-uncharacterized protein, HSD1 (high-copy suppressor of SLY1 defect 1). By epitope tagging of the gene product, we found that Hsd1 protein is an ER-resident membrane protein. Its overproduction induced enlargement of ER-like membrane structures. Copyright (C) 2001 John Wiley & Sons, Ltd.
引用
收藏
页码:1003 / 1014
页数:12
相关论文
共 48 条
[1]   A FAMILY OF PROTEINS INVOLVED IN INTRACELLULAR-TRANSPORT [J].
AALTO, MK ;
KERANEN, S ;
RONNE, H .
CELL, 1992, 68 (02) :181-182
[2]   THE MOLECULAR MACHINERY FOR SECRETION IS CONSERVED FROM YEAST TO NEURONS [J].
BENNETT, MK ;
SCHELLER, RH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (07) :2559-2563
[3]   Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins [J].
Cao, XC ;
Ballew, N ;
Barlowe, C .
EMBO JOURNAL, 1998, 17 (08) :2156-2165
[4]   Intracellular signaling from the endoplasmic reticulum to the nucleus [J].
Chapman, R ;
Sidrauski, C ;
Walter, P .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1998, 14 :459-485
[5]   The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane [J].
Cox, JS ;
Chapman, RE ;
Walter, P .
MOLECULAR BIOLOGY OF THE CELL, 1997, 8 (09) :1805-1814
[6]   Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport [J].
Dascher, C ;
Balch, WE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (27) :15866-15869
[7]   IDENTIFICATION AND STRUCTURE OF 4 YEAST GENES (SLY) THAT ARE ABLE TO SUPPRESS THE FUNCTIONAL LOSS OF YPT1, A MEMBER OF THE RAS SUPERFAMILY [J].
DASCHER, C ;
OSSIG, R ;
GALLWITZ, D ;
SCHMITT, HD .
MOLECULAR AND CELLULAR BIOLOGY, 1991, 11 (02) :872-885
[8]   High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking [J].
Grabowski, R ;
Gallwitz, D .
FEBS LETTERS, 1997, 411 (2-3) :169-172
[9]   A role for the Pkc1 MAP kinase pathway of Saccharomyces cerevisiae in bud emergence and identification of a putative upstream regulator [J].
Gray, JV ;
Ogas, JP ;
Kamada, Y ;
Stone, M ;
Levin, DE ;
Herskowitz, I .
EMBO JOURNAL, 1997, 16 (16) :4924-4937
[10]   SYNAPTIC VESICLE FUSION COMPLEX CONTAINS UNC-18 HOMOLOG BOUND TO SYNTAXIN [J].
HATA, Y ;
SLAUGHTER, CA ;
SUDHOF, TC .
NATURE, 1993, 366 (6453) :347-351