The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton

被引:76
作者
Goodman, A
Goode, BL
Matsudaira, P
Fink, GR [1 ]
机构
[1] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA
[2] MIT, Cambridge, MA 02139 USA
[3] Brandeis Univ, Dept Biol, Waltham, MA 02454 USA
[4] Brandeis Univ, Rosenstiel Ctr, Waltham, MA 02454 USA
关键词
D O I
10.1091/mbc.E03-01-0028
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Calponins and transgelins are members of a conserved family of actin-associated proteins widely expressed from yeast to humans. Although a role for calponin in muscle cells has been described, the biochemical activities and in vivo functions of nonmuscle calponins and transgelins are largely unknown. Herein, we have used genetic and biochemical analyses to characterize the budding yeast member of this family, Scp1, which most closely resembles transgelin and contains one calponin homology (CH) domain. We show that Scp1 is a novel component of yeast cortical actin patches and shares in vivo functions and biochemical activities with Sac6/fimbrin, the one other actin patch component that contains CH domains. Purified Scp1 binds directly to filamentous actin, cross-links actin filaments, and stabilizes filaments against disassembly. Sequences in Scp1 sufficient for actin binding and cross-linking reside in its carboxy terminus, outside the CH domain. Overexpression of SCP1 suppresses sac6Delta defects, and deletion of SCP1 enhances sac6Delta defects. Together, these data show that Scp1 and Sac6/fimbrin cooperate to stabilize and organize the yeast actin cytoskeleton.
引用
收藏
页码:2617 / 2629
页数:13
相关论文
共 56 条
[1]   REQUIREMENT OF YEAST FIMBRIN FOR ACTIN ORGANIZATION AND MORPHOGENESIS INVIVO [J].
ADAMS, AEM ;
BOTSTEIN, D ;
DRUBIN, DG .
NATURE, 1991, 354 (6352) :404-408
[2]  
[Anonymous], 1991, Methods Enzymol, V194, P1
[3]   High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A [J].
Ayscough, KR ;
Stryker, J ;
Pokala, N ;
Sanders, M ;
Crews, P ;
Drubin, DG .
JOURNAL OF CELL BIOLOGY, 1997, 137 (02) :399-416
[4]  
Babb SG, 1997, CELL MOTIL CYTOSKEL, V37, P308
[5]   FIMBRIN IS A CYTOSKELETAL PROTEIN THAT CROSSLINKS F-ACTIN INVITRO [J].
BRETSCHER, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (11) :6849-6853
[6]   MULTIFUNCTIONAL YEAST HIGH-COPY-NUMBER SHUTTLE VECTORS [J].
CHRISTIANSON, TW ;
SIKORSKI, RS ;
DANTE, M ;
SHERO, JH ;
HIETER, P .
GENE, 1992, 110 (01) :119-122
[7]   Integrating the actin and vimentin cytoskeletons: Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages [J].
Correia, I ;
Chu, D ;
Chou, YH ;
Goldman, RD ;
Matsudaira, P .
JOURNAL OF CELL BIOLOGY, 1999, 146 (04) :831-842
[8]   Movement of yeast cortical actin cytoskeleton visualized in vivo [J].
Doyle, T ;
Botstein, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (09) :3886-3891
[9]   YEAST ACTIN-BINDING PROTEINS - EVIDENCE FOR A ROLE IN MORPHOGENESIS [J].
DRUBIN, DG ;
MILLER, KG ;
BOTSTEIN, D .
JOURNAL OF CELL BIOLOGY, 1988, 107 (06) :2551-2561
[10]   An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast [J].
Epp, JA ;
Chant, J .
CURRENT BIOLOGY, 1997, 7 (12) :921-929