Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.

被引:122
作者
Brackley, Karen I. [1 ]
Grantham, Julie [1 ]
机构
[1] Univ Gothenburg, Dept Cell & Mol Biol, S-40530 Gothenburg, Sweden
关键词
CCT chaperonin; Cytoskeleton; Cell cycle; Actin; Tubulin; ANAPHASE-PROMOTING COMPLEX; CYTOSOLIC CHAPERONIN; EUKARYOTIC CHAPERONIN; CYTOPLASMIC CHAPERONIN; SACCHAROMYCES-CEREVISIAE; MOLECULAR CHAPERONES; SUBUNIT COMPOSITION; MEDIATED ACTIN; BINDING-SITES; ALPHA-TUBULIN;
D O I
10.1007/s12192-008-0057-x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The chaperonin containing TCP-1 (CCT) is required for the production of native actin and tubulin and numerous other proteins, several of which are involved in cell cycle progression. The mechanistic details of how CCT acts upon its folding substrates are intriguing: whilst actin and tubulin bind in a sequence-specific manner, it is possible that some proteins could use CCT as a more general binding interface. Therefore, how CCT accommodates the folding requirements of its substrates, some of which are produced in a cell cycle-specific manner, is of great interest. The reliance of folding substrates upon CCT for the adoption of their native structures results in CCT activity having far-reaching implications for a vast array of cellular processes. For example, the dependency of the major cytoskeletal proteins actin and tubulin upon CCT results in CCT activity being linked to any cellular process that depends on the integrity of the microfilament and microtubule-based cytoskeletal systems.
引用
收藏
页码:23 / 31
页数:9
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