Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative Ca2+ entry, mitochondrial perturbation and caspase overactivation-Reference-Cited by-同舟云学术

Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative Ca2+ entry, mitochondrial perturbation and caspase overactivation

Published:2012-11 Issue:11 Volume:3 Page:e434-e434
ISSN:2041-4889
Container-title:Cell Death & Disease
language:en
Short-container-title:Cell Death Dis

Author:

Lin Y-F,Lee Y-F,Liang P-H

Publisher

Springer Science and Business Media LLC

Subject

Cancer Research,Cell Biology,Cellular and Molecular Neuroscience,Immunology

Link

http://www.nature.com/articles/cddis2012173.pdf

Reference49 articles.

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2. Dekker C, Stirling PC, McCormack EA, Filmore H, Paul A, Brost RL et al. The interaction network of the chaperonin CCT. EMBO J 2008; 27: 1827–1839.

3. Rivenzon-Segal D, Wolf SG, Shimon L, Willison KR, Horovitz A . Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 2005; 12: 233–237.

4. Grantham J, Brackley KI, Willison KR . Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells. Exp Cell Res 2006; 312: 2309–2324.

5. Brackley KI, Grantham J . Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation. Cell Stress Chaperones 2009; 14: 23–31.

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