NDLI: Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative $Ca^{2+}$ entry, mitochondrial perturbation and caspase overactivation

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Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative $Ca^{2+}$ entry, mitochondrial perturbation and caspase overactivation

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Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative $Ca^{2+}$ entry, mitochondrial perturbation and caspase overactivation

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lin, Y-F Lee, Y-F Liang, P-H
Description	Author Affiliation: Lin YF ( Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan, ROC.)
Abstract	We have previously demonstrated that interrupting the protein-protein interaction (PPI) of ß-tubulin:chaperonin-containing TCP-1ß (CCT-ß) induces the selective killing of multidrug-resistant cancer cells due to CCT-ß overexpression. However, the molecular mechanism has not yet been identified. In this study, we found that CCT-ß interacts with a myriad of intracellular proteins involved in the cellular functions of the endoplasmic reticulum (ER), mitochondria, cytoskeleton, proteasome and apoptosome. Our data show that the targeted cells activate both the heat-shock protein 90 (Hsp90)-associated protein ubiquitination/degradation pathway to eliminate misfolded proteins in the cytoplasm and the valosin-containing protein (VCP)-centered ER-associated protein degradation pathway to reduce the excessive levels of unfolded polypeptides from the ER, thereby mitigating ER stress, at the onset of ß-tubulin:CCT-ß complex disruption. Once ER stress is expanded, ER stress-associated apoptotic signaling is enforced, as exhibited by cellular vacuolization and intracellular Ca2+ release. Furthermore, the elevated intracellular Ca2+ levels resulting from capacitative Ca2+ entry augments apoptotic signaling by provoking mitochondrial perturbation and caspase overactivation in the targeted cells. These findings not only provide a detailed picture of the apoptotic signaling cascades evoked by targeting the ß-tubulin:CCT-ß complex but also demonstrate a strategy to combat malignancies with chemoresistance to Hsp90- and VCP-related anticancer agents.
File Format	HTM / HTML
e-ISSN	20414889
DOI	10.1038/cddis.2012.173
Journal	Cell Death and Disease
Volume Number	3
Language	English
Publisher	Nature Publishing Group
Publisher Date	2012-11-29
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Cell Line Calcium Chaperonin Containing Tcp-1 Hsp90 Heat-shock Proteins Endoplasmic Reticulum-associated Degradation Endoplasmic Reticulum Metabolism Discipline Cell Biology Mitochondria Tubulin Adenosine Triphosphatases Proteolysis Endoplasmic Reticulum Stress Protein Binding Genetics Caspases Cell Cycle Proteins Apoptosis
Content Type	Text
Resource Type	Article

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