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Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress
Olga Voloshin Yana Gocheva Marina Gutnick Natalia Movshovich Anya Bakhrat Keren Baranes-Bachar Dudy Bar-Zvi Ruti Parvari Larisa Gheber Dina Raveh 《Cellular and molecular life sciences : CMLS》2010,67(12):2025-2038
Mutation of tubulin chaperone E (TBCE) underlies hypoparathyroidism, retardation, and dysmorphism (HRD) syndrome with defective
microtubule (MT) cytoskeleton. TBCE/yeast Pac2 comprises CAP-Gly, LRR (leucine-rich region), and UbL (ubiquitin-like) domains.
TBCE folds α-tubulin and promotes α/β dimerization. We show that Pac2 functions in MT dynamics: the CAP-Gly domain binds α-tubulin
and MTs, and functions in suppression of benomyl sensitivity of pac2Δ mutants. Pac2 binds proteasomes: the LRR binds Rpn1, and the UbL binds Rpn10; the latter interaction mediates Pac2 turnover.
The UbL also binds the Skp1-Cdc53-F-box (SCF) ubiquitin ligase complex; these competing interactions for the UbL may impact
on MT dynamics. pac2Δ mutants are sensitive to misfolded protein stress. This is suppressed by ectopic PAC2 with both the CAP-Gly and UbL domains being essential. We propose a novel role for Pac2 in the misfolded protein stress response
based on its ability to interact with both the MT cytoskeleton and the proteasomes. 相似文献
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