NDLI: Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress

Content Provider	Springer Nature Link
Author	Voloshin, Olga Gocheva, Yana Gutnick, Marina Movshovich, Natalia Bakhrat, Anya Baranes Bachar, Keren Bar Zvi, Dudy Parvari, Ruti Gheber, Larisa Raveh, Dina
Copyright Year	2010
Abstract	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.
Starting Page	2025
Ending Page	2038
Page Count	14
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	67
Issue Number	12
e-ISSN	14209071
Language	English
Publisher	SP Birkhäuser Verlag Basel
Publisher Date	2010-03-04
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Pac2 CAP-Gly Ubiquitin-like domain Rpn1 Rpn10 Proteasome TBCE Biochemistry Life Sciences Biomedicine general Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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