Literature search services are currently unavailable. During our hosting provider's UPS upgrade we experienced a hardware failure and are currently working to resolve the issue.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

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 alpha-tubulin and promotes alpha/beta dimerization. We show that Pac2 functions in MT dynamics: the CAP-Gly domain binds alpha-tubulin and MTs, and functions in suppression of benomyl sensitivity of pac2Delta 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. pac2Delta 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.

Pubmed ID: 20204449


  • Voloshin O
  • Gocheva Y
  • Gutnick M
  • Movshovich N
  • Bakhrat A
  • Baranes-Bachar K
  • Bar-Zvi D
  • Parvari R
  • Gheber L
  • Raveh D


Cellular and molecular life sciences : CMLS

Publication Data

June 27, 2010

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Cell Cycle Proteins
  • Cytoskeleton
  • Dimerization
  • F-Box Proteins
  • Humans
  • Hypoparathyroidism
  • Intellectual Disability
  • Microtubules
  • Molecular Chaperones
  • Mutation
  • Proteasome Endopeptidase Complex
  • Proteins
  • Syndrome
  • Tubulin
  • Ubiquitin
  • Ubiquitin-Protein Ligases