RRC ID 39527
Author Yokota S, Kayano T, Ohta T, Kurimoto M, Yanagi H, Yura T, Kubota H.
Title Proteasome-dependent degradation of cytosolic chaperonin CCT.
Journal Biochem Biophys Res Commun
Abstract The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We show here that degradation of CCT in mammalian cells is inhibited by a proteasome-specific inhibitor, lactacystin. When CCT synthesis was inhibited by growth arrest of cells, the decrease in CCT levels was much slower in the presence of lactacystin than in its absence. Pulse-chase experiments indicated that degradation of CCT is inhibited 2- to 2.5-fold by addition of lactacystin. In addition, CCT degradation rate in ts85 cells that produce thermolabile ubiquitin-activating enzyme E1 was reduced 3-fold at the nonpermissive temperature compared to the degradation at the permissive temperature. These results indicate that the ubiquitin-proteasome system is involved in CCT degradation.
Volume 279(2)
Pages 712-7
Published 2000-12-20
DOI 10.1006/bbrc.2000.4011
PII S0006291X00940117
PMID 11118350
MeSH Acetylcysteine / analogs & derivatives* Acetylcysteine / pharmacology Adenosine Triphosphatases / metabolism Animals Cell Division Chaperonin Containing TCP-1 Chaperonins / metabolism* Cysteine Endopeptidases / metabolism* Cysteine Proteinase Inhibitors / pharmacology Cytosol / metabolism Enzyme Stability Female Kinetics Ligases / metabolism Mammary Neoplasms, Experimental Mice Multienzyme Complexes / metabolism* Multiple Myeloma Protease Inhibitors / pharmacology Proteasome Endopeptidase Complex Temperature Thermodynamics Tumor Cells, Cultured Ubiquitin-Activating Enzymes Ubiquitin-Protein Ligases
IF 2.985
Times Cited 12
Human and Animal Cells DA-3(RCB1144) WEHI-3(RCB0035) FM3A(RCB0086)