RRC ID 39527
著者 Yokota S, Kayano T, Ohta T, Kurimoto M, Yanagi H, Yura T, Kubota H.
タイトル Proteasome-dependent degradation of cytosolic chaperonin CCT.
ジャーナル 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.
巻・号 279(2)
ページ 712-7
公開日 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
引用数 12
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
ヒト・動物細胞 DA-3(RCB1144) WEHI-3(RCB0035) FM3A(RCB0086)