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Proteasome-dependent degradation of cytosolic chaperonin CCT.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yokota S,Kayano T,Ohta T,Kurimoto M,Yanagi H,Yura T,Kubota H

doi

10.1006/bbrc.2000.4011

subject

Has Abstract

pub_date

2000-12-20 00:00:00

pages

712-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X00940117

journal_volume

279

pub_type

杂志文章

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