Anaphase-Promoting Complex/Cyclosome Participates in the Acute Response to Protein-Damaging Stress

被引:32
作者
Ahlskog, Johanna K.
Bjork, Johanna K.
Elsing, Alexandra N.
Aspelin, Camilla
Kallio, Marko [2 ]
Roos-Mattjus, Pia
Sistonen, Lea [1 ]
机构
[1] Abo Akad Univ, Turku Ctr Biotechnol, Dept Biosci, FIN-20520 Turku, Finland
[2] VTT Tech Res Ctr Finland, Turku 20520, Finland
基金
芬兰科学院;
关键词
SHOCK TRANSCRIPTION FACTOR-1; CELL-CYCLE; FACTOR-I; DEPENDENT DEGRADATION; POLYUBIQUITIN CHAINS; SPINDLE CHECKPOINT; PROTEOTOXIC STRESS; UBIQUITIN CHAINS; MITOTIC EXIT; HELA-CELLS;
D O I
10.1128/MCB.01506-09
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ubiquitin E3 ligase anaphase-promoting complex/cyclosome (APC/C) drives degradation of cell cycle regulators in cycling cells by associating with the coactivators Cdc20 and Cdh1. Although a plethora of APC/C substrates have been identified, only a few transcriptional regulators are described as direct targets of APC/C-dependent ubiquitination. Here we show that APC/C, through substrate recognition by both Cdc20 and Cdh1, mediates ubiquitination and degradation of heat shock factor 2 (HSF2), a transcription factor that binds to the Hsp70 promoter. The interaction between HSF2 and the APC/C subunit Cdc27 and coactivator Cdc20 is enhanced by moderate heat stress, and the degradation of HSF2 is induced during the acute phase of the heat shock response, leading to clearance of HSF2 from the Hsp70 promoter. Remarkably, Cdc20 and the proteasome 20S core alpha 2 subunit are recruited to the Hsp70 promoter in a heat shock-inducible manner. Moreover, the heat shock-induced expression of Hsp70 is increased when Cdc20 is silenced by a specific small interfering RNA (siRNA). Our results provide the first evidence for participation of APC/C in the acute response to protein-damaging stress.
引用
收藏
页码:5608 / 5620
页数:13
相关论文
共 106 条
[11]   Nuclear stress bodies: a heterochromatin affair? [J].
Biamonti, G .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2004, 5 (06) :493-498
[12]   AML1/RUNX1 phosphorylation by cyclin-dependent kinases regulates the degradation of AML1/RUNX1 by the anaphase-promoting complex [J].
Biggs, Joseph R. ;
Peterson, Luke F. ;
Zhang, Youhong ;
Kraft, Andrew S. ;
Zhang, Dong-Er .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (20) :7420-7429
[13]   miR-18, a member of Oncomir-1, targets heat shock transcription factor 2 in spermatogenesis [J].
Bjork, Johanna K. ;
Sandqvist, Anton ;
Elsing, Alexandra N. ;
Kotaja, Noora ;
Sistonen, Lea .
DEVELOPMENT, 2010, 137 (19) :3177-3184
[14]   Role of heat-shock factor 2 in cerebral cortex formation and as a regulator of p35 expression [J].
Chang, YH ;
Östling, P ;
Åkerfelt, M ;
Trouillet, D ;
Rallu, M ;
Gitton, Y ;
El Fatilmy, R ;
Fardeau, V ;
Le Crom, S ;
Morange, M ;
Sistonen, L ;
Mezger, V .
GENES & DEVELOPMENT, 2006, 20 (07) :836-847
[15]   Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains [J].
Chastagner, Patricia ;
Israel, Alain ;
Brou, Christel .
EMBO REPORTS, 2006, 7 (11) :1147-1153
[16]   Proteolysis: from the lysosome to ubiquitin and the proteasome [J].
Ciechanover, A .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2005, 6 (01) :79-86
[17]   UBIQUITIN DEPENDENCE OF SELECTIVE PROTEIN-DEGRADATION DEMONSTRATED IN THE MAMMALIAN-CELL CYCLE MUTANT TS85 [J].
CIECHANOVER, A ;
FINLEY, D ;
VARSHAVSKY, A .
CELL, 1984, 37 (01) :57-66
[18]   Temporal and spatial control of cyclin B1 destruction in metaphase [J].
Clute, P ;
Pines, J .
NATURE CELL BIOLOGY, 1999, 1 (02) :82-87
[19]   Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation [J].
Corey, LL ;
Weirich, CS ;
Benjamin, IJ ;
Kingston, RE .
GENES & DEVELOPMENT, 2003, 17 (11) :1392-1401
[20]   Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation [J].
Cripps, D ;
Thomas, SN ;
Jeng, Y ;
Yang, F ;
Davies, P ;
Yang, AJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (16) :10825-10838