HSP70 protects BCL2L12 and BCL2L12A from N-terminal ubiquitination-mediated proteasomal degradation

FEBS Letters

Volumn 583, Issue 9, 2009, Pages 1409-1414

  Yang, Junwu ^a   Hong, Yi ^a   Wang, Wenzong ^a   Wu, Weibing ^a   Chi, Yayun ^a   Zong, Hongliang ^a   Kong, Xiangfei ^a   Wei, Yuanyan ^a   Yun, Xiaojing ^a   Cheng, Chunming ^a   Chen, Kangli ^a   Gu, Jianxin ^a  

^a FUDAN UNIVERSITY   (China)

Author keywords

BCL2L12; HSP70; Ubiquitination

Indexed keywords

BCL2L12 PROTEIN; BCL2L12A PROTEIN; HEAT SHOCK PROTEIN 70; LYSINE; PROTEIN BCL 2; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; EMBRYO; FEMALE; GENETIC TRANSCRIPTION; GENETIC VARIABILITY; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN INTERACTION; UBIQUITINATION;

AMINO ACID SEQUENCE; CELL LINE; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; IMMUNOPRECIPITATION; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN ISOFORMS; PROTO-ONCOGENE PROTEINS C-BCL-2; UBIQUITINATION;

MAMMALIA;

EID: 67349286173     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.04.011     Document Type: Article

References (25)

1. Thomadaki H., and Scorilas A. Breast cancer cells response to the antineoplastic agents cisplatin, carboplatin, and doxorubicin at the mRNA expression levels of distinct apoptosis-related genes, including the new member, BCL2L12. Ann. NY Acad. Sci. 1095 (2007) 35-44
2. Floros K.V., Thomadaki H., Lallas G., Katsaros N., Talieri M., and Scorilas A. Cisplatin-induced apoptosis in HL-60 human promyelocytic leukemia cells: differential expression of BCL2 and novel apoptosis-related gene BCL2L12. Ann. NY Acad. Sci. 1010 (2003) 153-158
3. Floros K.V., Talieri M., and Scorilas A. Topotecan and methotrexate alter expression of the apoptosis-related genes BCL2, FAS and BCL2L12 in leukemic HL-60 cells. Biol. Chem. 387 (2006) 1629-1633
4. Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
5. Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70 (2001) 503-533
6. Robinson P.A., and Ardley H.C. Ubiquitin-protein ligases. J. Cell Sci. 117 (2004) 5191-5194
7. Li R.F., Shang Y., Liu D., Ren Z.S., Chang Z., and Sui S.F. Differential ubiquitination of Smad1 mediated by CHIP: implications in the regulation of the bone morphogenetic protein signaling pathway. J. Mol. Biol. 374 (2007) 777-790
8. Weiss Y.G., Bromberg Z., Raj N., Raphael J., Goloubinoff P., Ben-Neriah Y., and Deutschman C.S. Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Crit. Care Med. 35 (2007) 2128-2138
9. Chen H., et al. Hsp70 inhibits lipopolysaccharide-induced NF-kappaB activation by interacting with TRAF6 and inhibiting its ubiquitination. FEBS Lett. 580 (2006) 3145-3152
10. Hong Y., et al. Knockdown of BCL2L12 leads to cisplatin resistance in MDA-MB-231 breast cancer cells. Biochim. Biophys. Acta 1782 (2008) 649-657
11. Chen S., et al. The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis. J. Biol. Chem. 278 (2003) 20029-20036
12. Wang H., Shen H., Wang Y., Li Z., Yin H., Zong H., Jiang J., and Gu J. Overexpression of small glutamine-rich TPR-containing protein promotes apoptosis in 7721 cells. FEBS Lett. 579 (2005) 1279-1284
13. Dell'Angelica E.C., Mullins C., Caplan S., and Bonifacino J.S. Lysosome-related organelles. FASEB J. 14 (2000) 1265-1278
14. Reinstein E., and Ciechanover A. Narrative review: protein degradation and human diseases: the ubiquitin connection. Ann. Intern. Med. 145 (2006) 676-684
15. Pollice A., Sepe M., Villella V.R., Tolino F., Vivo M., Calabro V., and La Mantia G. TBP-1 protects the human oncosuppressor p14ARF from proteasomal degradation. Oncogene 26 (2007) 5154-5162
16. Fenteany G., and Schreiber S.L. Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273 (1998) 8545-8548
17. Hartmann-Petersen R., Seeger M., and Gordon C. Transferring substrates to the 26S proteasome. Trends Biochem. Sci. 28 (2003) 26-31
18. Pickart C.M. Targeting of substrates to the 26S proteasome. FASEB J. 11 (1997) 1055-1066
19. Herrmann J., Lerman L.O., and Lerman A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ. Res. 100 (2007) 1276-1291
20. Ben-Saadon R., Fajerman I., Ziv T., Hellman U., Schwartz A.L., and Ciechanover A. The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue. J. Biol. Chem. 279 (2004) 41414-41421
21. Ciechanover A. N-terminal ubiquitination. Methods Mol. Biol. 301 (2005) 255-270
22. Ciechanover A., and Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 14 (2004) 103-106
23. Coulombe P., Rodier G., Bonneil E., Thibault P., and Meloche S. N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome. Mol. Cell Biol. 24 (2004) 6140-6150
24. Fajerman I., Schwartz A.L., and Ciechanover A. Degradation of the Id2 developmental regulator: targeting via N-terminal ubiquitination. Biochem. Biophys. Res. Commun. 314 (2004) 505-512
25. Bloom J., Amador V., Bartolini F., DeMartino G., and Pagano M. Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 115 (2003) 71-82