HS 1-Associated protein X-1 is cleaved by Caspase-3 during apoptosis

Molecules and Cells

Volumn 25, Issue 1, 2008, Pages 86-90

  Lee, Ah Young ^a   Lee, Yoora ^a   Park, Yun Kyung ^a   Bae, Kwang Hee ^a   Cho, Sayeon ^b   Lee, Do Hee ^a   Park, Byoung Chul ^a   Kang, Sunghyun ^a   Park, Sung Goo ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Chung Ang University   (South Korea)

Author keywords

Apoptosis; Caspase 3; HAX 1

Indexed keywords

ASPARAGINE; CASPASE 3; ETOPOSIDE; HS 1 ASSOCIATED PROTEIN X 1; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN HAX1;

AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SUBSTRATE; FEMALE; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; IN VITRO STUDY; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN FUNCTION;

APOPTOSIS; ASPARTIC ACID; BLOOD PROTEINS; CASPASE 3; CELL LINE; HUMANS; PROTEINS;

EID: 42949130050     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

1. Bose, K. and Clark, A.C. (2005). pH effects on the stability and dimerization of procaspase-3. Protein.Sci. 14, 24-36.
2. Cilenti, L., Soundarapandian, M.M., Kyriazis, G.A., Stratico, V., Singh, S., Gupta, S., Bonventre, J.V., Alnemri, E.S., and Zervos, A.S. (2004). Regulation of HAX-1 anti-apoptotic protein by Omi/HtrA2 protease during cell death. J. Biol. Chem. 279, 50295-50301.
3. Cohen, G.M. (1997). Caspases: the executioners of apoptosis. Biochem. J. 326 (Pt 1), 1-16.
4. Deveraux, Q.L., Leo, E., Stennicke, H.R., Welsh, K., Salvesen, G.S., and Reed, J.C. (1999). Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J. 18, 5242-5251.
5. Deveraux, Q.L., Takahashi, R., Salvesen, G.S., and Reed, J.C. (1997). X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388, 300-304.
6. Earnshaw, W.C., Martins, L.M., and Kaufmann, S.H. (1999). Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424.
7. Gross, A., McDonnell, J.M., and Korsmeyer, S.J. (1999). BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13, 1899-1911.
8. Han, Y., Chen, Y.S., Liu, Z., Bodyak, N., Rigor, D., Bisping, E., Pu, W.T., and Kang, P.M. (2006). Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition. Circ. Res. 99, 415-423.
9. Hengartner, M.O. (2000). The biochemistry of apoptosis. Nature 407, 770-776.
10. Janicke, R.U., Sprengart, M.L., Wati, M.R., and Porter, A.G. (1998). Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273, 9357-9360.
11. Kroemer, G. and Reed, J.C. (2000). Mitochondrial control of cell death. Nat. Med. 6, 513-519.
12. Lee, A.Y., Park, B.C., Jang, M., Cho, S., Lee, D.H., Lee, S.C., Myung, P.K., and Park, S.G. (2004). Identification of caspase-3 degradome by two-dimensional get electrophoresis and matrix-assisted laser desorption/ ionization-time of flight' analysis. Proteomics 4, 3429-3436.
13. Mancini, M., Nicholson, D.W., Roy, S., Thornberry, N.A., Peterson, E.P., Casciola-Rosen, L.A., and Rosen, A. (1998). The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling. J. Cell Biol. 140, 1485-1495.
14. Maravei, D.V., Trbovich, A.M., Perez, G.I., Tilly, K.I., Banach, D., Talanian, R.V., Wong, W.W., and Tilly, J.L. (1997). Cleavage of cytoskeletal proteins by caspases during ovarian cell death: evidence that cell-free systems do not always mimic apoptotic events in intact cells. Cell Death Differ. 4, 707-712.
15. Mattson, M.P. (2000). Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1, 120-129.
16. Sharp, T.V., Wang, H.W., Koumi, A., Hollyman, D., Endo, Y., Ye, H., Du, M.Q., and Boshoff, C. (2002). K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function. J. Virol. 76, 802-816.
17. Suzuki, Y., Demoliere, C., Kitamura, D., Takeshita, H., Deuschle, U., and Watanabe, T. (1997). HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases. J. Immunol. 158, 2736-2744.
18. Tamm, I., Kornblau, S.M., Segall, H., Krajewski, S., Welsh, K., Kitada, S., Scudiero, D.A., Tudor, G., Qui, Y.H., Monks, A., et al. (2000). Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin. Cancer Res. 6, 1796-1803.
19. Thornberry, N.A. and Lazebnik, Y. (1999). Caspases: enemies within. Science 281, 1312-1316.
20. Yamanashi, Y., Fukuda, T., Nishizumi, H., Inazu, T., Higashi, K., Kitamura, D., Ishida, T., Yamamura, H., Watanabe, T., and Yamamoto, T. (1997). Role of tyrosine phosphorylation of HS1 in B cell antigen receptor-mediated apoptosis. J. Exp. Med. 185, 1387-1392.
21. Yedavalli, V.S., Shih, H.M, Chiang, Y.P., Lu, C.Y., Chang, L.Y., Chen, M.Y., Chuang, C.Y., Dayton, A.I., Jeang, K.T., and Huang, L.M. (2005). Human immunodeficiency virus type 1 Vpr interacts with antiapoptotic mitochondrial protein HAX-1. J. Virol. 79, 13735-13746.
22. Zhao, X., Fan, Y., Shen, J., Wu, Y., and Yin, Z. (2006). Human glutathione S-transferase P1 suppresses MEKK1-mediated apoptosis by regulating MEKK1 kinase activity in HEK293 cells. Mol. Cells 21, 395-400.