Identification of a motif in BMRP required for interaction with Bcl-2 by site-directed mutagenesis studies

Journal of Cellular Biochemistry

Volumn 113, Issue 11, 2012, Pages 3498-3508

  Conde, Juan A ^a   Claunch, Cheryl J ^a   Romo, Hannah E ^a   Benito Martín, Ana ^a   Ballestero, Rafael P ^a   González García, Maribel ^a  

^a TEXAS A AND M UNIVERSITY KINGSVILLE   (United States)

Author keywords

APOPTOSIS; Bcl 2; BMRP; MITOCHONDRIA; RIBOSOME

Indexed keywords

ASPARTIC ACID; BMRP PROTEIN; CASPASE; PROTEIN BCL 2; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; BINDING SITE; CELL DEATH; CONTROLLED STUDY; DELETION MUTANT; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; ANIMALS; APOPTOSIS; ASPARTIC ACID; BINDING SITES; GENE EXPRESSION; HEK293 CELLS; HUMANS; MICE; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NIH 3T3 CELLS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-BCL-2; RIBOSOMAL PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; TRANSFECTION;

MAMMALIA;

EID: 84866511759     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.24226     Document Type: Article

References (50)

1. Adams JM, Cory S,. 2001. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci 26: 61-66.
2. Adams JM, Cory S,. 2007. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 26: 1324-1337.
3. Akao Y, Otsuki Y, Kataoka S, Ito Y, Tsujimoto Y,. 1994. Multiple subcellular localization of bcl-2: Detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes. Cancer Res 54: 2468-2471.
4. Ballestero RP, Wilmot GR, Agranoff BW, Uhler MD,. 1997. gRICH68 and gRICH70 are 2',3'-cyclic-nucleotide 3'-phosphodiesterases induced during goldfish optic nerve regeneration. J Biol Chem 272: 11479-11486.
5. Banker GA, Cotman CW,. 1972. Measurement of free electrophoretic mobility and retardation coefficient of protein-sodium dodecyl sulfate complexes by gel electrophoresis. A method to validate molecular weight estimates. J Biol Chem 247: 5856-5861.
6. Barinaga M,. 1998a. Is apoptosis key in Alzheimer's disease ? Science 281: 1303-1304.
7. Barinaga M,. 1998b. Stroke-damaged neurons may commit cellular suicide. Science 281: 1302-1303.
8. Cavdar Koc E, Ranasinghe A, Burkhart W, Blackburn K, Koc H, Moseley A, Spremulli LL,. 2001. A new face on apoptosis: Death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins. FEBS Lett 492: 166-170.
9. Chintharlapalli SR, Jasti M, Malladi S, Parsa KV, Ballestero RP, Gonzalez-Garcia M,. 2005. BMRP is a Bcl-2 binding protein that induces apoptosis. J Cell Biochem 94: 611-626.
10. Danial NN, Korsmeyer SJ,. 2004. Cell death: Critical control points. Cell 116: 205-219.
11. del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G,. 1997. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278: 687-689.
12. Dorstyn L, Kumar S,. 1997. Differential inhibitory effects of CrmA, P35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli. Cell Death Differ 4: 570-579.
13. Fesik SW,. 2005. Promoting apoptosis as a strategy for cancer drug discovery. Nat Rev Cancer 5: 876-885.
14. Garcia-Ortega L, De los Rios, Martinez-Ruiz V, Onaderra A, Lacadena M, Martinez J, del Pozo A, Gavilanes JG,. 2005. Anomalous electrophoretic behavior of a very acidic protein: Ribonuclease U2. Electrophoresis 26: 3407-3413.
15. Gotow T, Shibata M, Kanamori S, Tokuno O, Ohsawa Y, Sato N, Isahara K, Yayoi Y, Watanabe T, Leterrier JF, Linden M, Kominami E, Uchiyama Y,. 2000. Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells. Cell Death Differ 7: 666-674.
16. Green DR, Evan GI,. 2002. A matter of life and death. Cancer Cell 1: 19-30.
17. Hanada M, Aime-Sempe C, Sato T, Reed JC,. 1995. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J Biol Chem 270: 11962-11969.
18. Huang DC, Adams JM, Cory S,. 1998. The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J 17: 1029-1039.
19. Hunter JJ, Bond BL, Parslow TG,. 1996. Functional dissection of the human Bc12 protein: Sequence requirements for inhibition of apoptosis. Mol Cell Biol 16: 877-883.
20. Innis MA, Gelfand DH, Sninsky JJ, White TJ,. 1990. PCR protocols: A guide to methods and applications. San Diego: Academic Press. p xviii, 482 p.
21. Jacobson MD, Weil M, Raff MC,. 1997. Programmed cell death in animal development. Cell 88: 347-354.
22. Khanna N, Reddy VG, Tuteja N, Singh N,. 2000. Differential gene expression in apoptosis: Identification of ribosomal protein S29 as an apoptotic inducer. Biochem Biophys Res Commun 277: 476-486.
23. Kim MJ, Yoo YA, Kim HJ, Kang S, Kim YG, Kim JS, Yoo YD,. 2005. Mitochondrial ribosomal protein L41 mediates serum starvation-induced cell-cycle arrest through an increase of p21(WAF1/CIP1). Biochem Biophys Res Commun 338: 1179-1184.
24. Kim HR, Chae HJ, Thomas M, Miyazaki T, Monosov A, Monosov E, Krajewska M, Krajewski S, Reed JC,. 2007. Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis. FASEB J 21: 188-196.
25. Kissil JL, Cohen O, Raveh T, Kimchi A,. 1999. Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death. EMBO J 18: 353-362.
26. Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD,. 1997. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 275: 1132-1136.
27. Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC,. 1993. Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res 53: 4701-4714.
28. Lemmon MA, Schlessinger J,. 2010. Cell signaling by receptor tyrosine kinases. Cell 141: 1117-1134.
29. Lindstrom MS,. 2009. Emerging functions of ribosomal proteins in gene-specific transcription and translation. Biochem Biophys Res Commun 379: 167-170.
30. Lucken-Ardjomande S, Martinou JC,. 2005. Regulation of Bcl-2 proteins and of the permeability of the outer mitochondrial membrane. C R Biol 328: 616-631.
31. Malladi S, Parsa KV, Bhupathi D, Rodriguez-Gonzalez MA, Conde JA, Anumula P, Romo HE, Claunch CJ, Ballestero RP, Gonzalez-Garcia M,. 2011. Deletion mutational analysis of BMRP, a pro-apoptotic protein that binds to Bcl-2. Mol Cell Biochem 351: 217-232.
32. Mattson MP,. 2000. Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol 1: 120-129.
33. Monaghan P, Robertson D, Amos TA, Dyer MJ, Mason DY, Greaves MF,. 1992. Ultrastructural localization of bcl-2 protein. J Histochem Cytochem 40: 1819-1825.
34. Mukamel Z, Kimchi A,. 2004. Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death. J Biol Chem 279: 36732-36738.
35. Naora H, Takai I, Adachi M, Naora H,. 1998. Altered cellular responses by varying expression of a ribosomal protein gene: Sequential coordination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis. J Cell Biol 141: 741-753.
36. Raff MC,. 1992. Social controls on cell survival and cell death. Nature 356: 397-400.
37. Rathmell JC, Thompson CB,. 2002. Pathways of apoptosis in lymphocyte development, homeostasis, and disease. Cell 109 (Suppl.): S97-S107.
38. Reed JC,. 1994. Bcl-2 and the regulation of programmed cell death. J Cell Biol 124: 1-6.
39. Rong YP, Barr P, Yee VC, Distelhorst CW,. 2009. Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor. Biochim Biophys Acta 1793: 971-978.
40. Sambrook J, Russell DW,. 2001. Molecular cloning: A laboratory manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. p 3v.
41. Schenning M, van Tiel CM, Van Manen D, Stam JC, Gadella BM, Wirtz KW, Snoek GT,. 2004. Phosphatidylinositol transfer protein alpha regulates growth and apoptosis of NIH3T3 cells: Involvement of a cannabinoid 1-like receptor. J Lipid Res 45: 1555-1564.
42. Strasser A, O'Connor L, Dixit VM,. 2000. Apoptosis signaling. Annu Rev Biochem 69: 217-245.
43. Tang T, Zheng B, Chen SH, Murphy AN, Kudlicka K, Zhou H, Farquhar MG,. 2009. hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis. J Biol Chem 284: 5414-5424.
44. Vaux DL, Cory S, Adams JM,. 1988. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature 335: 440-442.
45. Warner JR, McIntosh KB,. 2009. How common are extraribosomal functions of ribosomal proteins ? Mol Cell 34: 3-11.
46. Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ,. 1995. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80: 285-291.
47. Yoo YA, Kim MJ, Park JK, Chung YM, Lee JH, Chi SG, Kim JS, Yoo YD,. 2005. Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1. Mol Cell Biol 25: 6603-6616.
48. Youle RJ, Strasser A,. 2008. The BCL-2 protein family: Opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59.
49. Zhong LT, Sarafian T, Kane DJ, Charles AC, Mah SP, Edwards RH, Bredesen DE,. 1993. bcl-2 inhibits death of central neural cells induced by multiple agents. Proc Natl Acad Sci USA 90: 4533-4537.
50. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X,. 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90: 405-413.