메뉴 건너뛰기




Volumn 270, Issue 2, 2003, Pages 342-349

The resident endoplasmic reticulum protein, BAP31, associates with γ-actin and myosin B heavy chain: Analysis by capillary liquid chromatography microelectrospray tandem MS

Author keywords

Apoptosis; BAP31; Mass spectrometry; Post translational modifications

Indexed keywords

ACTIN; CELL PROTEIN; FAS ANTIGEN; GAMMA ACTIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; NONMUSCLE MYOSIN B HEAVY CHAIN; PROTEIN BAP31; UNCLASSIFIED DRUG;

EID: 0037240794     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03395.x     Document Type: Article
Times cited : (26)

References (20)
  • 1
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D.W. (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6, 1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 2
    • 0028146863 scopus 로고
    • A new human gene (DXS1357E) with ubiquitous expression, located in Xq28 adjacent to the adrenoleukodystrophy gene
    • Mosser, J., Sarde, C.O., Vicaire, S., Yates, J.R. & Mandel, J.L. (1994) A new human gene (DXS1357E) with ubiquitous expression, located in Xq28 adjacent to the adrenoleukodystrophy gene. Genomics 22, 469-471.
    • (1994) Genomics , vol.22 , pp. 469-471
    • Mosser, J.1    Sarde, C.O.2    Vicaire, S.3    Yates, J.R.4    Mandel, J.L.5
  • 3
    • 0029925943 scopus 로고    scopus 로고
    • The specificity of association of the IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD transmembrane sequence
    • Adachi, T., Schamel, W.W., Kim, K.M., Watanabe, T., Becker, B., Nielsen, P.J. & Reth, M. (1996) The specificity of association of the IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD transmembrane sequence. EMBO J. 15, 1534-1541.
    • (1996) EMBO J. , vol.15 , pp. 1534-1541
    • Adachi, T.1    Schamel, W.W.2    Kim, K.M.3    Watanabe, T.4    Becker, B.5    Nielsen, P.J.6    Reth, M.7
  • 5
    • 0031452943 scopus 로고    scopus 로고
    • Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31
    • Annaert, W.G., Becker, B., Kistner, U., Reth, M. & Jahn, R. (1997) Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31. J. Cell Biol. 139, 1397-1410.
    • (1997) J. Cell Biol. , vol.139 , pp. 1397-1410
    • Annaert, W.G.1    Becker, B.2    Kistner, U.3    Reth, M.4    Jahn, R.5
  • 7
    • 0035827636 scopus 로고    scopus 로고
    • Control of cystic fibrosis transmembrane conductance regulator expression by BAP31
    • Lambert, G., Becker, B., Schreiber, R., Boucherot, A., Reth, M. & Kunzelmann, K. (2001) Control of cystic fibrosis transmembrane conductance regulator expression by BAP31. J. Biol. Chem. 276, 20340-20345.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20340-20345
    • Lambert, G.1    Becker, B.2    Schreiber, R.3    Boucherot, A.4    Reth, M.5    Kunzelmann, K.6
  • 8
    • 0037007141 scopus 로고    scopus 로고
    • The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
    • Breckenridge, D.G., Nguyen, M., Kuppig, S., Reth, M. & Shore, G.C. (2002) The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 99, 4331-4336.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4331-4336
    • Breckenridge, D.G.1    Nguyen, M.2    Kuppig, S.3    Reth, M.4    Shore, G.C.5
  • 9
    • 0033816610 scopus 로고    scopus 로고
    • Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria
    • Nguyen, M., Breckenridge, D.G., Ducret, A. & Shore, G.C. (2000) Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol. Cell. Biol. 20, 6731-6740.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6731-6740
    • Nguyen, M.1    Breckenridge, D.G.2    Ducret, A.3    Shore, G.C.4
  • 10
    • 0022516684 scopus 로고
    • Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod
    • Strehler, E.E., Strehler-Page, M.A., Perriard, J.C., Periasamy, M. & Nadal-Ginard, B. (1986) Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod. J. Mol. Biol. 190, 291-317.
    • (1986) J. Mol. Biol. , vol.190 , pp. 291-317
    • Strehler, E.E.1    Strehler-Page, M.A.2    Perriard, J.C.3    Periasamy, M.4    Nadal-Ginard, B.5
  • 11
    • 0033598155 scopus 로고    scopus 로고
    • Extranuclear apoptosis. The role of the cytoplasm in the execution phase
    • Mills, J.C., Stone, N.L. & Pittman, R.N. (1999) Extranuclear apoptosis. The role of the cytoplasm in the execution phase. J. Cell Biol. 146, 703-708.
    • (1999) J. Cell Biol. , vol.146 , pp. 703-708
    • Mills, J.C.1    Stone, N.L.2    Pittman, R.N.3
  • 12
    • 0028983813 scopus 로고
    • Improvement of an 'In-Gel' digestion procedure for the micro-preparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Gonez, J. & Heldin, C.H. (1995) Improvement of an 3In-Gel3 digestion procedure for the micro-preparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224, 451-455.
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 13
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret, A., Van Oostveen, I., Eng, J.K., Yates, J.R., 3rd & Aebersold, R. (1998) High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sci. 7, 706-719.
    • (1998) Protein Sci. , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates J.R. III4    Aebersold, R.5
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J., McCormack, A.L. & Yates, J.R. III. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Mass Spectrom. 5, 976-989.
    • (1994) J. Am. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.L.2    Yates J.R. III3
  • 15
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J.R. III, Eng, J.K., McCormack, A.L. & Schieltz, D. (1995) Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67, 1426-1436.
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates J.R. III1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 16
    • 0026618996 scopus 로고
    • Preincubation with cysteine prevents modification of sulf-hydryl groups in proteins by unreacted acrylamide in a gel
    • Chiari, M., Righetti, P.G., Negri, A., Ceciliani, F. & Ronchi, S. (1992) Preincubation with cysteine prevents modification of sulf-hydryl groups in proteins by unreacted acrylamide in a gel. Electrophoresis 13, 882-844.
    • (1992) Electrophoresis , vol.13 , pp. 882-844
    • Chiari, M.1    Righetti, P.G.2    Negri, A.3    Ceciliani, F.4    Ronchi, S.5
  • 18
    • 0032488661 scopus 로고    scopus 로고
    • Bcl-XL cooperatively associates with the Bap31 complex in the endoplasmic reticulum, dependent on procaspase-8 and Ced-4 adaptor
    • Ng, F.W. & Shore, G.C. (1998) Bcl-XL cooperatively associates with the Bap31 complex in the endoplasmic reticulum, dependent on procaspase-8 and Ced-4 adaptor. J. Biol. Chem. 273, 327-338.
    • (1998) J. Biol. Chem. , vol.273 , pp. 327-338
    • Ng, F.W.1    Shore, G.C.2
  • 19
    • 0034711184 scopus 로고    scopus 로고
    • Nα-terminal acetylation of eukaryotic proteins
    • Polevoda, B. & Sherman, F. (2000) Na-terminal acetylation of eukaryotic proteins. J. Biol. Chem. 275, 36479-36482.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 20
    • 0034607086 scopus 로고    scopus 로고
    • Acetylation at the N-terminus of actin strengthens weak interaction between actin and myosin
    • Abe, A., Saeki, K., Yasunaga, T. & Wakabayashi, T. (2000) Acetylation at the N-terminus of actin strengthens weak interaction between actin and myosin. Biochem. Biophys. Res. Commun. 268, 14-19.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 14-19
    • Abe, A.1    Saeki, K.2    Yasunaga, T.3    Wakabayashi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.