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Volumn 150, Issue 4, 2011, Pages 411-421

Calpain-7 binds to CHMP1B at its second α-helical region and forms a ternary complex with IST1

Author keywords

calpain; CHMP; ESCRT; IST1; MIT domain

Indexed keywords

CALPAIN; CALPAIN 7; CHARGED MULTIVESICULAR BODY PROTEIN; CHARGED MULTIVESICULAR BODY PROTEIN 1B; ESCRT PROTEIN; INCREASED SODIUM TOLERANCE 1; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 80053464365     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr071     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 36248991778 scopus 로고    scopus 로고
    • ESCRTing proteins in the endocytic pathway
    • DOI 10.1016/j.tibs.2007.09.010, PII S0968000407002617
    • Saksena, S., Sun, J., Chu, T., and Emr, S.D. (2007) ESCRTing proteins in the endocytic pathway. Trends. Biochem. Sci. 32, 561-573 (Pubitemid 350123053)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.12 , pp. 561-573
    • Saksena, S.1    Sun, J.2    Chu, T.3    Emr, S.D.4
  • 2
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • DOI 10.1038/nrm2162, PII NRM2162
    • Williams, R.L. and Urbé, S. (2007) The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell. Biol. 8, 355-368 (Pubitemid 46643239)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 3
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRT machinery in viral budding and cytokinesis
    • McDonald, B. and Martin-Serrano, J. (2009) No strings attached: the ESCRT machinery in viral budding and cytokinesis. J. Cell. Sci. 122, 2167-2177
    • (2009) J. Cell. Sci. , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 7
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • DOI 10.1038/nature06171, PII NATURE06171
    • Obita, T., Saksena, S., Ghazi-Tabatabai, S., Gill, D.J., Perisic, O., Emr, S.D., and Williams, R.L. (2007) Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449, 735-739 (Pubitemid 47552090)
    • (2007) Nature , vol.449 , Issue.7163 , pp. 735-739
    • Obita, T.1    Saksena, S.2    Ghazi-Tabatabai, S.3    Gill, D.J.4    Perisic, O.5    Emr, S.D.6    Williams, R.L.7
  • 9
    • 46049099346 scopus 로고    scopus 로고
    • Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding
    • DOI 10.1016/j.devcel.2008.05.014, PII S1534580708002396
    • Kieffer, C., Skalicky, J.J., Morita, E., De Domenico, I., Ward, D.M., Kaplan, J., and Sundquist, W.I. (2008) Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev. Cell 15, 62-73 (Pubitemid 351895604)
    • (2008) Developmental Cell , vol.15 , Issue.1 , pp. 62-73
    • Kieffer, C.1    Skalicky, J.J.2    Morita, E.3    De Domenico, I.4    Ward, D.M.5    Kaplan, J.6    Sundquist, W.I.7
  • 13
  • 14
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • in press
    • Sorimachi, H., Hata, S., and Ono, Y. (2011) Impact of genetic insights into calpain biology. J. Biochem. (in press)
    • J. Biochem. , vol.2011
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 15
    • 0033573028 scopus 로고    scopus 로고
    • 2+-dependent protease activity and a novel mode of enzyme activation
    • +-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18, 6880-6889 (Pubitemid 30000441)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 18
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • DOI 10.1128/MCB.20.12.4474-4481.2000
    • Arthur, J.S., Elce, J.S., Hegadorn, C., Williams, K., and Greer, P.A. (2000) Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol.Cell. Biol. 20, 4474-4481 (Pubitemid 30346642)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.12 , pp. 4474-4481
    • Arthur, J.S.C.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 19
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • DOI 10.1016/S1471-4914(01)02049-4
    • Huang, Y. and Wang, K.K.W. (2001) The calpain family and human disease. Trend. Mol. Med. 7, 355-362 (Pubitemid 32735021)
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.8 , pp. 355-362
    • Huang, Y.1    Wang, K.K.W.2
  • 22
    • 0028892964 scopus 로고
    • Signaling of ambient pH in Aspergillus involves a cysteine protease
    • Denison, S.H., Orejas, M., and Arst, H.N. Jr. (1995) Signaling of ambient pH in Aspergillus involves a cysteine protease. J. Biol. Chem. 270, 28519-28522
    • (1995) J. Biol. Chem. , vol.270 , pp. 28519-28522
    • Denison, S.H.1    Orejas, M.2    Arst Jr., H.N.3
  • 23
    • 0036714075 scopus 로고    scopus 로고
    • Regulation of gene expression by ambient pH in filamentous fungi and yeasts
    • DOI 10.1128/MMBR.66.3.426-446.2002
    • Peñalva, M.A. and Arst, H.N. Jr (2002) Regulation of gene expression by ambient pH in filamentous fungi and yeasts. Microbiol. Mol. Biol. Rev. 66, 426-446 (Pubitemid 35001138)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.3 , pp. 426-446
    • Penalva, M.A.1    Arst Jr., H.N.2
  • 24
    • 9244245261 scopus 로고    scopus 로고
    • Recent advances in the characterization of ambient pH regulation of gene expression in filamentous fungi and yeasts
    • DOI 10.1146/annurev.micro.58.030603.123715
    • Peñalva, M.A. and Arst, H.N. Jr (2004) Recent advances in the characterization of ambient pH regulation of gene expression in filamentous fungi and yeasts. Annu. Rev. Microbiol. 58, 425-451 (Pubitemid 39551993)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 425-451
    • Penalva, M.A.1    Arst Jr., H.N.2
  • 25
    • 0032902815 scopus 로고    scopus 로고
    • The protease activity of a calpain-like cysteine protease in Saccharomyces cerevisiae is required for alkaline adaptation and sporulation
    • DOI 10.1007/s004380050929
    • Futai, E., Maeda, T., Sorimachi, H., Kitamoto, K., Ishiura, S., and Suzuki, K. (1999) The protease activity of a calpain-like cysteine protease in Saccharomyces cerevisiae is required for alkaline adaptation and sporulation. Mol. Gen. Genet. 260, 559-568 (Pubitemid 29046161)
    • (1999) Molecular and General Genetics , vol.260 , Issue.6 , pp. 559-568
    • Futai, E.1    Maeda, T.2    Sorimachi, H.3    Kitamoto, K.4    Ishiura, S.5    Suzuki, K.6
  • 26
    • 27144493736 scopus 로고    scopus 로고
    • Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway
    • DOI 10.1128/MCB.25.21.9478-9490.2005
    • Hayashi, M., Fukuzawa, T., Sorimachi, H., and Maeda, T. (2005) Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway. Mol. Cell. Biol. 25, 9478-9490 (Pubitemid 41507848)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9478-9490
    • Hayashi, M.1    Fukuzawa, T.2    Sorimachi, H.3    Maeda, T.4
  • 27
    • 79952112344 scopus 로고    scopus 로고
    • Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction
    • Osako, Y., Maemoto, Y., Tanaka, R., Suzuki, H., Shibata, H., and Maki, M. (2010) Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction. FEBS J. 277, 4412-4426
    • FEBS J. , vol.2010 , Issue.277 , pp. 4412-4426
    • Osako, Y.1    Maemoto, Y.2    Tanaka, R.3    Suzuki, H.4    Shibata, H.5    Maki, M.6
  • 29
    • 39449140052 scopus 로고    scopus 로고
    • Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting
    • DOI 10.1091/mbc.E07-07-0694
    • Rue, S.M., Mattei, S., Saksena, S., and Emr, S.D. (2008) Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol. Biol. Cell 19, 475-484 (Pubitemid 351272137)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 475-484
    • Rue, S.M.1    Mattei, S.2    Saksena, S.3    Emr, S.D.4
  • 30
    • 68149094429 scopus 로고    scopus 로고
    • Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis
    • Xiao, J., Chen, X.W., Davies, B.A., Saltiel, A.R., Katzmann, D.J., and Xu, Z. (2009) Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis. Mol. Biol. Cell 20, 3514-3524
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3514-3524
    • Xiao, J.1    Chen, X.W.2    Davies, B.A.3    Saltiel, A.R.4    Katzmann, D.J.5    Xu, Z.6
  • 31
    • 0141643096 scopus 로고    scopus 로고
    • The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
    • DOI 10.1074/jbc.M301604200
    • Katoh, K., Shibata, H., Suzuki, H., Nara, A., Ishidoh, K., Kominami, E., Yoshimori, T., and Maki, M. (2003) The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J. Biol. Chem. 278, 39104-39113 (Pubitemid 37221814)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39104-39113
    • Katoh, K.1    Shibata, H.2    Suzuki, H.3    Nara, A.4    Ishidoh, K.5    Kominami, E.6    Yoshimori, T.7    Maki, M.8
  • 34
    • 34447527768 scopus 로고    scopus 로고
    • Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain
    • DOI 10.1111/j.1600-0854.2007.00584.x
    • Shim, S., Kimpler, L.A., and Hanson, P.I. (2007) Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 8, 1068-1079 (Pubitemid 47074039)
    • (2007) Traffic , vol.8 , Issue.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 36
    • 63249101831 scopus 로고    scopus 로고
    • Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III
    • Rodr?́guez-Galán, O., Galindo, A., Hervás-Aguilar, A., Arst, H.N. Jr, and Peñalva, M.A. (2009) Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III. J. Biol. Chem. 284, 4404-4412
    • (2009) J. Biol. Chem. , vol.284 , pp. 4404-4412
    • Rodŕguez-Galán, O.1    Galindo, A.2    Hervás-Aguilar, A.3    Arst Jr., H.N.4    Peñalva, M.A.5
  • 38
    • 46049118283 scopus 로고    scopus 로고
    • Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly
    • Shim, S., Merrill, S.A., and Hanson, P.I. (2008) Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly. Mol. Biol. Cell 19, 2661-2672
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2661-2672
    • Shim, S.1    Merrill, S.A.2    Hanson, P.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.