메뉴 건너뛰기




Volumn 586, Issue 13, 2012, Pages 1759-1764

Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix)

Author keywords

Apoptosis linked gene 2 interacting protein X (Alix); NMR; Protein protein interaction; SAXS; Src family kinase (SFK); Src homology 3 domain (SH3 domain)

Indexed keywords

APOPTOSIS LINKED GENE 2 INTERACTING PROTEIN; HEMATOPOIETIC CELL KINASE; PROLINE; PROTEIN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 84862501603     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.017     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 0037047287 scopus 로고    scopus 로고
    • Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization
    • Chatellard-Causse, C., Blot, B., Cristina, N., Torch, S., Missotten, M. and Sadoul, R. (2002) Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization. J. Biol. Chem. 277, 29108-29115.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29108-29115
    • Chatellard-Causse, C.1    Blot, B.2    Cristina, N.3    Torch, S.4    Missotten, M.5    Sadoul, R.6
  • 3
    • 4744365071 scopus 로고    scopus 로고
    • Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex
    • DOI 10.1128/MCB.24.20.8981-8993.2004
    • Schmidt, M.H., Hoeller, D., Yu, J., Furnari, F.B., Cavenee, W.K., Dikic, I. and Bögler, O. (2004) Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex. Mol. Cell. Biol. 24, 8981-8993. (Pubitemid 39313903)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.20 , pp. 8981-8993
    • Schmidt, M.H.H.1    Hoeller, D.2    Yu, J.3    Furnari, F.B.4    Cavenee, W.K.5    Dikic, I.6    Bogler, O.7
  • 4
    • 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
  • 7
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • DOI 10.1016/S0092-8674(03)00653-6
    • Strack, B., Calistri, A., Craig, S., Popova, E. and Göttlinger, H.G. (2003) AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114, 689-699. (Pubitemid 37186765)
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 8
    • 33748302008 scopus 로고    scopus 로고
    • The multiple personalities of Alix
    • Odorizzi, G. (2006) The multiple personalities of Alix. J. Cell Sci. 119, 3025-3032.
    • (2006) J. Cell Sci. , vol.119 , pp. 3025-3032
    • Odorizzi, G.1
  • 9
    • 13544271663 scopus 로고    scopus 로고
    • Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities
    • DOI 10.1074/jbc.M409839200
    • Schmidt, M.H., Dikic, I. and Bögler, O. (2005) Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities. J. Biol. Chem. 280, 3414-3425. (Pubitemid 40223805)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3414-3425
    • Schmidt, M.H.H.1    Dikic, I.2    Bogler, O.3
  • 11
    • 33847355934 scopus 로고    scopus 로고
    • Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding
    • DOI 10.1016/j.cell.2007.01.035, PII S0092867407001808
    • Fisher, R.D., Chung, H.Y., Zhai, Q., Robinson, H., Sundquist, W.I. and Hill, C.P. (2007) Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128, 841-852. (Pubitemid 46341413)
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.-Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 12
    • 77956625350 scopus 로고    scopus 로고
    • Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X
    • Shi, X. et al. (2010) Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X. Biochem. J. 431, 93-102.
    • (2010) Biochem. J. , vol.431 , pp. 93-102
    • Shi, X.1
  • 13
    • 49049119270 scopus 로고    scopus 로고
    • Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - From signaling and actin reorganization to migration and phagocytosis
    • Guiet, R., Poincloux, R., Castandet, J., Marois, L., Labrousse, A., Le Cabec, V. and Maridonneau-Parini, I. (2008) Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from signaling and actin reorganization to migration and phagocytosis. Eur. J. Cell Biol. 87, 527-542.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 527-542
    • Guiet, R.1    Poincloux, R.2    Castandet, J.3    Marois, L.4    Labrousse, A.5    Le Cabec, V.6    Maridonneau-Parini, I.7
  • 14
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • DOI 10.1016/S0092-8674(00)81276-3
    • Lee, C.H., Saksela, K., Mirza, U.A., Chait, B.T. and Kuriyan, J. (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85, 931-942. (Pubitemid 26192143)
    • (1996) Cell , vol.85 , Issue.6 , pp. 931-942
    • Chi-Hon, L.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 15
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee, C.H., Leung, B., Lemmon, M.A., Zheng, J., Cowburn, D., Kuriyan, J. and Saksela, K. (1995) A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14, 5006-5015.
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Leung, B.2    Lemmon, M.A.3    Zheng, J.4    Cowburn, D.5    Kuriyan, J.6    Saksela, K.7
  • 16
    • 0031572847 scopus 로고    scopus 로고
    • The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling
    • Arold, S., Franken, P., Strub, M.P., Hoh, F., Benichou, S., Benarous, R. and Dumas, C. (1997) The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. Structure 5, 1361-1372. (Pubitemid 27484477)
    • (1997) Structure , vol.5 , Issue.10 , pp. 1361-1372
    • Arold, S.1    Franken, P.2    Strub, M.-P.3    Hoh, F.4    Benichou, S.5    Benarous, R.6    Dumas, C.7
  • 17
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li, S.S. (2005) Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem. J. 390, 641-653.
    • (2005) Biochem. J. , vol.390 , pp. 641-653
    • Li, S.S.1
  • 18
    • 0034854563 scopus 로고    scopus 로고
    • High-throughput yeast two-hybrid assays for large-scale protein interaction mapping
    • DOI 10.1006/meth.2001.1190
    • Walhout, A.J. and Vidal, M. (2001) High-throughput yeast two-hybrid assays for large-scale protein interaction mapping. Methods 24, 297-306. (Pubitemid 32846435)
    • (2001) Methods , vol.24 , Issue.3 , pp. 297-306
    • Walhout, A.J.M.1    Vidal, M.2
  • 19
    • 79959981040 scopus 로고    scopus 로고
    • Rosetta FlexPepDock web server - High resolution modeling of peptide-protein interactions
    • London, N., Raveh, B., Cohen, E., Fathi, G. and Schueler-Furman, O. (2011) Rosetta FlexPepDock web server - high resolution modeling of peptide-protein interactions. Nucleic Acids Res. 39, W249-W253.
    • (2011) Nucleic Acids Res. , vol.39
    • London, N.1    Raveh, B.2    Cohen, E.3    Fathi, G.4    Schueler-Furman, O.5
  • 20
    • 0032553012 scopus 로고    scopus 로고
    • RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef
    • DOI 10.1021/bi980989q
    • Arold, S., O'Brien, R., Franken, P., Strub, M.P., Hoh, F., Dumas, C. and Ladbury, J.E. (1998) RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef. Biochemistry 37, 14683-14691. (Pubitemid 28487576)
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14683-14691
    • Arold, S.1    O'Brien, R.2    Franken, P.3    Strub, M.-P.4    Hoh, F.5    Dumas, C.6    Ladbury, J.E.7
  • 21
    • 78650961103 scopus 로고    scopus 로고
    • Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling
    • Ladbury, J.E. and Arold, S.T. (2011) Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling. Methods Enzymol. 488, 147-183.
    • (2011) Methods Enzymol. , vol.488 , pp. 147-183
    • Ladbury, J.E.1    Arold, S.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.