메뉴 건너뛰기




Volumn 11, Issue 8, 2015, Pages 1184-1192

Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly

Author keywords

[No Author keywords available]

Indexed keywords

KILLER CELL ACTIVATING RECEPTOR ASSOCIATED PROTEIN; TETRAMER; MEMBRANE LIPID; MEMBRANE PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TYROBP PROTEIN, HUMAN;

EID: 84929962768     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.04.045     Document Type: Article
Times cited : (20)

References (39)
  • 4
    • 78649794988 scopus 로고    scopus 로고
    • A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer
    • Call M.E., Chou J.J. A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer. Structure 2010, 18:1559-1569.
    • (2010) Structure , vol.18 , pp. 1559-1569
    • Call, M.E.1    Chou, J.J.2
  • 5
    • 35548988341 scopus 로고    scopus 로고
    • Common themes in the assembly and architecture of activating immune receptors
    • Call M.E., Wucherpfennig K.W. Common themes in the assembly and architecture of activating immune receptors. Nat. Rev. Immunol. 2007, 7:841-850.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 841-850
    • Call, M.E.1    Wucherpfennig, K.W.2
  • 6
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the Tcell receptor-CD3 complex
    • Call M.E., Pyrdol J., Wiedmann M., Wucherpfennig K.W. The organizing principle in the formation of the Tcell receptor-CD3 complex. Cell 2002, 111:967-979.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 7
    • 33750022623 scopus 로고    scopus 로고
    • The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the Tcell receptor
    • Call M.E., Schnell J.R., Xu C., Lutz R.A., Chou J.J., Wucherpfennig K.W. The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the Tcell receptor. Cell 2006, 127:355-368.
    • (2006) Cell , vol.127 , pp. 355-368
    • Call, M.E.1    Schnell, J.R.2    Xu, C.3    Lutz, R.A.4    Chou, J.J.5    Wucherpfennig, K.W.6
  • 8
    • 77958153191 scopus 로고    scopus 로고
    • The structural basis forintramembrane assembly of an activating immunoreceptor complex
    • Call M.E., Wucherpfennig K.W., Chou J.J. The structural basis forintramembrane assembly of an activating immunoreceptor complex. Nat. Immunol. 2010, 11:1023-1029.
    • (2010) Nat. Immunol. , vol.11 , pp. 1023-1029
    • Call, M.E.1    Wucherpfennig, K.W.2    Chou, J.J.3
  • 9
    • 84859391450 scopus 로고    scopus 로고
    • NMR observable-based structure refinement of DAP12-NKG2C activating immunoreceptor complex in explicit membranes
    • Cheng X., Im W. NMR observable-based structure refinement of DAP12-NKG2C activating immunoreceptor complex in explicit membranes. Biophys. J. 2012, 102:L27-L29.
    • (2012) Biophys. J. , vol.102 , pp. L27-L29
    • Cheng, X.1    Im, W.2
  • 10
    • 84896689575 scopus 로고    scopus 로고
    • Helical membrane protein conformations and their environment
    • Cross T.A., Murray D.T., Watts A. Helical membrane protein conformations and their environment. Eur. Biophys. J. 2013, 42:731-755.
    • (2013) Eur. Biophys. J. , vol.42 , pp. 731-755
    • Cross, T.A.1    Murray, D.T.2    Watts, A.3
  • 11
    • 17444427074 scopus 로고    scopus 로고
    • Convergence on a distinctive assembly mechanism by unrelated families of activating immune receptors
    • Feng J., Garrity D., Call M.E., Moffett H., Wucherpfennig K.W. Convergence on a distinctive assembly mechanism by unrelated families of activating immune receptors. Immunity 2005, 22:427-438.
    • (2005) Immunity , vol.22 , pp. 427-438
    • Feng, J.1    Garrity, D.2    Call, M.E.3    Moffett, H.4    Wucherpfennig, K.W.5
  • 12
    • 33646718143 scopus 로고    scopus 로고
    • The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site
    • Feng J., Call M.E., Wucherpfennig K.W. The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site. PLoS Biol. 2006, 4:e142.
    • (2006) PLoS Biol. , vol.4 , pp. e142
    • Feng, J.1    Call, M.E.2    Wucherpfennig, K.W.3
  • 13
    • 19644365065 scopus 로고    scopus 로고
    • The activating NKG2D receptor assembles in the membrane with two signaling dimers into a hexameric structure
    • Garrity D., Call M.E., Feng J., Wucherpfennig K.W. The activating NKG2D receptor assembles in the membrane with two signaling dimers into a hexameric structure. Proc. Natl. Acad. Sci. USA 2005, 102:7641-7646.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7641-7646
    • Garrity, D.1    Call, M.E.2    Feng, J.3    Wucherpfennig, K.W.4
  • 14
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H., Lear J.D., DeGrado W.F. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. USA 2001, 98:880-885.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 15
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich S.U., Mothes W., Brunner J., Rapoport T.A. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 2000, 102:233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 17
    • 77955619741 scopus 로고    scopus 로고
    • Crystallizing transmembrane peptides in lipidic mesophases
    • Höfer N., Aragão D., Caffrey M. Crystallizing transmembrane peptides in lipidic mesophases. Biophys. J. 2010, 99:L23-L25.
    • (2010) Biophys. J. , vol.99 , pp. L23-L25
    • Höfer, N.1    Aragão, D.2    Caffrey, M.3
  • 18
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger L.J., Lamb R.A. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 1991, 183:32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 19
    • 41149134824 scopus 로고    scopus 로고
    • Automated builder and database of protein/membrane complexes for molecular dynamics simulations
    • Jo S., Kim T., Im W. Automated builder and database of protein/membrane complexes for molecular dynamics simulations. PLoS ONE 2007, 2:e880.
    • (2007) PLoS ONE , vol.2 , pp. e880
    • Jo, S.1    Kim, T.2    Im, W.3
  • 20
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: a web-based graphical user interface for CHARMM
    • Jo S., Kim T., Iyer V.G., Im W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J.Comput. Chem. 2008, 29:1859-1865.
    • (2008) J.Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 21
    • 68949149548 scopus 로고    scopus 로고
    • CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes
    • Jo S., Lim J.B., Klauda J.B., Im W. CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes. Biophys. J. 2009, 97:50-58.
    • (2009) Biophys. J. , vol.97 , pp. 50-58
    • Jo, S.1    Lim, J.B.2    Klauda, J.B.3    Im, W.4
  • 23
    • 26444611461 scopus 로고    scopus 로고
    • Transmembrane glycine zippers: physiological and pathological roles in membrane proteins
    • Kim S., Jeon T.J., Oberai A., Yang D., Schmidt J.J., Bowie J.U. Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc. Natl. Acad. Sci. USA 2005, 102:14278-14283.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14278-14283
    • Kim, S.1    Jeon, T.J.2    Oberai, A.3    Yang, D.4    Schmidt, J.J.5    Bowie, J.U.6
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J.Mol. Biol. 2007, 372:774-797.
    • (2007) J.Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 0032100703 scopus 로고    scopus 로고
    • Association of DAP12 with activating CD94/NKG2C NK cell receptors
    • Lanier L.L., Corliss B., Wu J., Phillips J.H. Association of DAP12 with activating CD94/NKG2C NK cell receptors. Immunity 1998, 8:693-701.
    • (1998) Immunity , vol.8 , pp. 693-701
    • Lanier, L.L.1    Corliss, B.2    Wu, J.3    Phillips, J.H.4
  • 26
    • 0032510146 scopus 로고    scopus 로고
    • Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells
    • Lanier L.L., Corliss B.C., Wu J., Leong C., Phillips J.H. Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells. Nature 1998, 391:703-707.
    • (1998) Nature , vol.391 , pp. 703-707
    • Lanier, L.L.1    Corliss, B.C.2    Wu, J.3    Leong, C.4    Phillips, J.H.5
  • 27
    • 65649127175 scopus 로고    scopus 로고
    • The structure of theintegrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau T.L., Kim C., Ginsberg M.H., Ulmer T.S. The structure of theintegrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J. 2009, 28:1351-1361.
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 29
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • Lu X., Gross A.W., Lodish H.F. Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J.Biol. Chem. 2006, 281:7002-7011.
    • (2006) J.Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 30
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo B.H., Springer T.A., Takagi J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2004, 2:e153.
    • (2004) PLoS Biol. , vol.2 , pp. e153
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 31
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., Engelman D.M. A transmembrane helix dimer: structure and implications. Science 1997, 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 34
    • 84873624057 scopus 로고    scopus 로고
    • An atomistic model for assembly of transmembrane domain of Tcell receptor complex
    • Sharma S., Juffer A.H. An atomistic model for assembly of transmembrane domain of Tcell receptor complex. J.Am. Chem. Soc. 2013, 135:2188-2197.
    • (2013) J.Am. Chem. Soc. , vol.135 , pp. 2188-2197
    • Sharma, S.1    Juffer, A.H.2
  • 35
    • 84882974287 scopus 로고    scopus 로고
    • Production of disulfide-stabilized transmembrane peptide complexes for structural studies
    • Sharma P., Kaywan-Lutfi M., Krshnan L., Byrne E.F., Call M.J., Call M.E. Production of disulfide-stabilized transmembrane peptide complexes for structural studies. J.Vis. Exp. 2013, e50141.
    • (2013) J.Vis. Exp. , pp. e50141
    • Sharma, P.1    Kaywan-Lutfi, M.2    Krshnan, L.3    Byrne, E.F.4    Call, M.J.5    Call, M.E.6
  • 36
    • 84875889882 scopus 로고    scopus 로고
    • The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies
    • Wei P., Zheng B.K., Guo P.R., Kawakami T., Luo S.Z. The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies. Biophys. J. 2013, 104:1435-1444.
    • (2013) Biophys. J. , vol.104 , pp. 1435-1444
    • Wei, P.1    Zheng, B.K.2    Guo, P.R.3    Kawakami, T.4    Luo, S.Z.5
  • 37
    • 84912552166 scopus 로고    scopus 로고
    • Molecular dynamic simulation of the self-assembly of DAP12-NKG2C activating immunoreceptor complex
    • Wei P., Xu L., Li C.D., Sun F.D., Chen L., Tan T., Luo S.Z. Molecular dynamic simulation of the self-assembly of DAP12-NKG2C activating immunoreceptor complex. PLoS ONE 2014, 9:e105560.
    • (2014) PLoS ONE , vol.9 , pp. e105560
    • Wei, P.1    Xu, L.2    Li, C.D.3    Sun, F.D.4    Chen, L.5    Tan, T.6    Luo, S.Z.7
  • 39
    • 64749101260 scopus 로고    scopus 로고
    • The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3
    • Zhu J., Luo B.H., Barth P., Schonbrun J., Baker D., Springer T.A. The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3. Mol. Cell 2009, 34:234-249.
    • (2009) Mol. Cell , vol.34 , pp. 234-249
    • Zhu, J.1    Luo, B.H.2    Barth, P.3    Schonbrun, J.4    Baker, D.5    Springer, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.