메뉴 건너뛰기




Volumn 90, Issue 2, 2015, Pages 587-598

Oligomerization and nanocluster organization render specificity

Author keywords

Allosteric; Allostery; Co localization; Conformational states; Cytoskeleton; Microclusters; Nanoclusters; Oligomerization; Ras; Scaffolding; Signalling; Structure

Indexed keywords

LIPID;

EID: 84927036139     PISSN: 14647931     EISSN: 1469185X     Source Type: Journal    
DOI: 10.1111/brv.12124     Document Type: Article
Times cited : (41)

References (86)
  • 6
    • 44949124597 scopus 로고    scopus 로고
    • Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters
    • Belanis, L., Plowman, S. J., Rotblat, B., Hancock, J. F. & Kloog, Y. (2008). Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters. Molecular Biology of the Cell 19, 1404-1414.
    • (2008) Molecular Biology of the Cell , vol.19 , pp. 1404-1414
    • Belanis, L.1    Plowman, S.J.2    Rotblat, B.3    Hancock, J.F.4    Kloog, Y.5
  • 8
    • 84874040939 scopus 로고    scopus 로고
    • TCR nanoclusters as the framework for transmission of conformational changes and cooperativity
    • Blanco, R. & Alarcon, B. (2012). TCR nanoclusters as the framework for transmission of conformational changes and cooperativity. Frontiers in Immunology 3, 115(7).
    • (2012) Frontiers in Immunology , vol.3 , Issue.7 , pp. 115
    • Blanco, R.1    Alarcon, B.2
  • 10
    • 0031804503 scopus 로고    scopus 로고
    • Signaling complexes: biophysical constraints on intracellular communication
    • Bray, D. (1998). Signaling complexes: biophysical constraints on intracellular communication. Annual Review of Biophysics and Biomolecular Structure 27, 59-75.
    • (1998) Annual Review of Biophysics and Biomolecular Structure , vol.27 , pp. 59-75
    • Bray, D.1
  • 11
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray, D., Levin, M. D. & Morton-Firth, C. J. (1998). Receptor clustering as a cellular mechanism to control sensitivity. Nature 393, 85-88.
    • (1998) Nature , vol.393 , pp. 85-88
    • Bray, D.1    Levin, M.D.2    Morton-Firth, C.J.3
  • 12
    • 76649135799 scopus 로고    scopus 로고
    • Signalling complexes and clusters: functional advantages and methodological hurdles
    • Cebecauer, M., Spitaler, M., Serge, A. & Magee, A. I. (2010). Signalling complexes and clusters: functional advantages and methodological hurdles. Journal of Cell Science 123, 309-320.
    • (2010) Journal of Cell Science , vol.123 , pp. 309-320
    • Cebecauer, M.1    Spitaler, M.2    Serge, A.3    Magee, A.I.4
  • 14
    • 79251589403 scopus 로고    scopus 로고
    • Galectin multimerization and lattice formation are regulated by linker region structure
    • Earl, L. A., Bi, S. & Baum, L. G. (2011). Galectin multimerization and lattice formation are regulated by linker region structure. Glycobiology 21, 6-12.
    • (2011) Glycobiology , vol.21 , pp. 6-12
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 15
    • 0034097043 scopus 로고    scopus 로고
    • Regulation of B lymphocyte responses to foreign and self-antigens by the CD19/CD21 complex
    • Fearon, D. T. & Carroll, M. C. (2000). Regulation of B lymphocyte responses to foreign and self-antigens by the CD19/CD21 complex. Annual Review of Immunology 18, 393-422.
    • (2000) Annual Review of Immunology , vol.18 , pp. 393-422
    • Fearon, D.T.1    Carroll, M.C.2
  • 16
    • 84861732291 scopus 로고    scopus 로고
    • Structural insights into the assembly of large oligomeric signalosomes in the Toll-like receptor-interleukin-1 receptor superfamily
    • Ferrao, R., Li, J., Bergamin, E. & Wu, H. (2012). Structural insights into the assembly of large oligomeric signalosomes in the Toll-like receptor-interleukin-1 receptor superfamily. Science Signaling 5, re3.
    • (2012) Science Signaling , vol.5 , pp. re3
    • Ferrao, R.1    Li, J.2    Bergamin, E.3    Wu, H.4
  • 17
    • 84873088843 scopus 로고    scopus 로고
    • Lck, membrane microdomains, and TCR triggering machinery: defining the new rules of engagement
    • Filipp, D., Ballek, O. & Manning, J. (2012). Lck, membrane microdomains, and TCR triggering machinery: defining the new rules of engagement. Frontiers in Immunology 3, 155(14).
    • (2012) Frontiers in Immunology , vol.3 , Issue.14 , pp. 155
    • Filipp, D.1    Ballek, O.2    Manning, J.3
  • 18
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., Sligar, S. G. & Wolynes, P. G. (1991). The energy landscapes and motions of proteins. Science 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 19
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
    • Ghosh, S., Strum, J. C., Sciorra, V. A., Daniel, L. & Bell, R. M. (1996). Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. The Journal of Biological Chemistry 271, 8472-8480.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 8472-8480
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 20
    • 0028083893 scopus 로고
    • The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras
    • Ghosh, S., Xie, W. Q., Quest, A. F., Mabrouk, G. M., Strum, J. C. & Bell, R. M. (1994). The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras. The Journal of Biological Chemistry 269, 10000-10007.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 10000-10007
    • Ghosh, S.1    Xie, W.Q.2    Quest, A.F.3    Mabrouk, G.M.4    Strum, J.C.5    Bell, R.M.6
  • 21
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer
    • Gorfe, A. A., Hanzal-Bayer, M., Abankwa, D., Hancock, J. F. & McCammon, J. A. (2007). Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1, 2-dimyristoylglycero-3-phosphocholine bilayer. Journal of Medicinal Chemistry 50, 674-684.
    • (2007) Journal of Medicinal Chemistry , vol.50 , pp. 674-684
    • Gorfe, A.A.1    Hanzal-Bayer, M.2    Abankwa, D.3    Hancock, J.F.4    McCammon, J.A.5
  • 23
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: different signals from different locations
    • Hancock, J. F. (2003). Ras proteins: different signals from different locations. Nature Reviews Molecular Cell Biology 4, 373-384.
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 24
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding, A. S. & Hancock, J. F. (2008). Using plasma membrane nanoclusters to build better signaling circuits. Trends in Cell Biology 18, 364-371.
    • (2008) Trends in Cell Biology , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 25
    • 61449215145 scopus 로고    scopus 로고
    • Ras acylation, compartmentalization and signaling nanoclusters (Review)
    • Henis, Y. I., Hancock, J. F. & Prior, I. A. (2009). Ras acylation, compartmentalization and signaling nanoclusters (Review). Molecular Membrane Biology 26, 80-92.
    • (2009) Molecular Membrane Biology , vol.26 , pp. 80-92
    • Henis, Y.I.1    Hancock, J.F.2    Prior, I.A.3
  • 26
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering, H., Lin, C. C. & Sheng, M. (2003). Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. The Journal of Neuroscience 23, 3262-3271.
    • (2003) The Journal of Neuroscience , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 31
    • 84867572593 scopus 로고    scopus 로고
    • The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction
    • Kapoor, S., Weise, K., Erlkamp, M., Triola, G., Waldmann, H. & Winter, R. (2012). The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction. European Biophysics Journal 41, 801-813.
    • (2012) European Biophysics Journal , vol.41 , pp. 801-813
    • Kapoor, S.1    Weise, K.2    Erlkamp, M.3    Triola, G.4    Waldmann, H.5    Winter, R.6
  • 36
    • 84874274026 scopus 로고    scopus 로고
    • How membrane structures control T cell signaling
    • Klammt, C. & Lillemeier, B. F. (2012). How membrane structures control T cell signaling. Frontiers in Immunology 3, 291(9).
    • (2012) Frontiers in Immunology , vol.3 , Issue.9 , pp. 291
    • Klammt, C.1    Lillemeier, B.F.2
  • 37
    • 84867882834 scopus 로고    scopus 로고
    • Eph/ephrin signalling during development
    • Klein, R. (2012). Eph/ephrin signalling during development. Development 139, 4105-4109.
    • (2012) Development , vol.139 , pp. 4105-4109
    • Klein, R.1
  • 38
    • 84861731097 scopus 로고    scopus 로고
    • Vav1 oncogenic mutation inhibits T cell receptor-induced calcium mobilization through inhibition of phospholipase Cgamma1 activation
    • Knyazhitsky, M., Moas, E., Shaginov, E., Luria, A. & Braiman, A. (2012). Vav1 oncogenic mutation inhibits T cell receptor-induced calcium mobilization through inhibition of phospholipase Cgamma1 activation. Journal of Biological Chemistry 287, 19725-19735.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 19725-19735
    • Knyazhitsky, M.1    Moas, E.2    Shaginov, E.3    Luria, A.4    Braiman, A.5
  • 40
    • 83455259711 scopus 로고    scopus 로고
    • Cancer: a drug-resistant duo
    • Lavoie, H. & Therrien, M. (2011). Cancer: a drug-resistant duo. Nature 480, 329-330.
    • (2011) Nature , vol.480 , pp. 329-330
    • Lavoie, H.1    Therrien, M.2
  • 43
    • 84888326531 scopus 로고    scopus 로고
    • Deformation of a two-domain lipid bilayer due to asymmetric insertion of lipid-modified Ras peptides
    • Li, Z. & Gorfe, A. A. (2013). Deformation of a two-domain lipid bilayer due to asymmetric insertion of lipid-modified Ras peptides. Soft Matter 9, 11249-11256.
    • (2013) Soft Matter , vol.9 , pp. 11249-11256
    • Li, Z.1    Gorfe, A.A.2
  • 45
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: linkers are not merely flexible
    • Ma, B., Tsai, C. J., Haliloglu, T. & Nussinov, R. (2011). Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917.
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloglu, T.3    Nussinov, R.4
  • 46
    • 79955574252 scopus 로고    scopus 로고
    • Interactions between kinase scaffold MP1/p14 and its endosomal anchoring protein p18
    • Magee, J. & Cygler, M. (2011). Interactions between kinase scaffold MP1/p14 and its endosomal anchoring protein p18. Biochemistry 50, 3696-3705.
    • (2011) Biochemistry , vol.50 , pp. 3696-3705
    • Magee, J.1    Cygler, M.2
  • 48
    • 77951620965 scopus 로고    scopus 로고
    • Spatial organization and signal transduction at intercellular junctions
    • Manz, B. N. & Groves, J. T. (2010). Spatial organization and signal transduction at intercellular junctions. Nature Reviews Molecular Cell Biology 11, 342-352.
    • (2010) Nature Reviews Molecular Cell Biology , vol.11 , pp. 342-352
    • Manz, B.N.1    Groves, J.T.2
  • 51
    • 33645310982 scopus 로고    scopus 로고
    • ITAM-mediated tonic signalling through pre-BCR and BCR complexes
    • Monroe, J. G. (2006). ITAM-mediated tonic signalling through pre-BCR and BCR complexes. Nature Reviews Immunology 6, 283-294.
    • (2006) Nature Reviews Immunology , vol.6 , pp. 283-294
    • Monroe, J.G.1
  • 53
    • 84884501302 scopus 로고    scopus 로고
    • Eph/ephrin recognition and the role of Eph/ephrin clusters in signaling initiation
    • Nikolov, D. B., Xu, K. & Himanen, J. P. (2013). Eph/ephrin recognition and the role of Eph/ephrin clusters in signaling initiation. Biochimica et Biophysica Acta 1834, 2160-2165.
    • (2013) Biochimica et Biophysica Acta , vol.1834 , pp. 2160-2165
    • Nikolov, D.B.1    Xu, K.2    Himanen, J.P.3
  • 54
    • 84881493915 scopus 로고    scopus 로고
    • The spatial structure of cell signaling systems
    • Nussinov, R. (2013). The spatial structure of cell signaling systems. Physical Biology 10, 045004.
    • (2013) Physical Biology , vol.10 , pp. 045004
    • Nussinov, R.1
  • 55
    • 84856078561 scopus 로고    scopus 로고
    • Protein dynamics and conformational selection in bidirectional signal transduction
    • Nussinov, R. & Ma, B. (2012). Protein dynamics and conformational selection in bidirectional signal transduction. BMC Biology 10, 2(5).
    • (2012) BMC Biology , vol.10 , Issue.5 , pp. 2
    • Nussinov, R.1    Ma, B.2
  • 56
    • 84876296757 scopus 로고    scopus 로고
    • A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery
    • Nussinov, R., Ma, B. & Tsai, C. J. (2013a). A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery. Biochimica et Biophysica Acta 1834, 820-829.
    • (2013) Biochimica et Biophysica Acta , vol.1834 , pp. 820-829
    • Nussinov, R.1    Ma, B.2    Tsai, C.J.3
  • 57
    • 84883480131 scopus 로고    scopus 로고
    • Allosteric conformational barcodes direct signaling in the cell
    • Nussinov, R., Ma, B., Tsai, C. J. & Csermely, P. (2013b). Allosteric conformational barcodes direct signaling in the cell. Structure 21, 1509-1521.
    • (2013) Structure , vol.21 , pp. 1509-1521
    • Nussinov, R.1    Ma, B.2    Tsai, C.J.3    Csermely, P.4
  • 58
    • 84876275408 scopus 로고    scopus 로고
    • The underappreciated role of allostery in the cellular network
    • Nussinov, R., Tsai, C. J. & Ma, B. (2013c). The underappreciated role of allostery in the cellular network. Annual Review of Biophysics 42, 169-189.
    • (2013) Annual Review of Biophysics , vol.42 , pp. 169-189
    • Nussinov, R.1    Tsai, C.J.2    Ma, B.3
  • 59
    • 84897052340 scopus 로고    scopus 로고
    • Free energy diagrams for protein function
    • Nussinov, R. & Tsai, C. J. (2014). Free energy diagrams for protein function. Chemistry & Biology 21, 311-318.
    • (2014) Chemistry & Biology , vol.21 , pp. 311-318
    • Nussinov, R.1    Tsai, C.J.2
  • 62
    • 62149129986 scopus 로고    scopus 로고
    • Compartmentalized signalling: Ras proteins and signalling nanoclusters
    • Omerovic, J. & Prior, I. A. (2009). Compartmentalized signalling: Ras proteins and signalling nanoclusters. The FEBS Journal 276, 1817-1825.
    • (2009) The FEBS Journal , vol.276 , pp. 1817-1825
    • Omerovic, J.1    Prior, I.A.2
  • 63
    • 84874284008 scopus 로고    scopus 로고
    • Spatial coupling of JNK activation to the B cell antigen receptor by tyrosine-phosphorylated ezrin
    • Parameswaran, N., Enyindah-Asonye, G., Bagheri, N., Shah, N. B. & Gupta, N. (2013). Spatial coupling of JNK activation to the B cell antigen receptor by tyrosine-phosphorylated ezrin. Journal of Immunology 190, 2017-2026.
    • (2013) Journal of Immunology , vol.190 , pp. 2017-2026
    • Parameswaran, N.1    Enyindah-Asonye, G.2    Bagheri, N.3    Shah, N.B.4    Gupta, N.5
  • 67
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., Muncke, C., Parton, R. G. & Hancock, J. F. (2003). Direct visualization of Ras proteins in spatially distinct cell surface microdomains. The Journal of Cell Biology 160, 165-170.
    • (2003) The Journal of Cell Biology , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 69
    • 84871201282 scopus 로고    scopus 로고
    • Conformational states of the kinase Lck regulate clustering in early T cell signaling
    • Rossy, J., Owen, D. M., Williamson, D. J., Yang, Z. & Gaus, K. (2013). Conformational states of the kinase Lck regulate clustering in early T cell signaling. Nature Immunology 14, 82-89.
    • (2013) Nature Immunology , vol.14 , pp. 82-89
    • Rossy, J.1    Owen, D.M.2    Williamson, D.J.3    Yang, Z.4    Gaus, K.5
  • 71
    • 84871551631 scopus 로고    scopus 로고
    • Cholesterol modulates the structure, binding modes, and energetics of caveolin-membrane interactions
    • Sengupta, D. (2012). Cholesterol modulates the structure, binding modes, and energetics of caveolin-membrane interactions. The Journal of Physical Chemistry B 116, 14556-14564.
    • (2012) The Journal of Physical Chemistry B , vol.116 , pp. 14556-14564
    • Sengupta, D.1
  • 73
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes
    • Smith, N. J. & Milligan, G. (2010). Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes. Pharmacological Reviews 62, 701-725.
    • (2010) Pharmacological Reviews , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 74
    • 68149157248 scopus 로고    scopus 로고
    • The origin of allosteric functional modulation: multiple pre-existing pathways
    • del Sol, A., Tsai, C. J., Ma, B. & Nussinov, R. (2009). The origin of allosteric functional modulation: multiple pre-existing pathways. Structure 17, 1042-1050.
    • (2009) Structure , vol.17 , pp. 1042-1050
    • del Sol, A.1    Tsai, C.J.2    Ma, B.3    Nussinov, R.4
  • 76
    • 84863107745 scopus 로고    scopus 로고
    • A conserved role of IQGAP1 in regulating TOR complex 1
    • Tekletsadik, Y. K., Sonn, R. & Osman, M. A. (2012). A conserved role of IQGAP1 in regulating TOR complex 1. Journal of Cell Science 125, 2041-2052.
    • (2012) Journal of Cell Science , vol.125 , pp. 2041-2052
    • Tekletsadik, Y.K.1    Sonn, R.2    Osman, M.A.3
  • 78
    • 77953536657 scopus 로고    scopus 로고
    • Organisation and dynamics of antigen receptors: implications for lymphocyte signalling
    • Treanor, B. & Batista, F. D. (2010). Organisation and dynamics of antigen receptors: implications for lymphocyte signalling. Current Opinion in Immunology 22, 299-307.
    • (2010) Current Opinion in Immunology , vol.22 , pp. 299-307
    • Treanor, B.1    Batista, F.D.2
  • 79
    • 84881109637 scopus 로고    scopus 로고
    • The molecular basis of targeting protein kinases in cancer therapeutics
    • Tsai, C. J. & Nussinov, R. (2013). The molecular basis of targeting protein kinases in cancer therapeutics. Seminars in Cancer Biology 23, 235-242.
    • (2013) Seminars in Cancer Biology , vol.23 , pp. 235-242
    • Tsai, C.J.1    Nussinov, R.2
  • 80
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms
    • Tsai, C. J., del Sol, A. & Nussinov, R. (2009). Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms. Molecular Biosystems 5, 207-216.
    • (2009) Molecular Biosystems , vol.5 , pp. 207-216
    • Tsai, C.J.1    del Sol, A.2    Nussinov, R.3
  • 84
    • 84856219974 scopus 로고    scopus 로고
    • IQGAP1 and its binding proteins control diverse biological functions
    • White, C. D., Erdemir, H. H. & Sacks, D. B. (2012). IQGAP1 and its binding proteins control diverse biological functions. Cellular Signalling 24, 826-834.
    • (2012) Cellular Signalling , vol.24 , pp. 826-834
    • White, C.D.1    Erdemir, H.H.2    Sacks, D.B.3
  • 85
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Yan, J., Roy, S., Apolloni, A., Lane, A. & Hancock, J. F. (1998). Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. The Journal of Biological Chemistry 273, 24052-24056.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 86
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X., Gureasko, J., Shen, K., Cole, P. A. & Kuriyan, J. (2006). An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125, 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.