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Volumn 586, Issue 10, 2012, Pages 1445-1451

Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1

Author keywords

Autoinhibition; Electrostatic interactions; Membrane targeting; PDZ; Phospholipids; Surface plasmon resonance

Indexed keywords

DISCS LARGE PROTEIN; LIPOSOME; MEMBRANE PROTEIN; PDZ PROTEIN; PHOSPHATIDYLINOSITIDE; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN ZO1; SYNTENIN; SYNTENIN 1; UNCLASSIFIED DRUG;

EID: 84861194648     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.04.024     Document Type: Article
Times cited : (25)

References (45)
  • 1
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: Hubs for controlling the flow of cellular information
    • M.C. Good, J.G. Zalatan, and W.A. Lim Scaffold proteins: hubs for controlling the flow of cellular information Science 332 2011 680 686
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 2
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: Where proteins come together and when they're apart
    • J.D. Scott, and T. Pawson Cell signaling in space and time: where proteins come together and when they're apart Science 326 2009 1220 1224
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 3
    • 74049118478 scopus 로고    scopus 로고
    • An electrostatic switch displaces phosphatidylinositol phosphate kinases from the membrane during phagocytosis
    • G.D. Fairn An electrostatic switch displaces phosphatidylinositol phosphate kinases from the membrane during phagocytosis J. Cell Biol. 187 2009 701 714
    • (2009) J. Cell Biol. , vol.187 , pp. 701-714
    • Fairn, G.D.1
  • 4
    • 33845313646 scopus 로고    scopus 로고
    • 2 lipids target proteins with polybasic clusters to the plasma membrane
    • DOI 10.1126/science.1134389
    • W.D. Heo, T. Inoue, W.S. Park, M.L. Kim, B.O. Park, T.J. Wandless, and T. Meyer PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane Science 314 2006 1458 1461 (Pubitemid 44871952)
    • (2006) Science , vol.314 , Issue.5804 , pp. 1458-1461
    • Won, D.H.1    Inoue, T.2    Wei, S.P.3    Man, L.K.4    Byung, O.P.5    Wandless, T.J.6    Meyer, T.7
  • 5
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • S. McLaughlin, and A. Aderem The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions Trends Biochem. Sci. 20 1995 272 276
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 6
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • G. Di Paolo, and P. De Camilli Phosphoinositides in cell regulation and membrane dynamics Nature 443 2006 651 657 (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 7
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • DOI 10.1016/j.plipres.2005.05.001, PII S0163782705000214
    • J.E. Vance, and R. Steenbergen Metabolism and functions of phosphatidylserine Prog. Lipid Res. 44 2005 207 234 (Pubitemid 40973811)
    • (2005) Progress in Lipid Research , vol.44 , Issue.4 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 8
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: Lessons in polarity
    • A. Suzuki, and S. Ohno The PAR-aPKC system: lessons in polarity J. Cell Sci. 119 2006 979 987
    • (2006) J. Cell Sci. , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 10
    • 80053280652 scopus 로고    scopus 로고
    • PDZ domains: The building blocks regulating tumorigenesis
    • V.K. Subbaiah, C. Kranjec, M. Thomas, and L. Banks PDZ domains: the building blocks regulating tumorigenesis Biochem. J. 439 2011 195 205
    • (2011) Biochem. J. , vol.439 , pp. 195-205
    • Subbaiah, V.K.1    Kranjec, C.2    Thomas, M.3    Banks, L.4
  • 11
    • 0037816293 scopus 로고    scopus 로고
    • Molecular roots of degenerate specificity in syntenin's PDZ2 domain: Reassessment of the PDZ recognition paradigm
    • DOI 10.1016/S0969-2126(03)00125-4
    • B.S. Kang, D.R. Cooper, Y. Devedjiev, U. Derewenda, and Z.S. Derewenda Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm Structure 11 2003 845 853 (Pubitemid 36833270)
    • (2003) Structure , vol.11 , Issue.7 , pp. 845-853
    • Kang, B.S.1    Cooper, D.R.2    Devedjiev, Y.3    Derewenda, U.4    Derewenda, Z.S.5
  • 16
    • 84861182034 scopus 로고    scopus 로고
    • Syntenin, a syndecan adaptor and an Arf6 phosphatidylinositol 4,5-bisphosphate effector, is essential for epiboly and gastrulation cell movements in zebrafish
    • K. Lambaerts Syntenin, a syndecan adaptor and an Arf6 phosphatidylinositol 4,5-bisphosphate effector, is essential for epiboly and gastrulation cell movements in zebrafish J. Cell Sci. 125 2012 1129 1140
    • (2012) J. Cell Sci. , vol.125 , pp. 1129-1140
    • Lambaerts, K.1
  • 19
    • 79959271521 scopus 로고    scopus 로고
    • MDA-9/syntenin interacts with ubiquitin via a novel ubiquitin-binding motif
    • F. Okumura, K. Yoshida, F. Liang, and S. Hatakeyama MDA-9/syntenin interacts with ubiquitin via a novel ubiquitin-binding motif Mol. Cell. Biochem. 352 2011 163 172
    • (2011) Mol. Cell. Biochem. , vol.352 , pp. 163-172
    • Okumura, F.1    Yoshida, K.2    Liang, F.3    Hatakeyama, S.4
  • 21
    • 13844281177 scopus 로고    scopus 로고
    • Probing the supramodular architecture of a multidomain protein: The structure of syntenin in solution
    • DOI 10.1016/j.str.2004.12.014
    • T. Cierpicki, J.H. Bushweller, and Z.S. Derewenda Probing the supramodular architecture of a multidomain protein: the structure of syntenin in solution Structure 13 2005 319 327 (Pubitemid 40247707)
    • (2005) Structure , vol.13 , Issue.2 , pp. 319-327
    • Cierpicki, T.1    Bushweller, J.H.2    Derewenda, Z.S.3
  • 22
    • 33749635768 scopus 로고    scopus 로고
    • Syntenin-1 is a new component of tetraspanin-enriched microdomains: Mechanisms and consequences of the interaction of syntenin-1 with CD63
    • DOI 10.1128/MCB.00849-06
    • N. Latysheva, G. Muratov, S. Rajesh, M. Padgett, N.A. Hotchin, M. Overduin, and F. Berditchevski Syntenin-1 is a new component of tetraspanin-enriched microdomains: mechanisms and consequences of the interaction of syntenin-1 with CD63 Mol. Cell. Biol. 26 2006 7707 7718 (Pubitemid 44547717)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.20 , pp. 7707-7718
    • Latysheva, N.1    Muratov, G.2    Rajesh, S.3    Padgett, M.4    Hotchin, N.A.5    Overduin, M.6    Berditchevski, F.7
  • 23
    • 84455170010 scopus 로고    scopus 로고
    • Cooperative phosphoinositide and peptide binding by the PSD-95/discs ZO-1 (PDZ) domain of Polychaetoid, the Drosophila Zonulin
    • Y. Ivarsson, A.M. Wawrzyniak, G. Wuytens, M. Kosloff, E. Vermeiren, M. Raport, and P. Zimmermann Cooperative phosphoinositide and peptide binding by the PSD-95/discs ZO-1 (PDZ) domain of Polychaetoid, the Drosophila Zonulin J. Biol. Chem. 286 2011 44669 44678
    • (2011) J. Biol. Chem. , vol.286 , pp. 44669-44678
    • Ivarsson, Y.1    Wawrzyniak, A.M.2    Wuytens, G.3    Kosloff, M.4    Vermeiren, E.5    Raport, M.6    Zimmermann, P.7
  • 25
    • 0035815656 scopus 로고    scopus 로고
    • The Neural Cell Recognition Molecule Neurofascin Interacts with Syntenin-1 but Not with Syntenin-2, Both of Which Reveal Self-associating Activity
    • DOI 10.1074/jbc.M010647200
    • M. Koroll, F.G. Rathjen, and H. Volkmer The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity J. Biol. Chem. 276 2001 10646 10654 (Pubitemid 38089234)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10646-10654
    • Koroll, M.1    Rathjen, F.G.2    Volkmer, H.3
  • 26
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Y. Xue, J. Ren, X. Gao, C. Jin, L. Wen, and X. Yao GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy Mol. Cell. Proteomics 7 2008 1598 1608
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4    Wen, L.5    Yao, X.6
  • 27
    • 0028361026 scopus 로고
    • Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin
    • J. Kim, P.J. Blackshear, J.D. Johnson, and S. McLaughlin Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin Biophys. J. 67 1994 227 237 (Pubitemid 24197888)
    • (1994) Biophysical Journal , vol.67 , Issue.1 , pp. 227-237
    • Kim, J.1    Blackshear, P.J.2    Johnson, J.D.3    McLaughlin, S.4
  • 28
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • DOI 10.1007/s00018-005-4527-3
    • R.F. Zwaal, P. Comfurius, and E.M. Bevers Surface exposure of phosphatidylserine in pathological cells Cell. Mol. Life Sci. 62 2005 971 988 (Pubitemid 40655614)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.9 , pp. 971-988
    • Zwaal, R.F.A.1    Comfurius, P.2    Bevers, E.M.3
  • 29
  • 31
    • 0032547744 scopus 로고    scopus 로고
    • 3H]inositol-labeled phosphoinositide pools
    • DOI 10.1083/jcb.143.2.501
    • P. Varnai, and T. Balla Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools J. Cell Biol. 143 1998 501 510 (Pubitemid 28487866)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 32
    • 34548574739 scopus 로고    scopus 로고
    • Syntenin mediates Delta1-induced cohesiveness of epidermal stem cells in culture
    • DOI 10.1242/jcs.016253
    • S. Estrach, J. Legg, and F.M. Watt Syntenin mediates Delta1-induced cohesiveness of epidermal stem cells in culture J. Cell Sci. 120 2007 2944 2952 (Pubitemid 47394268)
    • (2007) Journal of Cell Science , vol.120 , Issue.16 , pp. 2944-2952
    • Estrach, S.1    Legg, J.2    Watt, F.M.3
  • 33
    • 77951212822 scopus 로고    scopus 로고
    • A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation
    • S. Bhattacharya, Z. Dai, J. Li, S. Baxter, D.J. Callaway, D. Cowburn, and Z. Bu A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation J. Biol. Chem. 285 2010 9981 9994
    • (2010) J. Biol. Chem. , vol.285 , pp. 9981-9994
    • Bhattacharya, S.1    Dai, Z.2    Li, J.3    Baxter, S.4    Callaway, D.J.5    Cowburn, D.6    Bu, Z.7
  • 35
    • 57349141863 scopus 로고    scopus 로고
    • Mda-9/Syntenin promotes metastasis in human melanoma cells by activating c-Src
    • H. Boukerche, Z.Z. Su, C. Prevot, D. Sarkar, and P.B. Fisher Mda-9/Syntenin promotes metastasis in human melanoma cells by activating c-Src Proc. Natl. Acad. Sci. USA 105 2008 15914 15919
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15914-15919
    • Boukerche, H.1    Su, Z.Z.2    Prevot, C.3    Sarkar, D.4    Fisher, P.B.5
  • 36
    • 79953153131 scopus 로고    scopus 로고
    • Extensions of PDZ domains as important structural and functional elements
    • C.K. Wang, L. Pan, J. Chen, and M. Zhang Extensions of PDZ domains as important structural and functional elements Protein Cell 1 2010 737 751
    • (2010) Protein Cell , vol.1 , pp. 737-751
    • Wang, C.K.1    Pan, L.2    Chen, J.3    Zhang, M.4
  • 37
    • 0034721943 scopus 로고    scopus 로고
    • Formation of nNOS/PSD-95 PDZ dimer requires a preformed beta-finger structure from the nNOS PDZ domain
    • H. Tochio, Y.K. Mok, Q. Zhang, H.M. Kan, D.S. Bredt, and M. Zhang Formation of nNOS/PSD-95 PDZ dimer requires a preformed beta-finger structure from the nNOS PDZ domain J. Mol. Biol. 303 2000 359 370
    • (2000) J. Mol. Biol. , vol.303 , pp. 359-370
    • Tochio, H.1    Mok, Y.K.2    Zhang, Q.3    Kan, H.M.4    Bredt, D.S.5    Zhang, M.6
  • 38
    • 79951772229 scopus 로고    scopus 로고
    • The structural and dynamic response of MAGI-1 PDZ1 with noncanonical domain boundaries to the binding of human papillomavirus E6
    • S. Charbonnier The structural and dynamic response of MAGI-1 PDZ1 with noncanonical domain boundaries to the binding of human papillomavirus E6 J. Mol. Biol. 406 2011 745 763
    • (2011) J. Mol. Biol. , vol.406 , pp. 745-763
    • Charbonnier, S.1
  • 40
    • 84861117819 scopus 로고    scopus 로고
    • Beyond the Binding Site: The Role of the beta2 - Beta3 Loop and Extra-Domain Structures in PDZ Domains
    • S. Mostarda, D. Gfeller, and F. Rao Beyond the Binding Site: The Role of the beta2 - beta3 Loop and Extra-Domain Structures in PDZ Domains PLoS Comput. Biol. 8 2012 e1002429
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002429
    • Mostarda, S.1    Gfeller, D.2    Rao, F.3
  • 41
    • 67449096531 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation of the syndecan-1 PDZ binding domain regulates syntenin-1 recruitment
    • B. Sulka, H. Lortat-Jacob, R. Terreux, F. Letourneur, and P. Rousselle Tyrosine dephosphorylation of the syndecan-1 PDZ binding domain regulates syntenin-1 recruitment J. Biol. Chem. 284 2009 10659 10671
    • (2009) J. Biol. Chem. , vol.284 , pp. 10659-10671
    • Sulka, B.1    Lortat-Jacob, H.2    Terreux, R.3    Letourneur, F.4    Rousselle, P.5
  • 43
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • T. Yeung, G.E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein Membrane phosphatidylserine regulates surface charge and protein localization Science 319 2008 210 213
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 44
    • 44849120414 scopus 로고    scopus 로고
    • How is SOS activated? Let us count the ways
    • DOI 10.1038/nsmb0608-538, PII NSMB0608538
    • G.M. Findlay, and T. Pawson How is SOS activated? Let us count the ways Nat. Struct. Mol. Biol. 15 2008 538 540 (Pubitemid 351799144)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.6 , pp. 538-540
    • Findlay, G.M.1    Pawson, T.2
  • 45
    • 0036531884 scopus 로고    scopus 로고
    • How signaling proteins integrate multiple inputs: A comparison of N-WASP and Cdk2
    • DOI 10.1016/S0955-0674(02)00307-1
    • K.E. Prehoda, and W.A. Lim How signaling proteins integrate multiple inputs: a comparison of N-WASP and Cdk2 Curr. Opin. Cell Biol. 14 2002 149 154 (Pubitemid 34219502)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.2 , pp. 149-154
    • Prehoda, K.E.1    Lim, W.A.2


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