메뉴 건너뛰기




Volumn 348, Issue 2, 2005, Pages 491-501

Caveolin-1 interacts directly with dynamin-2

Author keywords

Caveolae; Caveolin dynamin interactions; Dynamin; Protein protein binding; Vesicle formation

Indexed keywords

ARGININE; CAVEOLIN 1; CHOLERA TOXIN; DYNAMIN II; GLUTATHIONE TRANSFERASE; GUANOSINE TRIPHOSPHATASE; HYBRID PROTEIN; MEMBRANE PROTEIN; PROLINE;

EID: 16244399830     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.003     Document Type: Article
Times cited : (94)

References (47)
  • 1
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • D.A. Brown, and E. London Structure and origin of ordered lipid domains in biological membranes J. Membr. Biol. 164 1998 103 114
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 2
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing preassembled signaling complexes at the plasma membrane
    • T. Okamoto, A. Schlegel, P.E. Scherer, and M.P. Lisanti Caveolins, a family of scaffolding proteins for organizing preassembled signaling complexes at the plasma membrane J. Biol. Chem. 273 1998 5419 5422
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 3
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • R.G.W. Anderson The caveolae membrane system Annu. Rev. Biochem. 67 1998 199 225
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 4
    • 0029075372 scopus 로고
    • Evidence for a regulated interaction between heterotrimeric G proteins and caveolin
    • S. Li Evidence for a regulated interaction between heterotrimeric G proteins and caveolin J. Biol. Chem. 270 1995 15693 15701
    • (1995) J. Biol. Chem. , vol.270 , pp. 15693-15701
    • Li, S.1
  • 5
    • 0029879507 scopus 로고    scopus 로고
    • Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae
    • P. Liu, Y. Ying, Y.G. Ko, and R.G.W. Anderson Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae J. Biol. Chem. 271 1996 10299 10303
    • (1996) J. Biol. Chem. , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.2    Ko, Y.G.3    Anderson, R.G.W.4
  • 6
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • J. Couet, M. Sargiacomo, and M.P. Lisanti Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities J. Biol. Chem. 272 1997 30429 30438
    • (1997) J. Biol. Chem. , vol.272 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 7
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • C. Mineo, G.L. James, E.J. Smart, and R.G.W. Anderson Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane J. Biol. Chem. 271 1996 11930 11935
    • (1996) J. Biol. Chem. , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.W.4
  • 8
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the NOS caveolin binding domain in vivo
    • G. Garcia-Cardena, P. Martasek, B.S. Masters, P.M. Skidd, J. Couet, and S. Li Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the NOS caveolin binding domain in vivo J. Biol. Chem. 272 1997 25437 25440
    • (1997) J. Biol. Chem. , vol.272 , pp. 25437-25440
    • Garcia-Cardena, G.1    Martasek, P.2    Masters, B.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6
  • 9
    • 0029787241 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase targeting to caveolae. specific interactions with caveolin isoforms in cardia myocytes and endothelial cells
    • O. Feron, L. Belhassen, L. Kobzik, T.W. Smith, R.A. Kelly, and T. Michel Endothelial nitric oxide synthase targeting to caveolae. specific interactions with caveolin isoforms in cardia myocytes and endothelial cells J. Biol. Chem. 271 1996 22810 22814
    • (1996) J. Biol. Chem. , vol.271 , pp. 22810-22814
    • Feron, O.1    Belhassen, L.2    Kobzik, L.3    Smith, T.W.4    Kelly, R.A.5    Michel, T.6
  • 10
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • S. Li, J. Couet, and M.P. Lisanti Src tyrosine kinases Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases J. Biol. Chem. 271 1996 29182 29190
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 11
    • 0030067984 scopus 로고    scopus 로고
    • Phosphorylation of caveolin by src tyrosine kinases the alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo
    • S. Li, R. Seitz, and M.P. Lisanti Phosphorylation of caveolin by src tyrosine kinases The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo J. Biol. Chem. 271 1996 3863 3868
    • (1996) J. Biol. Chem. , vol.271 , pp. 3863-3868
    • Li, S.1    Seitz, R.2    Lisanti, M.P.3
  • 12
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • K.K. Wary, A. Mariotti, C. Zurzolo, and F.G. Giancotti A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth Cell 94 1998 625 634
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 13
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • R.G. Anderson The caveolae membrane system Annu. Rev. Biochem. 67 1998 199 225
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 16
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with cavaeolae-associated proteins
    • J. Couet, S. Li, T. Okamoto, T. Ikezu, and M.P. Lisanti Identification of peptide and protein ligands for the caveolin-scaffolding domain. implications for the interaction of caveolin with cavaeolae-associated proteins J. Biol. Chem. 272 1997 6525 6533
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 18
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • R.G. Parton, B. Joggerst, and K. Simons Regulated internalization of caveolae J. Cell Biol. 127 1994 1199 1215
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 20
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • P. Oh, D.P. McIntosh, and J.E. Schnitzer Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium J. Cell Biol. 141 1998 101 114
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 21
    • 0034161330 scopus 로고    scopus 로고
    • Pinching in new places: Multiple functions for the dynamin family
    • M.A. McNiven, H. Cao, K.R. Pitts, and Y. Yoon Pinching in new places: multiple functions for the dynamin family Trends Biochem. Sci. 25 2000 115 120
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 22
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • G.J. Praefcke, and H.T. McMahon The dynamin superfamily: universal membrane tubulation and fission molecules? Nature Rev. Mol. Cell. Biol. 5 2004 133 147
    • (2004) Nature Rev. Mol. Cell. Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 23
    • 0030809132 scopus 로고    scopus 로고
    • Domain structure and intramolecular regulation of dynamin GTPase
    • A.B. Muhlberg, D.E. Warnock, and S.L. Schmid Domain structure and intramolecular regulation of dynamin GTPase EMBO J. 16 1997 6676 6683
    • (1997) EMBO J. , vol.16 , pp. 6676-6683
    • Muhlberg, A.B.1    Warnock, D.E.2    Schmid, S.L.3
  • 24
    • 0031000481 scopus 로고    scopus 로고
    • The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence
    • D. Grabs, V.I. Slepnev, Z. Songyang, C. David, M. Lynch, L.C. Cantley, and P. De Camilli The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence J. Biol. Chem. 272 1997 13419 13425
    • (1997) J. Biol. Chem. , vol.272 , pp. 13419-13425
    • Grabs, D.1    Slepnev, V.I.2    Songyang, Z.3    David, C.4    Lynch, M.5    Cantley, L.C.6    De Camilli, P.7
  • 25
    • 0028108262 scopus 로고
    • Association of Ash/Grb-2 with Dynamin through the Ssrc homology 3 domain
    • H. Miki, K. Miura, K. Matuoka, T. Nakata, N. Hirokawa, and S. Orita Association of Ash/Grb-2 with Dynamin through the Ssrc homology 3 domain J. Biol. Chem. 269 1994 5489 5492
    • (1994) J. Biol. Chem. , vol.269 , pp. 5489-5492
    • Miki, H.1    Miura, K.2    Matuoka, K.3    Nakata, T.4    Hirokawa, N.5    Orita, S.6
  • 27
    • 0032516055 scopus 로고    scopus 로고
    • Src interacts with dynamin and synapsin in neuronal cells
    • A. Foster-Barber, and J.M. Bishop Src interacts with dynamin and synapsin in neuronal cells Proc. Natl Acad. Sci. USA 95 1998 4673 4677
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4673-4677
    • Foster-Barber, A.1    Bishop, J.M.2
  • 29
    • 0034597062 scopus 로고    scopus 로고
    • Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape
    • M.A. McNiven, L. Kim, E.W. Krueger, J.D. Orth, H. Cao, and T.W. Wong Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape J. Cell Biol. 151 2000 187 198
    • (2000) J. Cell Biol. , vol.151 , pp. 187-198
    • McNiven, M.A.1    Kim, L.2    Krueger, E.W.3    Orth, J.D.4    Cao, H.5    Wong, T.W.6
  • 30
    • 0035897420 scopus 로고    scopus 로고
    • Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase Dynamin
    • M.M. Kessels, A.E.Y. Engqvist-Goldstein, D.G. Drubin, and B. Qualmann Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase Dynamin J. Cell Biol. 153 2001 351 366
    • (2001) J. Cell Biol. , vol.153 , pp. 351-366
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.Y.2    Drubin, D.G.3    Qualmann, B.4
  • 31
    • 0027362241 scopus 로고
    • The GTPase dynamin binds to and is activated by a subset of SH3 domains
    • I. Gout, R. Dhand, I.D. Hiles, M.J. Fry, G. Panayotou, and P. Das The GTPase dynamin binds to and is activated by a subset of SH3 domains Cell 75 1993 25 36
    • (1993) Cell , vol.75 , pp. 25-36
    • Gout, I.1    Dhand, R.2    Hiles, I.D.3    Fry, M.J.4    Panayotou, G.5    Das, P.6
  • 32
  • 33
    • 0036227351 scopus 로고    scopus 로고
    • The endocytosis-linked protein dynamin associates with caveolin-1 and is tyrosine phosphorylated in response to the activation of a noninternalizing epidermal growth factor receptor mutant
    • Y.N. Kim, and P.J. Bertics The endocytosis-linked protein dynamin associates with caveolin-1 and is tyrosine phosphorylated in response to the activation of a noninternalizing epidermal growth factor receptor mutant Endocrinology 143 2002 1726 1731
    • (2002) Endocrinology , vol.143 , pp. 1726-1731
    • Kim, Y.N.1    Bertics, P.J.2
  • 34
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • H. Cao, F. Garcia, and M.A. McNiven Differential distribution of dynamin isoforms in mammalian cells Mol. Biol. Cell 9 1998 2595 2609
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 35
    • 0344443664 scopus 로고    scopus 로고
    • Intersectin regulates fission and internalization of caveolae in endothelial cells
    • S.A. Predescu, D.N. Predescu, B.K. Timblin, R.V. Stan, and A.B. Malik Intersectin regulates fission and internalization of caveolae in endothelial cells Mol. Biol. Cell 14 2003 4997 5010
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4997-5010
    • Predescu, S.A.1    Predescu, D.N.2    Timblin, B.K.3    Stan, R.V.4    Malik, A.B.5
  • 37
    • 0030027901 scopus 로고    scopus 로고
    • Expression and characterization of recombinant caveolin
    • S. Li, K.S. Song, and M.P. Lisanti Expression and characterization of recombinant caveolin J. Biol. Chem. 271 1996 568 573
    • (1996) J. Biol. Chem. , vol.271 , pp. 568-573
    • Li, S.1    Song, K.S.2    Lisanti, M.P.3
  • 38
    • 0033603325 scopus 로고    scopus 로고
    • The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers
    • K. Das, R.L. Lewis, P.E. Scherer, and M.P. Lisanti The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers J. Biol. Chem. 274 1999 18721 18728
    • (1999) J. Biol. Chem. , vol.274 , pp. 18721-18728
    • Das, K.1    Lewis, R.L.2    Scherer, P.E.3    Lisanti, M.P.4
  • 39
    • 0033529643 scopus 로고    scopus 로고
    • A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro
    • A. Schlegel, R.B. Schwab, P.E. Scherer, and M.P. Lisanti A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro J. Biol. Chem. 274 1999 22660 22667
    • (1999) J. Biol. Chem. , vol.274 , pp. 22660-22667
    • Schlegel, A.1    Schwab, R.B.2    Scherer, P.E.3    Lisanti, M.P.4
  • 40
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • K. Farsad, N. Ringstad, K. Takei, S.R. Floyd, K. Rose, and P. De Camilli Generation of high curvature membranes mediated by direct endophilin bilayer interactions J. Cell Biol. 155 2001 193 200
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 41
    • 0034532164 scopus 로고    scopus 로고
    • Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members
    • F. Sotgia, J.K. Lee, K. Das, M. Bedford, T.C. Petrucci, and P. Macioce Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members J. Biol. Chem. 275 2000 38048 38058
    • (2000) J. Biol. Chem. , vol.275 , pp. 38048-38058
    • Sotgia, F.1    Lee, J.K.2    Das, K.3    Bedford, M.4    Petrucci, T.C.5    MacIoce, P.6
  • 42
    • 0037452948 scopus 로고    scopus 로고
    • Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer
    • N.W. Gray, L. Fourgeaud, B. Huang, J. Chen, H. Cao, and B.J. Oswald Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer Curr. Biol. 13 2003 510 515
    • (2003) Curr. Biol. , vol.13 , pp. 510-515
    • Gray, N.W.1    Fourgeaud, L.2    Huang, B.3    Chen, J.4    Cao, H.5    Oswald, B.J.6
  • 43
    • 16244401381 scopus 로고    scopus 로고
    • A dynamin 3 spliced variant modulates the actin/cortactin-dependent morphogenesis of dendritic spines
    • N.W. Gray, A.E. Kruchten, J. Chen, and M. McNiven A dynamin 3 spliced variant modulates the actin/cortactin-dependent morphogenesis of dendritic spines. J. Cell Sci. 2005 In the press
    • (2005) J. Cell Sci.
    • Gray, N.W.1    Kruchten, A.E.2    Chen, J.3    McNiven, M.4
  • 45
    • 4644342865 scopus 로고    scopus 로고
    • Regulation of WASP/WAVE proteins: Making a long story short
    • G. Bompard, and E. Caron Regulation of WASP/WAVE proteins: making a long story short J. Cell. Biol. 166 2004 957 962
    • (2004) J. Cell. Biol. , vol.166 , pp. 957-962
    • Bompard, G.1    Caron, E.2
  • 46
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • L. Pelkmans, D. Puntener, and A. Helenius Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae Science 296 2002 535 539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 47
    • 0037371802 scopus 로고    scopus 로고
    • Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis
    • H. Cao, J.D. Orth, J. Chen, S.G. Weller, J.E. Heuser, and M.A. McNiven Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis Mol. Cell. Biol. 23 2003 2162 2170
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2162-2170
    • Cao, H.1    Orth, J.D.2    Chen, J.3    Weller, S.G.4    Heuser, J.E.5    McNiven, M.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.