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Volumn 22, Issue 5, 2013, Pages 517-529

The clathrin adaptor complexes as a paradigm for membrane-associated allostery

Author keywords

Arf1; Membrane biology; Membrane traffic; Phosphoinositides; Protein crystallography; Protein structure

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CLATHRIN; CLATHRIN ASSOCIATED ADAPTOR PROTEIN 1; CLATHRIN ASSOCIATED ADAPTOR PROTEIN 2; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; UNCLASSIFIED DRUG; VESICULAR TRANSPORT PROTEIN;

EID: 84878323594     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2235     Document Type: Review
Times cited : (46)

References (51)
  • 1
    • 34547963038 scopus 로고    scopus 로고
    • Evolution of allosteric models for hemoglobin
    • DOI 10.1080/15216540701272380, PII 778359268, IUBMB Life Dedicated to Maurizio Brunori in the Occasion of his 70th Birthday
    • Eaton WA, Henry ER, Hofrichter J, Bettati S, Viappiani C, Mozzarelli A (2007) Evolution of allosteric models for hemoglobin. Iubmb Life 59:586-599. (Pubitemid 47265849)
    • (2007) IUBMB Life , vol.59 , Issue.8-9 , pp. 586-599
    • Eaton, W.A.1    Henry, E.R.2    Hofrichter, J.3    Bettati, S.4    Viappiani, C.5    Mozzarelli, A.6
  • 2
    • 78651189765 scopus 로고
    • On nature of allosteric transitions -A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On nature of allosteric transitions -a plausible model. J Mol Biol 12: 88-&.
    • (1965) J Mol Biol , vol.12 , pp. 88
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 3
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • DOI 10.1016/S0092-8674(03)01079-1
    • Bonifacino JS, Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116:153-166. (Pubitemid 38167309)
    • (2004) Cell , vol.116 , Issue.2 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 4
    • 30844453760 scopus 로고    scopus 로고
    • Life of a clathrin coat: Insights from clathrin and AP structures
    • DOI 10.1038/nrm1786, PII N1786
    • Edeling MA, Smith C, Owen D (2006) Life of a clathrin coat: insights from clathrin and AP structures. Nat Rev Mol Cell Biol 7:32-44. (Pubitemid 43361570)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.1 , pp. 32-44
    • Edeling, M.A.1    Smith, C.2    Owen, D.3
  • 6
    • 0032572560 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • DOI 10.1083/jcb.142.2.391
    • Ooi CE, Dell'Angelica EC, Bonifacino JS (1998) ADPribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J Cell Biol 142:391-402. (Pubitemid 28361547)
    • (1998) Journal of Cell Biology , vol.142 , Issue.2 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 7
    • 0037148533 scopus 로고    scopus 로고
    • Assembly and function of AP-3 complexes in cells expressing mutant subunits
    • DOI 10.1083/jcb.200107140
    • Peden AA, Rudge RE, Lui WWY, Robinson MS (2002) Assembly and function of AP-3 complexes in cells expressing mutant subunits. J Cell Biol 156:327-336. (Pubitemid 34839913)
    • (2002) Journal of Cell Biology , vol.156 , Issue.2 , pp. 327-336
    • Peden, A.A.1    Rudge, R.E.2    Lui, W.W.Y.3    Robinson, M.S.4
  • 9
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen DJ, Evans PR (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282:1327-1332. (Pubitemid 28524497)
    • (1998) Science , vol.282 , Issue.5392 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 10
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 γ-σ1 and AP-3 δ-σ3 hemicomplexes
    • DOI 10.1083/jcb.200307157
    • Janvier K, Kato Y, Boehm M, Rose JR, Martina JA, Kim BY, Venkatesan S, Bonifacino JS (2003) Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma 1 and AP-3 delta-sigma 3 hemicomplexes. J Cell Biol 163: 1281-1290. (Pubitemid 38032089)
    • (2003) Journal of Cell Biology , vol.163 , Issue.6 , pp. 1281-1290
    • Janvier, K.1    Kato, Y.2    Boehm, M.3    Rose, J.R.4    Martina, J.A.5    Kim, B.-Y.6    Venkatesan, S.7    Bonifacino, J.S.8
  • 11
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • DOI 10.1128/JVI.02725-06
    • Chaudhuri R, Lindwasser OW, Smith WJ, Hurley JH, Bonifacino JS (2007) Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J Virol 81:3877-3890. (Pubitemid 46586884)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 3877-3890
    • Chaudhuri, R.1    Lindwasser, O.W.2    Smith, W.J.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 12
    • 34248198351 scopus 로고    scopus 로고
    • The γ/σ1 and α/σ2 hemicomplexes of clathrin adaptors AP-1 and AP-2 Harbor the dileucine recognition site
    • DOI 10.1091/mbc.E07-01-0012
    • Doray B, Lee I, Knisely J, Bu GJ, Kornfeld S (2007) The gamma/sigma 1 and alpha/sigma 2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site. Mol Biol Cell 18:1887-1896. (Pubitemid 46717568)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1887-1896
    • Doray, B.1    Lee, I.2    Knisely, J.3    Bu, G.4    Kornfeld, S.5
  • 14
    • 78751505790 scopus 로고    scopus 로고
    • Conservation and diversification of dileucine signal recognition by adaptor protein (AP) complex variants
    • Mattera R, Boehm M, Chaudhuri R, Prabhu Y, Bonifacino JS (2011) Conservation and diversification of dileucine signal recognition by adaptor protein (AP) complex variants. J Biol Chem 286:2022-2030.
    • (2011) J Biol Chem , vol.286 , pp. 2022-2030
    • Mattera, R.1    Boehm, M.2    Chaudhuri, R.3    Prabhu, Y.4    Bonifacino, J.S.5
  • 15
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • DOI 10.1016/S0092-8674(02)00735-3
    • Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ (2002) Molecular architecture and functional model of the endocytic AP2 complex. Cell 109:523-535. (Pubitemid 34564478)
    • (2002) Cell , vol.109 , Issue.4 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 18
    • 84874033425 scopus 로고    scopus 로고
    • Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1
    • in press
    • Ren X, Farias GG, Canagarajah B, Bonifacino JS, Hurley JH (in press) Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell 152:755-767.
    • Cell , vol.152 , pp. 755-767
    • Ren, X.1    Farias, G.G.2    Canagarajah, B.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 19
    • 5044252143 scopus 로고    scopus 로고
    • An ear-core interaction regulates the recruitment of the AP-3 complex to membranes
    • DOI 10.1016/j.devcel.2004.08.009, PII S1534580704002874
    • Lefrancois S, Janvier K, Boehm M, Ooi CE, Bonifacino JS (2004) An ear-core interaction regulates the recruitment of the AP-3 complex to membranes. Dev Cell 7: 619-625. (Pubitemid 39341846)
    • (2004) Developmental Cell , vol.7 , Issue.4 , pp. 619-625
    • Lefran, S.1    Janvier, K.2    Boehm, M.3    Ooi, C.E.4    Bonifacino, J.S.5
  • 21
    • 84875971537 scopus 로고    scopus 로고
    • Structural basis for the recognition of tyrosine-based sorting signals by the Mu3A subunit of the AP-3 adaptor complex
    • Feb [Epub ahead of print]
    • Mardones GA, Burgos PV, Lin Y, Kloer DP, Magadan JG, Hurley JH, Bonifacino JS (2013) Structural Basis for the Recognition of Tyrosine-based Sorting Signals by the Mu3A Subunit of the AP-3 Adaptor Complex. J Biol Chem. 2013 Feb 12. [Epub ahead of print].
    • (2013) J Biol Chem , vol.2013 , pp. 12
    • Mardones, G.A.1    Burgos, P.V.2    Lin, Y.3    Kloer, D.P.4    Magadan, J.G.5    Hurley, J.H.6    Bonifacino, J.S.7
  • 23
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • Di Paolo G, De Camilli P (2006) Phosphoinositides in cell regulation and membrane dynamics. Nature 443: 651-657. (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 24
    • 0029808103 scopus 로고    scopus 로고
    • A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 α subunit. Implications for the endocytic pathway
    • DOI 10.1074/jbc.271.34.20922
    • Gaidarov I, Chen Q, Falck JR, Reddy KK, Keen JH (1996) A functional phosphatidylinositol 3, 4, 5-trisphosphate/ phosphoinositide binding domain in the clathrin adaptor AP-2 ‡ subunit. Implications for the endocytic pathway. J Biol Chem 271:20922-20929. (Pubitemid 26281882)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20922-20929
    • Gaidarov, I.1    Chen, Q.2    Falck, J.R.3    Reddy, K.K.4    Keen, J.H.5
  • 25
    • 0037157830 scopus 로고    scopus 로고
    • A phosphatidylinositol (4,5)-bisphosphate binding site within mu 2-adaptin regulates clathrin-mediated endocytosis
    • Rohde G, Wenzel D, Haucke V (2002) A phosphatidylinositol (4, 5)-bisphosphate binding site within mu 2-adaptin regulates clathrin-mediated endocytosis. J Cell Biol 158:209-214.
    • (2002) J Cell Biol , vol.158 , pp. 209-214
    • Rohde, G.1    Wenzel, D.2    Haucke, V.3
  • 26
    • 21144445951 scopus 로고    scopus 로고
    • Phosphatidylinositol-(4,5)-bisphosphate regulates sorting signal recognition by the clathrin-associated adaptor complex AP2
    • DOI 10.1016/j.molcel.2005.04.019, PII S1097276505012827
    • Honing S, Ricotta D, Krauss M, Spate K, Spolaore B, Motley A, Robinson M, Robinson C, Haucke V, Owen DJ (2005) Phosphatidylinositol-(4, 5)-bisphosphate regulates sorting signal recognition by the clathrin-associated adaptor complex AP2. Mol Cell 18:519-531. (Pubitemid 40726229)
    • (2005) Molecular Cell , vol.18 , Issue.5 , pp. 519-531
    • Honing, S.1    Ricotta, D.2    Krauss, M.3    Spate, K.4    Spolaore, B.5    Motley, A.6    Robinson, M.7    Robinson, C.8    Haucke, V.9    Owen, D.J.10
  • 27
    • 0042591490 scopus 로고    scopus 로고
    • Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi
    • DOI 10.1016/S0092-8674(03)00603-2
    • Wang YJ, Wang J, Sun HQ, Martinez M, Sun YX, Macia E, Kirchhausen T, Albanesi JP, Roth MG, Yin HL (2003) Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the golgi. Cell 114:299-310. (Pubitemid 36962929)
    • (2003) Cell , vol.114 , Issue.3 , pp. 299-310
    • Wang, Y.J.1    Wang, J.2    Sun, H.Q.3    Martinez, M.4    Sun, Y.X.5    Macia, E.6    Kirchhausen, T.7    Albanesi, J.P.8    Roth, M.G.9    Yin, H.L.10
  • 28
    • 0037018152 scopus 로고    scopus 로고
    • Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis
    • DOI 10.1083/jcb.200108123
    • Conner SD, Schmid SL (2002) Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J Cell Biol 156:921-929. (Pubitemid 34839873)
    • (2002) Journal of Cell Biology , vol.156 , Issue.5 , pp. 921-929
    • Conner, S.D.1    Schmid, S.L.2
  • 29
    • 0037018156 scopus 로고    scopus 로고
    • Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
    • DOI 10.1083/jcb.200111068
    • Ricotta D, Conner SD, Schmid SL, von Figura K, Honing S (2002) Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol 156:791-795. (Pubitemid 34839862)
    • (2002) Journal of Cell Biology , vol.156 , Issue.5 , pp. 791-795
    • Ricotta, D.1    Conner, S.D.2    Schmid, S.L.3    Von Figura, K.4    Honing, S.5
  • 30
    • 0035810915 scopus 로고    scopus 로고
    • Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
    • DOI 10.1016/S0960-9822(01)00240-8
    • Olusanya O, Andrews PD, Swedlow JR, Smythe E (2001) Phosphorylation of threonine 156 of the mu2 subunit of hte AP2 complex is essential for endocytosis in vitro and in vivo. Curr Biol 11:896-900. (Pubitemid 32532818)
    • (2001) Current Biology , vol.11 , Issue.11 , pp. 896-900
    • Olusanya, O.1    Andrews, P.D.2    Swedlow, J.R.3    Smythe, E.4
  • 31
    • 0034118754 scopus 로고    scopus 로고
    • Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation
    • Umeda A, Meyerholz A, Ungewickell E (2000) Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation. Eur J Cell Biol 79:336-342. (Pubitemid 30345280)
    • (2000) European Journal of Cell Biology , vol.79 , Issue.5 , pp. 336-342
    • Umeda, A.1    Meyerholz, A.2    Ungewickell, E.3
  • 32
    • 38149068433 scopus 로고    scopus 로고
    • The small G proteins of the arf family and their regulators
    • Annual Reviews Palo Alto
    • Gillingham AK, Munro S. The small G proteins of the arf family and their regulators. (2007) Annu Rev Cell Dev Biol. Annual Reviews, Palo Alto, pp. 579-611.
    • (2007) Annu Rev Cell Dev Biol , pp. 579-611
    • Gillingham, A.K.1    Munro, S.2
  • 33
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators: Roles in membrane transport, development and disease
    • Donaldson JG, Jackson CL (2011) ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nat Rev Mol Cell Biol 12:362-375.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 34
    • 84856760126 scopus 로고    scopus 로고
    • A structurebased mechanism for Arf1-dependent recruitment of coatomer to membranes
    • Yu XC, Breitman M, Goldberg J (2012) A structurebased mechanism for Arf1-dependent recruitment of coatomer to membranes. Cell 148:530-542.
    • (2012) Cell , vol.148 , pp. 530-542
    • Yu, X.C.1    Breitman, M.2    Goldberg, J.3
  • 35
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE (1991) ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67:239-253. (Pubitemid 121001440)
    • (1991) Cell , vol.67 , Issue.2 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 36
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • DOI 10.1016/0092-8674(93)90277-W
    • Stamnes MA, Rothman JE (1993) The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73:999-1005. (Pubitemid 23165614)
    • (1993) Cell , vol.73 , Issue.5 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 37
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • DOI 10.1083/jcb.123.3.561
    • Traub LM, Ostrom JA, Kornfeld S (1993) Biochemical dissection of AP-1 recruitment onto Golgi membranes. J Cell Biol 123:561-573. (Pubitemid 23324914)
    • (1993) Journal of Cell Biology , vol.123 , Issue.3 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 38
    • 0035890324 scopus 로고    scopus 로고
    • Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs)
    • DOI 10.1093/emboj/20.22.6265
    • Boehm M, Aguilar RC, Bonifacino JS (2001) Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO J 20:6265-6276. (Pubitemid 33078700)
    • (2001) EMBO Journal , vol.20 , Issue.22 , pp. 6265-6276
    • Boehm, M.1    Aguilar, R.C.2    Bonifacino, J.S.3
  • 39
    • 39049139459 scopus 로고    scopus 로고
    • Binding of cargo sorting signals to AP-1 enhances its association with ADP ribosylation factor 1-GTP
    • DOI 10.1083/jcb.200709037
    • Lee I, Doray B, Govero J, Kornfeld S (2008) Binding of cargo sorting signals to AP-1 enhances its association with ADP ribosylation factor 1-GTP. J Cell Biol 180: 467-472. (Pubitemid 351240696)
    • (2008) Journal of Cell Biology , vol.180 , Issue.3 , pp. 467-472
    • Lee, I.1    Doray, B.2    Govero, J.3    Kornfeld, S.4
  • 40
    • 0038825177 scopus 로고    scopus 로고
    • ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ
    • DOI 10.1083/jcb.200301006
    • Krauss M, Kinuta M, Wenk MR, De Camilli P, Takei K, Haucke V (2003) ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma. J Cell Biol 162:113-124. (Pubitemid 36859539)
    • (2003) Journal of Cell Biology , vol.162 , Issue.1 , pp. 113-124
    • Krauss, M.1    Kinuta, M.2    Wenk, M.R.3    De Camilli, P.4    Takei, K.5    Haucke, V.6
  • 41
    • 34548420952 scopus 로고    scopus 로고
    • ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin
    • DOI 10.1016/j.cellsig.2007.07.015, PII S0898656807002318
    • Poupart M-E, Fessart D, Cotton M, Laporte SA, Claing A (2007) ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin. Cell Signal 19:2370-2378. (Pubitemid 47361691)
    • (2007) Cellular Signalling , vol.19 , Issue.11 , pp. 2370-2378
    • Poupart, M.-E.1    Fessart, D.2    Cotton, M.3    Laporte, S.A.4    Claing, A.5
  • 44
    • 0032540419 scopus 로고    scopus 로고
    • Association of the AP-3 adaptor complex with clathrin
    • DOI 10.1126/science.280.5362.431
    • Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998) Association of the AP-3 adaptor complex with clathrin. Science 280:431-434. (Pubitemid 28208164)
    • (1998) Science , vol.280 , Issue.5362 , pp. 431-434
    • Dell'Angelica, E.C.1    Klumperman, J.2    Stoorvogel, W.3    Bonifacino, J.S.4
  • 45
    • 84864634144 scopus 로고    scopus 로고
    • The first five seconds in the life of a clathrin-coated pit
    • Cocucci E, Aguet F, Boulant S, Kirchhausen T (2012) The first five seconds in the life of a clathrin-coated pit. Cell 150:495-507.
    • (2012) Cell , vol.150 , pp. 495-507
    • Cocucci, E.1    Aguet, F.2    Boulant, S.3    Kirchhausen, T.4
  • 46
    • 55549125212 scopus 로고    scopus 로고
    • Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding
    • Krauss M, Jia JY, Roux A, Beck R, Wieland FT, De Camilli P, Haucke V (2008) Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding. J Biol Chem 283:27717-27723.
    • (2008) J Biol Chem , vol.283 , pp. 27717-27723
    • Krauss, M.1    Jia, J.Y.2    Roux, A.3    Beck, R.4    Wieland, F.T.5    De Camilli, P.6    Haucke, V.7
  • 47
    • 50949133967 scopus 로고    scopus 로고
    • Arf family GTP loading is activated by, and generates, positive membrane curvature
    • Lundmark R, Doherty GJ, Vallis Y, Peter BJ, McMahon HT (2008) Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem J 414:189-194.
    • (2008) Biochem J , vol.414 , pp. 189-194
    • Lundmark, R.1    Doherty, G.J.2    Vallis, Y.3    Peter, B.J.4    McMahon, H.T.5
  • 48
    • 77954382701 scopus 로고    scopus 로고
    • Dynamic structure of membrane-anchored Arf center dot GTP
    • Liu Y, Kahn RA, Prestegard JH (2010) Dynamic structure of membrane-anchored Arf center dot GTP. Nat Struct Mol Biol 17:876-U128.
    • (2010) Nat Struct Mol Biol , vol.17
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 49
    • 1442317538 scopus 로고    scopus 로고
    • BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
    • DOI 10.1126/science.1092586
    • Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJG, Evans PR, McMahon HT (2004) BAR domains as sensors of membrane curvature: The amphiphysin BAR structure. Science 303:495-499. (Pubitemid 38120842)
    • (2004) Science , vol.303 , Issue.5657 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6    McMahon, H.T.7
  • 51
    • 84879037961 scopus 로고    scopus 로고
    • A novel GTPbinding protein-adaptor protein complex responsible for export of Vangl2 from the trans golgi network
    • Guo Y, Zanetti G, Schekman R (2013) A novel GTPbinding protein-adaptor protein complex responsible for export of Vangl2 from the trans golgi network. eLife. Available at: http://dx.doi.org/10.7554/eLife.00160.
    • (2013) ELife
    • Guo, Y.1    Zanetti, G.2    Schekman, R.3


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