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Volumn , Issue , 2009, Pages 39-48

The PACSIN proteins and their role in membrane trafficking

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EID: 76449116752     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781498712798-10     Document Type: Chapter
Times cited : (5)

References (48)
  • 1
    • 0030770817 scopus 로고    scopus 로고
    • Fap52, a novel, sh3 domain-containing focal adhesion protein
    • Meriläinen J, Lehto VP, Wasenius VM. FAP52, a novel, SH3 domain-containing focal adhesion protein. J Biol Chem 1997; 272:23278-23284.
    • (1997) J Biol Chem , vol.272 , pp. 23278-23284
    • Meriläinen, J.1    Lehto, V.P.2    Wasenius, V.M.3
  • 2
    • 15144353034 scopus 로고    scopus 로고
    • Pacsin, a brain protein that is upregulated upon differentiation into neuronal cells
    • Plomann M, Lange R, Vopper G et al. PACSIN, a brain protein that is upregulated upon differentiation into neuronal cells. Eur J Biochem 1998; 256:201-211.
    • (1998) Eur J Biochem , vol.256 , pp. 201-211
    • Plomann, M.1    Lange, R.2    Vopper, G.3
  • 3
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin i, a synaptic dynamin-binding protein that associates with the neural wiskott-aldrich syndrome protein
    • Qualmann B, Roos J, DiGregorio PJ et al. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol Biol Cell 1999; 10:501-513.
    • (1999) Mol Biol Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3
  • 4
    • 0033016181 scopus 로고    scopus 로고
    • Pacsin 2, a novel member of the pacsin family of cytoplasmic adapter proteins
    • Ritter B, Modregger J, Paulsson M et al. PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins. FEBS Lett 1999; 454:356-362.
    • (1999) FEBS Lett , vol.454 , pp. 356-362
    • Ritter, B.1    Modregger, J.2    Paulsson, M.3
  • 5
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B, Kelly RB. Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J Cell Biol 2000; 148:1047-1062.
    • (2000) J Cell Biol , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 6
    • 0034503124 scopus 로고    scopus 로고
    • All three pacsin isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger J, Ritter B, Witter B et al. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J Cell Sci 2000; 113:4511-4521.
    • (2000) J Cell Sci , vol.113 , pp. 4511-4521
    • Modregger, J.1    Ritter, B.2    Witter, B.3
  • 7
    • 0035834983 scopus 로고    scopus 로고
    • Pacsin 3 is a novel sh3 domain cytoplasmic adapter protein of the pacsin-syndapin-fap52 gene family
    • Sumoy L, Pluvinet R, Andreu N et al. PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family. Gene 2001; 262:199-205.
    • (2001) Gene , vol.262 , pp. 199-205
    • Sumoy, L.1    Pluvinet, R.2    Reu, N.3
  • 8
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskclcton
    • Kessels MM, Qualmann B. The syndapin protein family: linking membrane trafficking with the cytoskclcton. J Cell Sci 2004; 117:3077-3086.
    • (2004) J Cell Sci , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 9
    • 33745751770 scopus 로고    scopus 로고
    • Endocytosis and synaptic removal of nr3a-containing nmda receptors by pacsin 1/syndapin 1
    • Perez-Otano I, Lujan R, Tavalin SJ et al. Endocytosis and synaptic removal of NR3A-containing NMDA receptors by PACSIN 1/syndapin 1. Nat Ncurosci 2006; 9:611-621.
    • (2006) Nat Ncurosci , vol.9 , pp. 611-621
    • Perez-Otano, I.1    Lujan, R.2    Tavalin, S.J.3
  • 10
    • 0034331252 scopus 로고    scopus 로고
    • Pacsin2 is a regulator of the metalloprotease/disintegrin adam 13
    • Cousin H, Gaultier A, Blcux C et al. PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM 13. Dev Biol 2000; 227:197-210.
    • (2000) Dev Biol , vol.227 , pp. 197-210
    • Cousin, H.1    Gaultier, A.2    Blcux, C.3
  • 11
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskclcton and membrane deformation by a novel membrane tubulation domain of pch proteins is involved in endocytosis
    • Tsujita K, Suetsugu S, Sasaki N et al. Coordination between the actin cytoskclcton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol 2006; 172:269-279.
    • (2006) J Cell Biol , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3
  • 12
    • 0031194076 scopus 로고    scopus 로고
    • A cdc42 target protein with homology to the nonkinase domain of fer has a potential role in regulating the actin cytoskclcton
    • Aspenström P. A Cdc42 target protein with homology to the nonkinase domain of FER has a potential role in regulating the actin cytoskclcton. Curr Biol 1997; 7:479-487.
    • (1997) Curr Biol , vol.7 , pp. 479-487
    • Aspenström, P.1
  • 13
    • 33751204126 scopus 로고    scopus 로고
    • Pombc cdcl5 homology proteins: Regulators of membrane dynamics and the actin cytoskclcton
    • Aspenstrom P, Fransson A, Richnau N. Pombc Cdcl5 homology proteins: regulators of membrane dynamics and the actin cytoskclcton. Trends Biochem Sci 2006; 31:670-679.
    • (2006) Trends Biochem Sci , vol.31 , pp. 670-679
    • Aspenstrom, P.1    Fransson, A.2    Richnau, N.3
  • 14
    • 33847343505 scopus 로고    scopus 로고
    • Pombc cdcl5 homology (Pch) proteins: Coordinators of membrane-cytoskeletal interactions
    • Chitu V, Stanley ER. Pombc Cdcl5 homology (PCH) proteins: coordinators of membrane-cytoskeletal interactions. Trends Cell Biol 2007; 17:145-156.
    • (2007) Trends Cell Biol , vol.17 , pp. 145-156
    • Chitu, V.1    Stanley, E.R.2
  • 15
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of fcho2 f-bar domain: A dimerizing and membrane recruitment module that effects membrane curvature
    • Henne WM, Kent HM, Ford MG et al. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 2007; 15:839-852.
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.3
  • 16
    • 34249316521 scopus 로고    scopus 로고
    • Curved efc/f-bar-domain dimers arc joined end to end into a filament for membrane invagination in endocytosis
    • Shimada A, Niwa H, Tsujita K et al. Curved EFC/F-BAR-domain dimers arc joined end to end into a filament for membrane invagination in endocytosis. Cell 2007; 129:761-772.
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1    Niwa, H.2    Tsujita, K.3
  • 17
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskclcton cooperatively regulate plasma membrane invagination by bar and f-bar proteins
    • Itoh T, Erdmann KS, Roux A et al. Dynamin and the actin cytoskclcton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 2005; 9:791-804.
    • (2005) Dev Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3
  • 18
    • 0037150113 scopus 로고    scopus 로고
    • Focal adhesion protein fap52 self-associates through a sequence conserved among the members of the pch family proteins
    • Nikki M, Merilainen J, Lehto VP. Focal adhesion protein FAP52 self-associates through a sequence conserved among the members of the PCH family proteins. Biochemistry 2002; 41:6320-6329.
    • (2002) Biochemistry , vol.41 , pp. 6320-6329
    • Nikki, M.1    Merilainen, J.2    Lehto, V.P.3
  • 19
    • 33745000739 scopus 로고    scopus 로고
    • Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization
    • Kessels MM, Qualmann B. Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization. J Biol Chem 2006; 281:13285-13299.
    • (2006) J Biol Chem , vol.281 , pp. 13285-13299
    • Kessels, M.M.1    Qualmann, B.2
  • 20
    • 33846420997 scopus 로고    scopus 로고
    • Pacsin 1 forms tetramers via its n-terminal f-bar domain
    • Halbach A, Morgelin M, Baumgarten M et al. PACSIN 1 forms tetramers via its N-terminal F-BAR domain. FEBS J 2007; 274:773-782.
    • (2007) FEBS J , vol.274 , pp. 773-782
    • Halbach, A.1    Morgelin, M.2    Baumgarten, M.3
  • 21
    • 34447316407 scopus 로고    scopus 로고
    • Syndapin i and endophilin i bind overlapping proline-rich regions of dynamin i: Role in synaptic vesicle endocytosis
    • Anggono V, Robinson PJ. Syndapin I and endophilin I bind overlapping proline-rich regions of dynamin I: role in synaptic vesicle endocytosis. J Neurochem 2007; 102:931-943.
    • (2007) J Neurochem , vol.102 , pp. 931-943
    • Anggono, V.1    Robinson, P.J.2
  • 22
    • 0036796261 scopus 로고    scopus 로고
    • Pacsin 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic huntingtons disease brains
    • Modregger J, DiProspero NA, Charles V et al. PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntingtons disease brains. Hum Mol Genet 2002; 11:2547-2558.
    • (2002) Hum Mol Genet , vol.11 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.A.2    Charles, V.3
  • 23
    • 4444374647 scopus 로고    scopus 로고
    • Mutually exclusive interactions of ehd1 with gs32 and syndapin ii
    • Xu Y, Shi H, Wei S et al. Mutually exclusive interactions of EHD1 with GS32 and syndapin II. Mol Membr Biol 2004; 21:269-277.
    • (2004) Mol Membr Biol , vol.21 , pp. 269-277
    • Xu, Y.1    Shi, H.2    Wei, S.3
  • 24
    • 23144467137 scopus 로고    scopus 로고
    • Ehd proteins associate with syndapin i and ii and such interactions play a crucial role in endosomal recycling
    • Braun A, Pinyol R, Dahlhaus R et al. EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling. Mol Biol Cell 2005; 16:3642-3658.
    • (2005) Mol Biol Cell , vol.16 , pp. 3642-3658
    • Braun, A.1    Pinyol, R.2    Dahlhaus, R.3
  • 25
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate n-wasp in receptor-mediated endocytosis
    • Kessels MM, Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J 2002; 21:6083-6094.
    • (2002) EMBO J , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 26
    • 0033147449 scopus 로고    scopus 로고
    • Sh3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
    • Simpson F, Hussain NK, Qualmann B et al. SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation. Nat Cell Biol 1999; 1:119-124.
    • (1999) Nat Cell Biol , vol.1 , pp. 119-124
    • Simpson, F.1    Hussain, N.K.2    Qualmann, B.3
  • 27
    • 10744231094 scopus 로고    scopus 로고
    • Impairing actin filament or syndapin functions promotes accumulation of clathrin-coated vesicles at the apical plasma membrane of acinar epithelial cells
    • Da Costa SR, Sou E, Xie J et al. Impairing actin filament or syndapin functions promotes accumulation of clathrin-coated vesicles at the apical plasma membrane of acinar epithelial cells. Mol Biol Cell 2003; 14:4397-4413.
    • (2003) Mol Biol Cell , vol.14 , pp. 4397-4413
    • Da Costa, S.R.1    Sou, E.2    Xie, J.3
  • 28
    • 0032736675 scopus 로고    scopus 로고
    • Essential role of phosphoinositide metabolism in synaptic vesicle recycling
    • Cremona O, Di Paolo G, Wenk MR et al. Essential role of phosphoinositide metabolism in synaptic vesicle recycling. Cell 1999; 99:179-188.
    • (1999) Cell , vol.99 , pp. 179-188
    • Cremona, O.1    Di Paolo, G.2    Wenk, M.R.3
  • 29
    • 0029024135 scopus 로고
    • Essential functions of synapsins i and ii in synaptic vesicle regulation
    • Rosahl TW, Spillane D, Missler M et al. Essential functions of synapsins I and II in synaptic vesicle regulation. Nature 1995; 375:488-493.
    • (1995) Nature , vol.375 , pp. 488-493
    • Rosahl, T.W.1    Spillane, D.2    Missler, M.3
  • 30
    • 0031867231 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways
    • Velier J, Kim M, Schwarz C et al. Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways. Exp Neurol 1998; 152:34-40.
    • (1998) Exp Neurol , vol.152 , pp. 34-40
    • Velier, J.1    Kim, M.2    Schwarz, C.3
  • 31
    • 0037192776 scopus 로고    scopus 로고
    • Fap52 regulates actin organization via binding to iilamin
    • Nikki M, Merilainen J, Lehto VP. FAP52 regulates actin organization via binding to iilamin. J Biol Chem 2002; 277:11432-11440.
    • (2002) J Biol Chem , vol.277 , pp. 11432-11440
    • Nikki, M.1    Merilainen, J.2    Lehto, V.P.3
  • 32
    • 33748917630 scopus 로고    scopus 로고
    • Interaction of spin90 with syndapin is implicated in clathrin-mediated endocytic pathway in fibroblasts
    • Kim SH, Choi HJ, Lee KW et al. Interaction of SPIN90 with syndapin is implicated in clathrin-mediated endocytic pathway in fibroblasts. Genes Cells 2006; 11:1197-1211.
    • (2006) Genes Cells , vol.11 , pp. 1197-1211
    • Kim, S.H.1    Choi, H.J.2    Lee, K.W.3
  • 33
    • 33646710836 scopus 로고    scopus 로고
    • Complexes of syndapin ii with dynamin ii promote vesicle formation at the trans-golgi network
    • Kessels MM, Dong J, Leibig W et al. Complexes of syndapin II with dynamin II promote vesicle formation at the trans-Golgi network. J Cell Sci 2006; 119:1504-1516.
    • (2006) J Cell Sci , vol.119 , pp. 1504-1516
    • Kessels, M.M.1    Dong, J.2    Leibig, W.3
  • 34
    • 18244394543 scopus 로고    scopus 로고
    • Novel cytosolic binding partners of the neural cell adhesion molecule: Mapping the binding domains of plc gamma, lanp, toad-64, syndapin, pp1 and pp2a
    • Büttner B, Kannicht C, Reutter W et al. Novel cytosolic binding partners of the neural cell adhesion molecule: mapping the binding domains of PLC gamma, LANP, TOAD-64, syndapin, PP1 and PP2A. Biochemistry 2005; 44:6938-6947.
    • (2005) Biochemistry , vol.44 , pp. 6938-6947
    • Büttner, B.1    Kannicht, C.2    Reutter, W.3
  • 35
    • 29244446227 scopus 로고    scopus 로고
    • The regulatory subunit of pde6 interacts with pacsin in photoreceptors
    • Houdart F, Girard-Nau N, Morin F et al. The regulatory subunit of PDE6 interacts with PACSIN in photoreceptors. Mol Vis 2005; 11:1061-1070.
    • (2005) Mol Vis , vol.11 , pp. 1061-1070
    • Houdart, F.1    Girard-Nau, N.2    Morin, F.3
  • 36
    • 0242580234 scopus 로고    scopus 로고
    • Pacsin3 binds adam12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor
    • Mori S, Tanaka M, Nanba D et al. PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J Biol Chem 2003; 278:46029-46034.
    • (2003) J Biol Chem , vol.278 , pp. 46029-46034
    • Mori, S.1    Tanaka, M.2    Nanba, D.3
  • 37
    • 33745818873 scopus 로고    scopus 로고
    • Pacsins bind to the trpv4 cation channel. Pacsin 3 modulates the subcellular localization of trpv4
    • Cuajungco MP, Grimm C, Oshima K et al. PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4. J Biol Chem 2006; 281:18753-18762.
    • (2006) J Biol Chem , vol.281 , pp. 18753-18762
    • Cuajungco, M.P.1    Grimm, C.2    Oshima, K.3
  • 38
    • 44449092146 scopus 로고    scopus 로고
    • Stimulus-specific modulation of the cation channel trpv4 by pacsin 3
    • D’Hoedt D, Owsianik G, Prenen J et al. Stimulus-specific modulation of the cation channel TRPV4 by PACSIN 3. J Biol Chem 2008; 283(10):6272-6280.
    • (2008) J Biol Chem , vol.283 , Issue.10 , pp. 6272-6280
    • D’Hoedt, D.1    Owsianik, G.2    Prenen, J.3
  • 39
    • 33847334259 scopus 로고    scopus 로고
    • Pacsin3 overexpression increases adipocyte glucose transport through glut1
    • Roach W, Plomann M. PACSIN3 overexpression increases adipocyte glucose transport through GLUT1. Biochem Biophys Res Commun 2007; 355:745-750.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 745-750
    • Roach, W.1    Plomann, M.2
  • 40
    • 0037157139 scopus 로고    scopus 로고
    • Identification of interaction partners of the cytosolic polyproline region of cd95 ligand (Cd 178)
    • Ghadimi MP, Sanzenbacher R, Thiede B et al. Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD 178). FEBS Lett 2002; 519:50-58.
    • (2002) FEBS Lett , vol.519 , pp. 50-58
    • Ghadimi, M.P.1    Sanzenbacher, R.2    Thiede, B.3
  • 41
    • 34548388779 scopus 로고    scopus 로고
    • A protcomic screen reveals novel fas ligand interacting proteins within nervous system schwann cells
    • Thornhill PB, Cohn JB, Drury G et al. A protcomic screen reveals novel Fas ligand interacting proteins within nervous system Schwann cells. FEBS Lett 2007; 581:4455-4462.
    • (2007) FEBS Lett , vol.581 , pp. 4455-4462
    • Thornhill, P.B.1    Cohn, J.B.2    Drury, G.3
  • 42
    • 0035854813 scopus 로고    scopus 로고
    • Ras/rac guanine nucleotide exchange factor mammalian son-of-sevenless interacts with pacsin 1/syndapin i, a regulator of endocytosis and the actin cyto-skclcton
    • Wasiak S, Quinn CC, Ritter B et al. Ras/Rac guanine nucleotide exchange factor mammalian Son-of-sevenless interacts with PACSIN 1/syndapin I, a regulator of endocytosis and the actin cyto-skclcton. J Biol Chem 2001; 276:26622-26628.
    • (2001) J Biol Chem , vol.276 , pp. 26622-26628
    • Wasiak, S.1    Quinn, C.C.2    Ritter, B.3
  • 43
    • 0035844186 scopus 로고    scopus 로고
    • Phosphorylation of a synaptic vesicle-associated protein by an inositol hexakisphosphate-regulated protein kinase
    • Hilton JM, Plomann M, Ritter B et al. Phosphorylation of a synaptic vesicle-associated protein by an inositol hexakisphosphate-regulated protein kinase. J Biol Chem 2001; 276:16341-16347.
    • (2001) J Biol Chem , vol.276 , pp. 16341-16347
    • Hilton, J.M.1    Plomann, M.2    Ritter, B.3
  • 44
    • 6344278697 scopus 로고    scopus 로고
    • Regulation of casein kinase-2 (Ck2) activity by inositol phosphates
    • Solyakov L, Cain K, Tracey BM et al. Regulation of casein kinase-2 (CK2) activity by inositol phosphates. J Biol Chem 2004; 279:43403-43410.
    • (2004) J Biol Chem , vol.279 , pp. 43403-43410
    • Solyakov, L.1    Cain, K.2    Tracey, B.M.3
  • 45
    • 33745726868 scopus 로고    scopus 로고
    • Syndapin i is the phosphorylation-regulated dynamin i partner in synaptic vesicle endocytosis
    • Anggono V, Smillie KJ, Graham ME et al. Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis. Nat Neurosci 2006; 9:752-760.
    • (2006) Nat Neurosci , vol.9 , pp. 752-760
    • Anggono, V.1    Smillie, K.J.2    Graham, M.E.3
  • 46
    • 37249036671 scopus 로고    scopus 로고
    • Activity-dependent control of bulk endocytosis by protein déphosphorylation in central nerve terminals
    • Clayton EL, Evans GJ, Cousin MA. Activity-dependent control of bulk endocytosis by protein déphosphorylation in central nerve terminals. J Physiol 2007; 585:687-691.
    • (2007) J Physiol , vol.585 , pp. 687-691
    • Clayton, E.L.1    Evans, G.J.2    Cousin, M.A.3
  • 47
    • 34447499146 scopus 로고    scopus 로고
    • The in vivo phosphorylation sites of rat brain dynamin i
    • Graham ME, Anggono V, Bache N et al. The in vivo phosphorylation sites of rat brain dynamin I. J Biol Chem 2007; 282:14695-14707.
    • (2007) J Biol Chem , vol.282 , pp. 14695-14707
    • Graham, M.E.1    Anggono, V.2    Bache, N.3
  • 48
    • 20044377268 scopus 로고    scopus 로고
    • Early changes in huntington’s disease patient brains involve alterations in cytoskeletal and synaptic elements
    • DiProspero NA, Chen EY, Charles V et al. Early changes in Huntington's disease patient brains involve alterations in cytoskeletal and synaptic elements. J Neurocytol 2004; 33:517-533.
    • (2004) J Neurocytol , vol.33 , pp. 517-533
    • DiProspero, N.A.1    Chen, E.Y.2    Charles, V.3


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