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Volumn 8, Issue 4, 2007, Pages 414-430

Rab11-FIP3 is critical for the structural integrity of the endosomal recycling compartment

Author keywords

Coiled coil; Endosomal recycling compartment; Nuf; Rab11; Rab11 FIP3

Indexed keywords

CARRIER PROTEIN; PROTEIN RAB11 FIP3; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 33947255109     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2007.00543.x     Document Type: Article
Times cited : (59)

References (59)
  • 2
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich O, Reinsch S, Urbe S, Zerial M, Parton RG. Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol 1996; 135: 913-924.
    • (1996) J Cell Biol , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 3
    • 0034714574 scopus 로고    scopus 로고
    • Rab11b is essential for recycling of transferrin to the plasma membrane
    • Schlierf B, Fey GH, Hauber J, Hocke GM, Rosorius O. Rab11b is essential for recycling of transferrin to the plasma membrane. Exp Cell Res 2000; 259: 257-265.
    • (2000) Exp Cell Res , vol.259 , pp. 257-265
    • Schlierf, B.1    Fey, G.H.2    Hauber, J.3    Hocke, G.M.4    Rosorius, O.5
  • 5
    • 2442648748 scopus 로고    scopus 로고
    • Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis
    • Horgan CP, Walsh M, Zurawski TH, McCaffrey MW. Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis. Biochem Biophys Res Commun 2004; 319: 83-94.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 83-94
    • Horgan, C.P.1    Walsh, M.2    Zurawski, T.H.3    McCaffrey, M.W.4
  • 8
    • 0036921649 scopus 로고    scopus 로고
    • Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells
    • Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW. Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells. Biochem Biophys Res Commun 2002; 299: 770-779.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 770-779
    • Wallace, D.M.1    Lindsay, A.J.2    Hendrick, A.G.3    McCaffrey, M.W.4
  • 9
    • 0037178832 scopus 로고    scopus 로고
    • Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain
    • Lindsay AJ, McCaffrey MW. Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. J Biol Chem 2002; 277: 27193-27199.
    • (2002) J Biol Chem , vol.277 , pp. 27193-27199
    • Lindsay, A.J.1    McCaffrey, M.W.2
  • 10
    • 2342570318 scopus 로고    scopus 로고
    • Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis
    • Fan GH, Lapierre LA, Goldenring JR, Sai J., Richmond A. Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis. Mol Biol Cell 2004; 15: 2456-2469.
    • (2004) Mol Biol Cell , vol.15 , pp. 2456-2469
    • Fan, G.H.1    Lapierre, L.A.2    Goldenring, J.R.3    Sai, J.4    Richmond, A.5
  • 11
    • 0034502463 scopus 로고    scopus 로고
    • A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes
    • Prekeris R, Klumperman J, Scheller RH. A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes. Mol Cell 2000; 6: 1437-1448.
    • (2000) Mol Cell , vol.6 , pp. 1437-1448
    • Prekeris, R.1    Klumperman, J.2    Scheller, R.H.3
  • 12
    • 0038299239 scopus 로고    scopus 로고
    • Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout
    • Hickson GR, Matheson J, Riggs B, Maier VH, Fielding AB, Prekeris R, Sullivan W, Barr FA, Gould GW. Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout. Mol Biol Cell 2003; 14: 2908-2920.
    • (2003) Mol Biol Cell , vol.14 , pp. 2908-2920
    • Hickson, G.R.1    Matheson, J.2    Riggs, B.3    Maier, V.H.4    Fielding, A.B.5    Prekeris, R.6    Sullivan, W.7    Barr, F.A.8    Gould, G.W.9
  • 13
    • 0035845640 scopus 로고    scopus 로고
    • Arfophilin is a common target of both class II and class III ADP-ribosylation factors
    • Shin OH, Couvillon AD, Exton JH. Arfophilin is a common target of both class II and class III ADP-ribosylation factors. Biochemistry 2001; 40: 10846-10852.
    • (2001) Biochemistry , vol.40 , pp. 10846-10852
    • Shin, O.H.1    Couvillon, A.D.2    Exton, J.H.3
  • 16
    • 0142123246 scopus 로고    scopus 로고
    • Actin cytoskeleton remodeling during early Drosophila furrow formation requires recycling endosomal components nuclear-fallout and Rab11
    • Riggs B, Rothwell W, Mische S, Hickson GR, Matheson J, Hays TS, Gould GW, Sullivan W. Actin cytoskeleton remodeling during early Drosophila furrow formation requires recycling endosomal components nuclear-fallout and Rab11. J Cell Biol 2003; 163: 143-154.
    • (2003) J Cell Biol , vol.163 , pp. 143-154
    • Riggs, B.1    Rothwell, W.2    Mische, S.3    Hickson, G.R.4    Matheson, J.5    Hays, T.S.6    Gould, G.W.7    Sullivan, W.8
  • 17
    • 24144503375 scopus 로고    scopus 로고
    • Asymmetric Rab 11 endosomes regulate delta recycling and specify cell fate in the Drosophila nervous system
    • Emery G, Hutterer A, Berdnik D, Mayer B, Wirtz-Peitz F, Gaitan MG, Knoblich JA. Asymmetric Rab 11 endosomes regulate delta recycling and specify cell fate in the Drosophila nervous system. Cell 2005; 122: 763-773.
    • (2005) Cell , vol.122 , pp. 763-773
    • Emery, G.1    Hutterer, A.2    Berdnik, D.3    Mayer, B.4    Wirtz-Peitz, F.5    Gaitan, M.G.6    Knoblich, J.A.7
  • 18
    • 33744532148 scopus 로고    scopus 로고
    • Recycling endosomes
    • van Ijzendoorn SC. Recycling endosomes. J Cell Sci 2006; 119: 1679-1681.
    • (2006) J Cell Sci , vol.119 , pp. 1679-1681
    • van Ijzendoorn, S.C.1
  • 19
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2: 107-117.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 20
    • 0034965057 scopus 로고    scopus 로고
    • Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells
    • Lin SX, Grant B, Hirsh D, Maxfield FR. Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells. Nat Cell Biol 2001; 3: 567-572.
    • (2001) Nat Cell Biol , vol.3 , pp. 567-572
    • Lin, S.X.1    Grant, B.2    Hirsh, D.3    Maxfield, F.R.4
  • 21
    • 0034965059 scopus 로고    scopus 로고
    • Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling
    • Grant B, Zhang Y, Paupard MC, Lin SX, Hall DH, Hirsh D. Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling. Nat Cell Biol 2001; 3: 573-579.
    • (2001) Nat Cell Biol , vol.3 , pp. 573-579
    • Grant, B.1    Zhang, Y.2    Paupard, M.C.3    Lin, S.X.4    Hall, D.H.5    Hirsh, D.6
  • 22
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers"and contains a calmodulin-binding IQ motif
    • Mu FT, Callaghan JM, Steele-Mortimer O, Stenmark H, Parton RG, Campbell PL, McCluskey J, Yeo JP, Tock EP, Toh fBH. EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers"and contains a calmodulin-binding IQ motif. J Biol Chem 1995; 270: 13503-13511.
    • (1995) J Biol Chem , vol.270 , pp. 13503-13511
    • Mu, F.T.1    Callaghan, J.M.2    Steele-Mortimer, O.3    Stenmark, H.4    Parton, R.G.5    Campbell, P.L.6    McCluskey, J.7    Yeo, J.P.8    Tock, E.P.9    Toh, B.H.10
  • 23
    • 0032510238 scopus 로고    scopus 로고
    • Membrane sorting. Endosome marker is fat not fiction
    • Schmid SL, Cullis PR. Membrane sorting. Endosome marker is fat not fiction. Nature 1998; 392: 135-136.
    • (1998) Nature , vol.392 , pp. 135-136
    • Schmid, S.L.1    Cullis, P.R.2
  • 24
    • 0026586004 scopus 로고
    • Gamma-tubulin: The microtubule organizer?
    • Oakley BR. Gamma-tubulin: The microtubule organizer? Trends Cell Biol 1992; 2: 1-5.
    • (1992) Trends Cell Biol , vol.2 , pp. 1-5
    • Oakley, B.R.1
  • 26
    • 2542468981 scopus 로고    scopus 로고
    • Dual-polarization interferometry: An analytical technique to measure changes in protein structure in real time, to determine the stoichiometry of binding events, and to differentiate between specific and nonspecific interactions
    • Swann MJ, Peel LL, Carrington S, Freeman NJ. Dual-polarization interferometry: An analytical technique to measure changes in protein structure in real time, to determine the stoichiometry of binding events, and to differentiate between specific and nonspecific interactions. Anal Biochem 2004; 329: 190-198.
    • (2004) Anal Biochem , vol.329 , pp. 190-198
    • Swann, M.J.1    Peel, L.L.2    Carrington, S.3    Freeman, N.J.4
  • 28
    • 3342887805 scopus 로고    scopus 로고
    • Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis
    • Lindsay AJ, McCaffrey MW. Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis. FEBS Lett 2004; 571: 86-92.
    • (2004) FEBS Lett , vol.571 , pp. 86-92
    • Lindsay, A.J.1    McCaffrey, M.W.2
  • 29
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham AK, Munro S. Long coiled-coil proteins and membrane traffic. Biochim Biophys Acta 2003; 1641: 71-85.
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 30
    • 33750437407 scopus 로고    scopus 로고
    • Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes
    • Eathiraj S, Mishra A, Prekeris R, Lambright DG. Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes. J Mol Biol 2006; 364: 121-135.
    • (2006) J Mol Biol , vol.364 , pp. 121-135
    • Eathiraj, S.1    Mishra, A.2    Prekeris, R.3    Lambright, D.G.4
  • 31
    • 33750365184 scopus 로고    scopus 로고
    • Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/arfophilin-1
    • Shiba T, Koga H, Shin HW, Kawasaki M, Kato R, Nakayama K, Wakatsuki S. Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/arfophilin-1. Proc Natl Acad Sci U S A 2006; 103: 15416-15421.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15416-15421
    • Shiba, T.1    Koga, H.2    Shin, H.W.3    Kawasaki, M.4    Kato, R.5    Nakayama, K.6    Wakatsuki, S.7
  • 32
    • 0036296761 scopus 로고    scopus 로고
    • The novel Rab11-FIP/Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities
    • Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW. The novel Rab11-FIP/ Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities. Biochem Biophys Res Commun 2002; 292: 909-915.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 909-915
    • Wallace, D.M.1    Lindsay, A.J.2    Hendrick, A.G.3    McCaffrey, M.W.4
  • 34
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004; 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 35
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two- and three-stranded coiled coils
    • Wolf E, Kim PS, Berger B. MultiCoil: A program for predicting two- and three-stranded coiled coils. Protein Sci 1997; 6: 1179-1189.
    • (1997) Protein Sci , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 36
    • 0035900013 scopus 로고    scopus 로고
    • Alpha beta Spectrin coiled coil association at the tetramerization site
    • Mehboob S, Luo BH, Patel BM, Fung LW. alpha beta Spectrin coiled coil association at the tetramerization site. Biochemistry 2001; 40: 12457-12464.
    • (2001) Biochemistry , vol.40 , pp. 12457-12464
    • Mehboob, S.1    Luo, B.H.2    Patel, B.M.3    Fung, L.W.4
  • 37
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils
    • Lau SY, Taneja AK, Hodges RS. Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils. J Biol Chem 1984; 259: 13253-13261.
    • (1984) J Biol Chem , vol.259 , pp. 13253-13261
    • Lau, S.Y.1    Taneja, A.K.2    Hodges, R.S.3
  • 38
    • 0026795513 scopus 로고
    • Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils
    • Zhou NE, Kay CM, Hodges RS. Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils. J Biol Chem 1992; 267: 2664-2670.
    • (1992) J Biol Chem , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 39
    • 0027146666 scopus 로고
    • Controlled formation of model homo- and heterodimer coiled coil polypeptides
    • Graddis TJ, Myszka DG, Chaiken IM. Controlled formation of model homo- and heterodimer coiled coil polypeptides. Biochemistry 1993; 32: 12664-12671.
    • (1993) Biochemistry , vol.32 , pp. 12664-12671
    • Graddis, T.J.1    Myszka, D.G.2    Chaiken, I.M.3
  • 40
    • 0242662225 scopus 로고    scopus 로고
    • Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain
    • Choy N, Raussens V, Narayanaswami V. Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain. J Mol Biol 2003; 334: 527-539.
    • (2003) J Mol Biol , vol.334 , pp. 527-539
    • Choy, N.1    Raussens, V.2    Narayanaswami, V.3
  • 41
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo P, Baldwin RL. Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 1997; 36: 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 42
    • 0033607791 scopus 로고    scopus 로고
    • Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures
    • Maroun RG, Krebs D, El Antri S, Deroussent A, Lescot E, Troalen F, Porumb H, Goldberg ME, Fermandjian S. Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures. J Biol Chem 1999; 274: 34174-34185.
    • (1999) J Biol Chem , vol.274 , pp. 34174-34185
    • Maroun, R.G.1    Krebs, D.2    El Antri, S.3    Deroussent, A.4    Lescot, E.5    Troalen, F.6    Porumb, H.7    Goldberg, M.E.8    Fermandjian, S.9
  • 43
    • 0039182128 scopus 로고    scopus 로고
    • FTIR-Spectroscopy of multistranded coiled coil proteins
    • Heimburg T, Schunemann J, Weber K, Geisler N. FTIR-Spectroscopy of multistranded coiled coil proteins. Biochemistry 1999; 38: 12727-12734.
    • (1999) Biochemistry , vol.38 , pp. 12727-12734
    • Heimburg, T.1    Schunemann, J.2    Weber, K.3    Geisler, N.4
  • 44
    • 0030019825 scopus 로고    scopus 로고
    • Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins
    • Heimburg T, Schuenemann J, Weber K, Geisler N. Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins. Biochemistry 1996; 35: 1375-1382.
    • (1996) Biochemistry , vol.35 , pp. 1375-1382
    • Heimburg, T.1    Schuenemann, J.2    Weber, K.3    Geisler, N.4
  • 45
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GN Jr, Fillers JP, Cohen C. Tropomyosin crystal structure and muscle regulation. J Mol Biol 1986; 192: 111-131.
    • (1986) J Mol Biol , vol.192 , pp. 111-131
    • Phillips Jr., G.N.1    Fillers, J.P.2    Cohen, C.3
  • 46
    • 3242687293 scopus 로고    scopus 로고
    • Using light scattering to determine the stoichiometry of protein complexes
    • Mogridge J. Using light scattering to determine the stoichiometry of protein complexes. Methods Mol Biol 2004; 261: 113-118.
    • (2004) Methods Mol Biol , vol.261 , pp. 113-118
    • Mogridge, J.1
  • 47
    • 4344685822 scopus 로고    scopus 로고
    • Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins
    • Rose A, Meier I. Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins. Cell Mol Life Sci 2004; 61: 1996-2009.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1996-2009
    • Rose, A.1    Meier, I.2
  • 48
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr FA, Short B. Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 2003; 15: 405-413.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 49
    • 0034681147 scopus 로고    scopus 로고
    • A Rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis
    • Cox D, Lee DJ, Dale BM, Calafat J, Greenberg S. A Rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis. Proc Natl Acad Sci U S A 2000; 97: 680-685.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 680-685
    • Cox, D.1    Lee, D.J.2    Dale, B.M.3    Calafat, J.4    Greenberg, S.5
  • 50
    • 24144477936 scopus 로고    scopus 로고
    • Drosophila exocyst components Sec5, Sec6, and Sec15 regulate DE-cadherin trafficking from recycling endosomes to the plasma membrane
    • Langevin J, Morgan MJ, Sibarita JB, Aresta S, Murthy M, Schwarz T, Camonis J, Bellaiche Y. Drosophila exocyst components Sec5, Sec6, and Sec15 regulate DE-cadherin trafficking from recycling endosomes to the plasma membrane. Dev Cell 2005; 9: 355-376.
    • (2005) Dev Cell , vol.9 , pp. 355-376
    • Langevin, J.1    Morgan, M.J.2    Sibarita, J.B.3    Aresta, S.4    Murthy, M.5    Schwarz, T.6    Camonis, J.7    Bellaiche, Y.8
  • 51
  • 52
    • 16844362958 scopus 로고    scopus 로고
    • Hypoxia stimulates carcinoma invasion by stabilizing microtubules and promoting the Rab11 trafficking of the alpha6beta4 integrin
    • Yoon SO, Shin S, Mercurio AM. Hypoxia stimulates carcinoma invasion by stabilizing microtubules and promoting the Rab11 trafficking of the alpha6beta4 integrin. Cancer Res 2005; 65: 2761-2769.
    • (2005) Cancer Res , vol.65 , pp. 2761-2769
    • Yoon, S.O.1    Shin, S.2    Mercurio, A.M.3
  • 53
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis MA, Morrow JS. Spectrin tethers and mesh in the biosynthetic pathway. J Cell Sci 2000; 113: 2331-2343.
    • (2000) J Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 54
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay BK, Williamson MP, Sudol M. The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J 2000; 14: 231-241.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 55
  • 56
    • 0036156394 scopus 로고    scopus 로고
    • Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin
    • Lin SX, Gundersen GG, Maxfield FR. Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin. Mol Biol Cell 2002; 13: 96-109.
    • (2002) Mol Biol Cell , vol.13 , pp. 96-109
    • Lin, S.X.1    Gundersen, G.G.2    Maxfield, F.R.3
  • 57
    • 0142026241 scopus 로고    scopus 로고
    • Rab11b resides in a vesicular compartment distinct from Rab11a in parietal cells and other epithelial cells
    • Lapierre LA, Dorn MC, Zimmerman CF, Navarre J, Burnette JO, Goldenring JR. Rab11b resides in a vesicular compartment distinct from Rab11a in parietal cells and other epithelial cells. Exp Cell Res 2003; 290: 322-331.
    • (2003) Exp Cell Res , vol.290 , pp. 322-331
    • Lapierre, L.A.1    Dorn, M.C.2    Zimmerman, C.F.3    Navarre, J.4    Burnette, J.O.5    Goldenring, J.R.6
  • 58
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network
    • Wilcke M, Johannes L, Galli T, Mayau V, Goud B, Salamero J. Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network. J Cell Biol 2000; 151: 1207-1220.
    • (2000) J Cell Biol , vol.151 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6
  • 59
    • 0029610381 scopus 로고
    • Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex
    • Stinchcombe JC, Nomoto H, Cutler DF, Hopkins CR. Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex. J Cell Biol 1995; 131: 1387-1401.
    • (1995) J Cell Biol , vol.131 , pp. 1387-1401
    • Stinchcombe, J.C.1    Nomoto, H.2    Cutler, D.F.3    Hopkins, C.R.4


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