메뉴 건너뛰기




Volumn 34, Issue 8, 2014, Pages 1486-1499

Rab8 binding to immune cell-specific adaptor LAX facilitates formation of trans-golgi network-proximal CTLA-4 vesicles for surface expression

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; INTERLEUKIN 2; LAX PROTEIN; RAB PROTEIN; RAB8 PROTEIN; SMALL INTERFERING RNA; T LYMPHOCYTE RECEPTOR; TRIM PROTEIN; TUBULIN; UNCLASSIFIED DRUG; GERMINAL CENTER KINASES; LAX1 PROTEIN, HUMAN; LYMPHOCYTE ANTIGEN RECEPTOR; MONOMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SERINE THREONINE KINASE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84896512664     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01331-13     Document Type: Article
Times cited : (23)

References (63)
  • 1
    • 0028867420 scopus 로고
    • Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4
    • Tivol EA, Borriello F, Schweitzer AN, Lynch WP, Bluestone JA, Sharpe AH. 1995. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 3:541-547. http://dx.doi.org/10.1016/1074-7613(95)90125-6.
    • (1995) Immunity , vol.3 , pp. 541-547
    • Tivol, E.A.1    Borriello, F.2    Schweitzer, A.N.3    Lynch, W.P.4    Bluestone, J.A.5    Sharpe, A.H.6
  • 4
    • 38349074305 scopus 로고    scopus 로고
    • CTLA-4 disrupts ZAP70 microcluster formation with reduced T cell/APC dwell times and calcium mobilization
    • Schneider H, Smith X, Liu H, Bismuth G, Rudd CE. 2008. CTLA-4 disrupts ZAP70 microcluster formation with reduced T cell/APC dwell times and calcium mobilization. Eur. J. Immunol. 38:40-47. http://dx.doi.org/10.1002/eji.200737423.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 40-47
    • Schneider, H.1    Smith, X.2    Liu, H.3    Bismuth, G.4    Rudd, C.E.5
  • 5
    • 4444369694 scopus 로고    scopus 로고
    • B7-1 and B7-2 selectively recruit CTLA-4 and CD28 to the immunological synapse
    • Pentcheva-Hoang T, Egen JG, Wojnoonski K, Allison JP. 2004. B7-1 and B7-2 selectively recruit CTLA-4 and CD28 to the immunological synapse. Immunity 21:401-413. http://dx.doi.org/10.1016/j.immuni.2004.06.017.
    • (2004) Immunity , vol.21 , pp. 401-413
    • Pentcheva-Hoang, T.1    Egen, J.G.2    Wojnoonski, K.3    Allison, J.P.4
  • 7
    • 0030001318 scopus 로고    scopus 로고
    • Regulation of T cell receptor signaling by tyrosine phosphatase Syp association with CTLA-4
    • Marengère LEM, Waterhouse P, Duncan GS, Mittrücker HW, Feng GS, Mak TW. 1996. Regulation of T cell receptor signaling by tyrosine phosphatase Syp association with CTLA-4. Science 272:1170-1173. http://dx.doi.org/10.1126/science.272.5265.1170.
    • (1996) Science , vol.272 , pp. 1170-1173
    • Marengère, L.E.M.1    Waterhouse, P.2    Duncan, G.S.3    Mittrücker, H.W.4    Feng, G.S.5    Mak, T.W.6
  • 10
    • 13544271675 scopus 로고    scopus 로고
    • Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNAsynthetase by CTLA-4-Fc in human CD4 T cells
    • Boasso A, Herbeuval JP, Hardy AW, Winkler C, Shearer GM. 2005. Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNAsynthetase by CTLA-4-Fc in human CD4 T cells. Blood 105:1574-1581. http://dx.doi.org/10.1182/blood-2004-06-2089.
    • (2005) Blood , vol.105 , pp. 1574-1581
    • Boasso, A.1    Herbeuval, J.P.2    Hardy, A.W.3    Winkler, C.4    Shearer, G.M.5
  • 11
    • 33746933828 scopus 로고    scopus 로고
    • TGF-β-mediated suppression by CD4 CD25 T cells is facilitated by CTLA-4 signaling
    • Oida T, Xu L, Weiner HL, Kitani A, Strober W. 2006. TGF-β-mediated suppression by CD4 CD25 T cells is facilitated by CTLA-4 signaling. J. Immunol. 177:2331-2339.
    • (2006) J. Immunol. , vol.177 , pp. 2331-2339
    • Oida, T.1    Xu, L.2    Weiner, H.L.3    Kitani, A.4    Strober, W.5
  • 12
    • 24644506094 scopus 로고    scopus 로고
    • CTLA-4 upregulation of lymphocyte function-associated antigen 1 adhesion and clustering as an alternate basis for coreceptor function
    • Schneider H, Valk E, da Rocha Dias S, Wei B, Rudd CE. 2005. CTLA-4 upregulation of lymphocyte function-associated antigen 1 adhesion and clustering as an alternate basis for coreceptor function. Proc. Natl. Acad. Sci. U. S. A. 102:12861-12866. http://dx.doi.org/10.1073/pnas.0505802102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12861-12866
    • Schneider, H.1    Valk, E.2    da Rocha Dias, S.3    Wei, B.4    Rudd, C.E.5
  • 14
    • 38549089084 scopus 로고    scopus 로고
    • The reverse stop-signal model for CTLA4 function
    • Rudd CE. 2008. The reverse stop-signal model for CTLA4 function. Nat. Rev. Immunol. 8:153-160. http://dx.doi.org/10.1038/nri2253.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 153-160
    • Rudd, C.E.1
  • 15
    • 33749331268 scopus 로고    scopus 로고
    • Immunology Restless T cells sniffand go
    • Mustelin T. 2006. Immunology Restless T cells sniffand go. Science 313: 1902-1903. http://dx.doi.org/10.1126/science.1133578.
    • (2006) Science , vol.313 , pp. 1902-1903
    • Mustelin, T.1
  • 16
    • 67949118936 scopus 로고    scopus 로고
    • Involvement of Rap-1 activation and early termination of immune synapse in CTLA-4-mediated negative signal
    • Hara S, Nakaseko C, Yamasaki S, Hattori M, Bos JL, Saito Y, Minato N, Saito T. 2009. Involvement of Rap-1 activation and early termination of immune synapse in CTLA-4-mediated negative signal. Hematology 14: 150-158. http://dx.doi.org/10.1179/102453309X402241.
    • (2009) Hematology , vol.14 , pp. 150-158
    • Hara, S.1    Nakaseko, C.2    Yamasaki, S.3    Hattori, M.4    Bos, J.L.5    Saito, Y.6    Minato, N.7    Saito, T.8
  • 19
    • 0028852073 scopus 로고
    • Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail
    • Leung HT, Bradshaw J, Cleaveland JS, Linsley PS. 1995. Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail. J. Biol. Chem. 270:25107-25114. http://dx.doi.org/10.1074/jbc.270.42.25107.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25107-25114
    • Leung, H.T.1    Bradshaw, J.2    Cleaveland, J.S.3    Linsley, P.S.4
  • 20
    • 0033567050 scopus 로고    scopus 로고
    • Cytolytic T lymphocyte-associated antigen-4 and the TcRz/CD3 complex, but not CD28, interact with clathrin adaptor complexes AP-1 and AP-2
    • Schneider H, Martin M, Agarraberes FA, Yin L, Rapoport I, Kirchhausen T, Rudd CE. 1999. Cytolytic T lymphocyte-associated antigen-4 and the TcRz/CD3 complex, but not CD28, interact with clathrin adaptor complexes AP-1 and AP-2. J. Immunol. 163:1868-1879.
    • (1999) J. Immunol. , vol.163 , pp. 1868-1879
    • Schneider, H.1    Martin, M.2    Agarraberes, F.A.3    Yin, L.4    Rapoport, I.5    Kirchhausen, T.6    Rudd, C.E.7
  • 21
    • 0034327809 scopus 로고    scopus 로고
    • Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4 T cells
    • Iida T, Ohno H, Nakaseko C, Sakuma M, Takeda-Ezaki M, Arase H, Kominami E, Fujisawa T, Saito T. 2000. Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4 T cells. J. Immunol. 165:5062-5068.
    • (2000) J. Immunol. , vol.165 , pp. 5062-5068
    • Iida, T.1    Ohno, H.2    Nakaseko, C.3    Sakuma, M.4    Takeda-Ezaki, M.5    Arase, H.6    Kominami, E.7    Fujisawa, T.8    Saito, T.9
  • 22
    • 33846391306 scopus 로고    scopus 로고
    • H. Schneider, T cell receptor-interacting molecule acts as a chaperone to modulate surface expression of the CTLA-4 coreceptor
    • Valk E, Leung R, Kang H, Kaneko K, Rudd CE, Schneider H. 2006. H. Schneider, T cell receptor-interacting molecule acts as a chaperone to modulate surface expression of the CTLA-4 coreceptor. Immunity 25: 807-821. http://dx.doi.org/10.1016/j.immuni.2006.08.024.
    • (2006) Immunity , vol.25 , pp. 807-821
    • Valk, E.1    Leung, R.2    Kang, H.3    Kaneko, K.4    Rudd, C.E.5    Schneider, H.6
  • 23
    • 0030176371 scopus 로고    scopus 로고
    • Intracellular trafficking of CTLA-4 and focal localization toward sites of TCR engagement
    • Linsley PS, Bradshaw J, Greene J, Peach R, Bennet KL, Mittler RS. 1996. Intracellular trafficking of CTLA-4 and focal localization toward sites of TCR engagement. Immunity 4:535-543. http://dx.doi.org/10.1016/S1074-7613(00)80480-X.
    • (1996) Immunity , vol.4 , pp. 535-543
    • Linsley, P.S.1    Bradshaw, J.2    Greene, J.3    Peach, R.4    Bennet, K.L.5    Mittler, R.S.6
  • 24
    • 0033587676 scopus 로고    scopus 로고
    • Defective CTLA-4 cycling pathway in Chediak- Higashi syndrome: a possible mechanism for deregulation of T lymphocyte activation
    • Barrat FJ, Le Deist F, Benkerrou M, Bousso P, Feldmann J, Fischer A, de Saint Basile G. 1999. Defective CTLA-4 cycling pathway in Chediak- Higashi syndrome: a possible mechanism for deregulation of T lymphocyte activation. Proc. Natl. Acad. Sci. U. S. A. 96:8645-8650. http://dx.doi.org/10.1073/pnas.96.15.8645.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8645-8650
    • Barrat, F.J.1    Le Deist, F.2    Benkerrou, M.3    Bousso, P.4    Feldmann, J.5    Fischer, A.6    de Saint Basile, G.7
  • 25
    • 44549085250 scopus 로고    scopus 로고
    • CTLA-4 trafficking and surface expression
    • Valk E, Rudd CE, Schneider H. 2008. CTLA-4 trafficking and surface expression. Trends Immunol. 29:272-279. http://dx.doi.org/10.1016/j.it.2008.02.011.
    • (2008) Trends Immunol. , vol.29 , pp. 272-279
    • Valk, E.1    Rudd, C.E.2    Schneider, H.3
  • 26
    • 0028910221 scopus 로고
    • CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells
    • Schneider H, Prasad KVS, Shoelson SE, Rudd CE. 1995. CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells. J. Exp. Med. 181:351-355. http://dx.doi.org/10.1084/jem.181.1.351.
    • (1995) J. Exp. Med. , vol.181 , pp. 351-355
    • Schneider, H.1    Prasad, K.V.S.2    Shoelson, S.E.3    Rudd, C.E.4
  • 27
    • 0031471027 scopus 로고    scopus 로고
    • Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation
    • Bradshaw JD, Lu P, Leytze G, Rodgers J, Schieven GL, Bennett KL, Linsley PS, Kurtz SE. 1997. Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation. Biochemistry 36:15975-15982. http://dx.doi.org/10.1021/bi971762i.
    • (1997) Biochemistry , vol.36 , pp. 15975-15982
    • Bradshaw, J.D.1    Lu, P.2    Leytze, G.3    Rodgers, J.4    Schieven, G.L.5    Bennett, K.L.6    Linsley, P.S.7    Kurtz, S.E.8
  • 28
    • 0030917081 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2
    • Shiratori T, Miyatake S, Ohno H, Nakaseko C, Isono K, Bonifacino JS, Saito TT. 1997. Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2. Immunity 6:583-589. http://dx.doi.org/10.1016/S1074-7613(00)80346-5.
    • (1997) Immunity , vol.6 , pp. 583-589
    • Shiratori, T.1    Miyatake, S.2    Ohno, H.3    Nakaseko, C.4    Isono, K.5    Bonifacino, J.S.6    Saito, T.T.7
  • 29
    • 0030611358 scopus 로고    scopus 로고
    • Interaction of CTLA-4 with AP-50, a clathrincoated pit adaptor protein
    • Zhang Y, Allison JP. 1997. Interaction of CTLA-4 with AP-50, a clathrincoated pit adaptor protein. Proc. Natl. Acad. Sci. U. S. A. 94:9273-9278. http://dx.doi.org/10.1073/pnas.94.17.9273.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9273-9278
    • Zhang, Y.1    Allison, J.P.2
  • 30
    • 0031181647 scopus 로고    scopus 로고
    • Interaction of CTLA-4 with the clathrin-associated protein AP50 results in ligand-independent endocytosis that limits cell surface expression
    • Chuang E, Alègre ML, Duckett CS, Noel PJ, Vander Heiden MG, Thompson CB. 1997. Interaction of CTLA-4 with the clathrin-associated protein AP50 results in ligand-independent endocytosis that limits cell surface expression. J. Immunol. 159:144-151.
    • (1997) J. Immunol. , vol.159 , pp. 144-151
    • Chuang, E.1    Alègre, M.L.2    Duckett, C.S.3    Noel, P.J.4    Vander Heiden, M.G.5    Thompson, C.B.6
  • 31
    • 65349119978 scopus 로고    scopus 로고
    • CD28 and CTLA-4 coreceptor expression and signal transduction
    • Rudd CE, Taylor A, Schneider H. 2009. CD28 and CTLA-4 coreceptor expression and signal transduction. Immunol. Rev. 229:12-26. http://dx.doi.org/10.1111/j.1600-065X.2009.00770.x.
    • (2009) Immunol. Rev. , vol.229 , pp. 12-26
    • Rudd, C.E.1    Taylor, A.2    Schneider, H.3
  • 32
    • 8444223064 scopus 로고    scopus 로고
    • Transmembrane adapters: structure, biochemistry, and biology
    • Kliche S, Lindquist JA, Schraven B. 2004. Transmembrane adapters: structure, biochemistry, and biology. Semin. Immunol. 16:367-377. http://dx.doi.org/10.1016/j.smim.2004.08.017.
    • (2004) Semin. Immunol. , vol.16 , pp. 367-377
    • Kliche, S.1    Lindquist, J.A.2    Schraven, B.3
  • 33
    • 0025108858 scopus 로고
    • Assembly and function of the T cell antigen receptor: requirement of either the lysine or arginine residues in the transmembrane region of the alpha chain
    • Blumberg RS, Alarcon B, Sancho J, McDermott FV, Lopez P, Breitmeyer J, Terhorst C. 1990. Assembly and function of the T cell antigen receptor: requirement of either the lysine or arginine residues in the transmembrane region of the alpha chain. J. Biol. Chem. 265:14036-14043.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14036-14043
    • Blumberg, R.S.1    Alarcon, B.2    Sancho, J.3    McDermott, F.V.4    Lopez, P.5    Breitmeyer, J.6    Terhorst, C.7
  • 35
    • 23844464509 scopus 로고    scopus 로고
    • The transmembrane adapter protein SIT regulates thymic development and peripheral T-cell functions
    • Simeoni L, Posevitz V, Kölsch U, Meinert I, Bruyns E, Pfeffer K, Reinhold D, Schraven B. 2005. The transmembrane adapter protein SIT regulates thymic development and peripheral T-cell functions. Mol. Cell. Biol. 25:7557-7568. http://dx.doi.org/10.1128/MCB.25.17.7557-7568.2005.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7557-7568
    • Simeoni, L.1    Posevitz, V.2    Kölsch, U.3    Meinert, I.4    Bruyns, E.5    Pfeffer, K.6    Reinhold, D.7    Schraven, B.8
  • 36
    • 17844394466 scopus 로고    scopus 로고
    • Negative regulation of lymphocyte activation by the adaptor protein LAX
    • Zhu M, Granillo O, Wen R, Yang K, Dai X, Wang D, Zhang W. 2005. Negative regulation of lymphocyte activation by the adaptor protein LAX. J. Immunol. 174:5612-5619.
    • (2005) J. Immunol. , vol.174 , pp. 5612-5619
    • Zhu, M.1    Granillo, O.2    Wen, R.3    Yang, K.4    Dai, X.5    Wang, D.6    Zhang, W.7
  • 37
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes CD, Hall A. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235-1244. http://dx.doi.org/10.1083/jcb.144.6.1235.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 8444243363 scopus 로고    scopus 로고
    • Targeting Rab GTPases to distinct membrane compartments
    • Pfeffer S, Aivazian D. 2004. Targeting Rab GTPases to distinct membrane compartments. Nat. Rev. Mol. Cell. Biol. 5:886-896. http://dx.doi.org/10.1038/nrm1500.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 886-896
    • Pfeffer, S.1    Aivazian, D.2
  • 39
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. 2009. Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell. Biol. 10:513-525. http://dx.doi.org/10.1038/nrm2728.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 41
    • 0029117606 scopus 로고
    • Expression of Rab GTPases using recombinant vaccinia viruses
    • Stenmark H, Bucci C, Zerial M. 1995. Expression of Rab GTPases using recombinant vaccinia viruses. Methods Enzymol. 257:155-164. http://dx.doi.org/10.1016/S0076-6879(95)57021-7.
    • (1995) Methods Enzymol. , vol.257 , pp. 155-164
    • Stenmark, H.1    Bucci, C.2    Zerial, M.3
  • 42
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi H, Lippe R, McBride HM, Rubino M, Woodman P, Stenmark H, Rybin V, Wilm M, Ashman K, Mann M, Zerial M. 1997. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 90:1149-1159. http://dx.doi.org/10.1016/S0092-8674(00)80380-3.
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1    Lippe, R.2    McBride, H.M.3    Rubino, M.4    Woodman, P.5    Stenmark, H.6    Rybin, V.7    Wilm, M.8    Ashman, K.9    Mann, M.10    Zerial, M.11
  • 44
    • 33845903831 scopus 로고    scopus 로고
    • Characterization of the Rab8-specific membrane traffic route linked to protrusion formation
    • Hattula K, Furuhjelm J, Tikkanen J, Tanhuanpaa K, Laakkonen P, Peränen J. 2006. Characterization of the Rab8-specific membrane traffic route linked to protrusion formation. J. Cell Sci. 119:4866-4877. http://dx.doi.org/10.1242/jcs.03275.
    • (2006) J. Cell Sci. , vol.119 , pp. 4866-4877
    • Hattula, K.1    Furuhjelm, J.2    Tikkanen, J.3    Tanhuanpaa, K.4    Laakkonen, P.5    Peränen, J.6
  • 45
    • 0242298589 scopus 로고    scopus 로고
    • The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells
    • Ang AL, Folsch H, Koivisto UM, Pypaert M, Mellman I. 2003. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. J. Cell Biol. 163:339-350. http://dx.doi.org/10.1083/jcb.200307046.
    • (2003) J. Cell Biol. , vol.163 , pp. 339-350
    • Ang, A.L.1    Folsch, H.2    Koivisto, U.M.3    Pypaert, M.4    Mellman, I.5
  • 46
    • 0034986111 scopus 로고    scopus 로고
    • The Rab GTPase family
    • REVIEWS3007
    • Stenmark H, Olkkonen VM. 2001. The Rab GTPase family. Genome Biol. 2:REVIEWS3007. http://dx.doi.org/10.1186/gb-2001-2-5-reviews3007.
    • (2001) Genome Biol. , vol.2
    • Stenmark, H.1    Olkkonen, V.M.2
  • 47
    • 0036500526 scopus 로고    scopus 로고
    • Human myosin-Vc is a novel class V myosin expressed in epithelial cells
    • Rodriguez OC, Cheney RE. 2002. Human myosin-Vc is a novel class V myosin expressed in epithelial cells. J. Cell Sci. 115:991-1004.
    • (2002) J. Cell Sci. , vol.115 , pp. 991-1004
    • Rodriguez, O.C.1    Cheney, R.E.2
  • 48
    • 0029819793 scopus 로고    scopus 로고
    • Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts
    • Peränen J, Auvinen P, Virta H, Wepf R, Simons K. 1996. Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts. J. Cell Biol. 135:153-167. http://dx.doi.org/10.1083/jcb.135.1.153.
    • (1996) J. Cell Biol. , vol.135 , pp. 153-167
    • Peränen, J.1    Auvinen, P.2    Virta, H.3    Wepf, R.4    Simons, K.5
  • 49
    • 0035139796 scopus 로고    scopus 로고
    • Expression, purification, and properties of Rab8 function in actin cortical skeleton organization and polarized transport
    • Peränen J, Furuhjelm J. 2001. Expression, purification, and properties of Rab8 function in actin cortical skeleton organization and polarized transport. Methods Enzymol. 329:188-196. http://dx.doi.org/10.1016/S0076-6879(01)29079-X.
    • (2001) Methods Enzymol. , vol.329 , pp. 188-196
    • Peränen, J.1    Furuhjelm, J.2
  • 50
    • 77249158951 scopus 로고    scopus 로고
    • Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucomaassociated mutant
    • Nagabhushana A, Chalasani ML, Jain N, Radha V, Rangaraj N, Balasubramanian D, Swarup G. 2010. Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucomaassociated mutant. BMC Cell Biol. 11:4. http://dx.doi.org/10.1186/1471-2121-11-4.
    • (2010) BMC Cell Biol. , vol.11 , pp. 4
    • Nagabhushana, A.1    Chalasani, M.L.2    Jain, N.3    Radha, V.4    Rangaraj, N.5    Balasubramanian, D.6    Swarup, G.7
  • 51
    • 34547810829 scopus 로고    scopus 로고
    • Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3
    • Roland JT, Kenworthy AK, Peränen J, Caplan S, Goldenring JR. 2007. Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. Mol. Biol. Cell 18:2828-2837. http://dx.doi.org/10.1091/mbc. E07-02-0169.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2828-2837
    • Roland, J.T.1    Kenworthy, A.K.2    Peränen, J.3    Caplan, S.4    Goldenring, J.R.5
  • 53
    • 0034649661 scopus 로고    scopus 로고
    • FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis
    • Hattula K, Peränen J. 2000. FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr. Biol. 10:1603-1606. http://dx.doi.org/10.1016/S0960-9822(00)00864-2.
    • (2000) Curr. Biol. , vol.10 , pp. 1603-1606
    • Hattula, K.1    Peränen, J.2
  • 54
    • 77953742527 scopus 로고    scopus 로고
    • Rab8 interacts with distinct motifs in α2B- and β2-adrenergic receptors and differentially modulates their transport
    • Dong C, Yang L, Zhang X, Gu H, Lam ML, Claycomb WCWC, Xia H, Wu G. 2010. Rab8 interacts with distinct motifs in α2B- and β2-adrenergic receptors and differentially modulates their transport. J. Biol. Chem. 285:20369-20380. http://dx.doi.org/10.1074/jbc. M109.081521.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20369-20380
    • Dong, C.1    Yang, L.2    Zhang, X.3    Gu, H.4    Lam, M.L.5    Claycomb, W.C.W.C.6    Xia, H.7    Wu, G.8
  • 55
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M, Mcbride H. 2001. Rab proteins as membrane organizers. Nat. Rev. Mol. Cell. Biol. 2:107-117. http://dx.doi.org/10.1038/35052055.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 107-117
    • Zerial, M.1    Mcbride, H.2
  • 56
    • 0036172220 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte antigen-4 accumulation in the immunological synapse is regulated by TCR signal strength
    • Egen JG, Allison JP. 2002. Cytotoxic T lymphocyte antigen-4 accumulation in the immunological synapse is regulated by TCR signal strength. Immunity 16:23-35. http://dx.doi.org/10.1016/S1074-7613(01)00259-X.
    • (2002) Immunity , vol.16 , pp. 23-35
    • Egen, J.G.1    Allison, J.P.2
  • 60
    • 84862726617 scopus 로고    scopus 로고
    • Coordination between RAB GTPase and phosphoinositide regulation and functions
    • Jean S, Kiger AA. 2012. Coordination between RAB GTPase and phosphoinositide regulation and functions. Nat. Rev. Mol. Cell. Biol. 13:463-470. http://dx.doi.org/10.1038/nrm3379.
    • (2012) Nat. Rev. Mol. Cell. Biol. , vol.13 , pp. 463-470
    • Jean, S.1    Kiger, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.