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Volumn 303, Issue 8, 2012, Pages

VIP17/MAL expression modulates epithelial cyst formation and ciliogenesis

Author keywords

Cystogenesis; Epithelial trafficking; Polycystic kidney disease

Indexed keywords

CELL PROTEIN; CONTACTIN 1; MYELIN AND LYMPHOCYTE PROTEIN; UNCLASSIFIED DRUG; VESICULAR INTEGRAL PROTEIN OF 17 KDA;

EID: 84867624034     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00338.2011     Document Type: Article
Times cited : (8)

References (62)
  • 1
    • 0004183876 scopus 로고
    • cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation
    • Alonso MA, Weissman SM. cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation. Proc Natl Acad Sci USA 84: 1997-2001, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1997-2001
    • Alonso, M.A.1    Weissman, S.M.2
  • 2
    • 0023918616 scopus 로고
    • Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells
    • Anderson JM, Stevenson BR, Jesaitis LA, Goodenough DA, Mooseker MS. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. J Cell Biol 106: 1141-1149, 1988.
    • (1988) J Cell Biol , vol.106 , pp. 1141-1149
    • Anderson, J.M.1    Stevenson, B.R.2    Jesaitis, L.A.3    Goodenough, D.A.4    Mooseker, M.S.5
  • 3
    • 0345377061 scopus 로고
    • Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line
    • Balcarova-Stander J, Pfeiffer SE, Fuller SD, Simons K. Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line. EMBO J 3: 2687-2694, 1984.
    • (1984) EMBO J , vol.3 , pp. 2687-2694
    • Balcarova-Stander, J.1    Pfeiffer, S.E.2    Fuller, S.D.3    Simons, K.4
  • 4
    • 34948834648 scopus 로고    scopus 로고
    • Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell cell mechanical adhesion
    • Boca M, D'Amato L, Distefano G, Polishchuk RS, Germino GG, Boletta A. Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell cell mechanical adhesion. Mol Biol Cell 18: 4050-4061, 2007.
    • (2007) Mol Biol Cell , vol.18 , pp. 4050-4061
    • Boca, M.1    D'amato, L.2    Distefano, G.3    Polishchuk, R.S.4    Germino, G.G.5    Boletta, A.6
  • 7
    • 34247558062 scopus 로고    scopus 로고
    • The graded response to Sonic Hedgehog depends on cilia architecture
    • Caspary T, Larkins CE, Anderson KV. The graded response to Sonic Hedgehog depends on cilia architecture. Dev Cell 12: 767-778, 2007.
    • (2007) Dev Cell , vol.12 , pp. 767-778
    • Caspary, T.1    Larkins, C.E.2    Anderson, K.V.3
  • 8
    • 78349286779 scopus 로고    scopus 로고
    • The cell biology of polycystic kidney disease
    • Chapin HC, Caplan MJ. The cell biology of polycystic kidney disease. J Cell Biol 191: 701-710, 2010.
    • (2010) J Cell Biol , vol.191 , pp. 701-710
    • Chapin, H.C.1    Caplan, M.J.2
  • 9
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong KH, Zacchetti D, Schneeberger EE, Simons K. VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc Natl Acad Sci USA 96: 6241-6248, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 10
    • 23944450197 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) during assembly and disassembly of Chlamydomonas flagella
    • Dentler W. Intraflagellar transport (IFT) during assembly and disassembly of Chlamydomonas flagella. J Cell Biol 170: 649-659, 2005.
    • (2005) J Cell Biol , vol.170 , pp. 649-659
    • Dentler, W.1
  • 11
    • 34547574593 scopus 로고    scopus 로고
    • A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin beta interactions
    • Fan S, Fogg V, Wang Q, Chen XW, Liu CJ, Margolis B. A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin beta interactions. J Cell Biol 178: 387-398, 2007.
    • (2007) J Cell Biol , vol.178 , pp. 387-398
    • Fan, S.1    Fogg, V.2    Wang, Q.3    Chen, X.W.4    Liu, C.J.5    Margolis, B.6
  • 13
    • 0033061321 scopus 로고    scopus 로고
    • Transmembrane proteins in the tight junction barrier
    • Fanning AS, Mitic LL, Anderson JM. Transmembrane proteins in the tight junction barrier. J Am Soc Nephrol 10: 1337-1345, 1999.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1337-1345
    • Fanning, A.S.1    Mitic, L.L.2    Anderson, J.M.3
  • 15
    • 75749089291 scopus 로고    scopus 로고
    • The cytoplasmic tail of fibrocystin contains a ciliary targeting sequence
    • Follit JA, Li L, Vucica Y, Pazour GJ. The cytoplasmic tail of fibrocystin contains a ciliary targeting sequence. J Cell Biol 188: 21-28, 2010.
    • (2010) J Cell Biol , vol.188 , pp. 21-28
    • Follit, J.A.1    Li, L.2    Vucica, Y.3    Pazour, G.J.4
  • 16
    • 33748327050 scopus 로고    scopus 로고
    • The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly
    • Follit JA, Tuft RA, Fogarty KE, Pazour GJ. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly. Mol Biol Cell 17: 3781-3792, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 3781-3792
    • Follit, J.A.1    Tuft, R.A.2    Fogarty, K.E.3    Pazour, G.J.4
  • 17
    • 79955494220 scopus 로고    scopus 로고
    • A hierarchy of signals regulates entry of membrane proteins into the ciliary membrane domain in epithelial cells
    • Francis SS, Sfakianos J, Lo B, Mellman I. A hierarchy of signals regulates entry of membrane proteins into the ciliary membrane domain in epithelial cells. J Cell Biol 193: 219-233, 2011.
    • (2011) J Cell Biol , vol.193 , pp. 219-233
    • Francis, S.S.1    Sfakianos, J.2    Lo, B.3    Mellman, I.4
  • 18
    • 0033792248 scopus 로고    scopus 로고
    • Progressive segregation of unmyelinated axons in peripheral nerves, myelin alterations in the CNS, and cyst formation in the kidneys of myelin and lymphocyte protein-overexpressing mice
    • Frank M, Atanasoski S, Sancho S, Magyar JP, Rulicke T, Schwab ME, Suter U. Progressive segregation of unmyelinated axons in peripheral nerves, myelin alterations in the CNS, and cyst formation in the kidneys of myelin and lymphocyte protein-overexpressing mice. J Neu-rochem 75: 1927-1939, 2000.
    • (2000) J Neu-rochem , vol.75 , pp. 1927-1939
    • Frank, M.1    Atanasoski, S.2    Sancho, S.3    Magyar, J.P.4    Rulicke, T.5    Schwab, M.E.6    Suter, U.7
  • 19
    • 0032124916 scopus 로고    scopus 로고
    • rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach
    • Frank M, van der Haar ME, Schaeren-Wiemers N, Schwab ME. rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach. J Neurosci 18: 4901-4913, 1998.
    • (1998) J Neurosci , vol.18 , pp. 4901-4913
    • Frank, M.1    van der Haar, M.E.2    Schaeren-Wiemers, N.3    Schwab, M.E.4
  • 20
    • 33645510592 scopus 로고    scopus 로고
    • Identification of glycosylated marker proteins of epithelial polarity in MDCK cells by homology driven proteomics
    • Fullekrug J, Shevchenko A, Simons K. Identification of glycosylated marker proteins of epithelial polarity in MDCK cells by homology driven proteomics. BMC Biochem 7: 8, 2006.
    • (2006) BMC Biochem , vol.7 , pp. 8
    • Fullekrug, J.1    Shevchenko, A.2    Simons, K.3
  • 21
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET, Nelson WJ. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329: 436-439, 2010.
    • (2010) Science , vol.329 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3    Scott, M.P.4    Nachury, M.V.5    Spiliotis, E.T.6    Nelson, W.J.7
  • 22
    • 0032744937 scopus 로고    scopus 로고
    • Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins
    • Huan Y, van Adelsberg J. Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins. J Clin Invest 104: 1459-1468, 1999.
    • (1999) J Clin Invest , vol.104 , pp. 1459-1468
    • Huan, Y.1    van Adelsberg, J.2
  • 24
    • 14344262312 scopus 로고    scopus 로고
    • Identification of vasopressin-induced genes in AQP2-transfected MDCK cells by suppression subtractive hybridization
    • Kang DY, Park JI, Cho WS, Jeong MH, Cho GW, Park HT, Bae HR. Identification of vasopressin-induced genes in AQP2-transfected MDCK cells by suppression subtractive hybridization. Biochem Biophys Res Commun 324: 1234-1241, 2004.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1234-1241
    • Kang, D.Y.1    Park, J.I.2    Cho, W.S.3    Jeong, M.H.4    Cho, G.W.5    Park, H.T.6    Bae, H.R.7
  • 25
    • 0028875824 scopus 로고
    • Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes
    • Kim T, Fiedler K, Madison DL, Krueger WH, Pfeiffer SE. Cloning and characterization of MVP17: a developmentally regulated myelin protein in oligodendrocytes. J Neurosci Res 42: 413-422, 1995.
    • (1995) J Neurosci Res , vol.42 , pp. 413-422
    • Kim, T.1    Fiedler, K.2    Madison, D.L.3    Krueger, W.H.4    Pfeiffer, S.E.5
  • 26
    • 0036192093 scopus 로고    scopus 로고
    • Retention of membrane-localized beta-catenin in cells lacking functional polycystin-1 and tuberin
    • Kugoh H, Kleymenova E, Walker CL. Retention of membrane-localized beta-catenin in cells lacking functional polycystin-1 and tuberin. Mol Carcinog 33: 131-136, 2002.
    • (2002) Mol Carcinog , vol.33 , pp. 131-136
    • Kugoh, H.1    Kleymenova, E.2    Walker, C.L.3
  • 28
    • 79955368025 scopus 로고    scopus 로고
    • Rabs and other small GTPases in ciliary transport
    • Lim YS, Chua CE, Tang BL. Rabs and other small GTPases in ciliary transport. Biol Cell 103: 209-221, 2011.
    • (2011) Biol Cell , vol.103 , pp. 209-221
    • Lim, Y.S.1    Chua, C.E.2    Tang, B.L.3
  • 29
    • 0037884961 scopus 로고    scopus 로고
    • Kidney-specific inactivation of the KIF3A subunit of kine-sin-II inhibits renal ciliogenesis and produces polycystic kidney disease
    • Lin F, Hiesberger T, Cordes K, Sinclair AM, Goldstein LS, Somlo S, Igarashi P. Kidney-specific inactivation of the KIF3A subunit of kine-sin-II inhibits renal ciliogenesis and produces polycystic kidney disease. Proc Natl Acad Sci USA 100: 5286-5291, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5286-5291
    • Lin, F.1    Hiesberger, T.2    Cordes, K.3    Sinclair, A.M.4    Goldstein, L.S.5    Somlo, S.6    Igarashi, P.7
  • 31
    • 0013537241 scopus 로고
    • Renal epithelial cyst formation and enlargement in vitro: Dependence on cAMP
    • Mangoo-Karim R, Uchic M, Lechene C, Grantham JJ. Renal epithelial cyst formation and enlargement in vitro: dependence on cAMP. Proc Natl Acad Sci USA 86: 6007-6011, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6007-6011
    • Mangoo-Karim, R.1    Uchic, M.2    Lechene, C.3    Grantham, J.J.4
  • 32
    • 0031763488 scopus 로고    scopus 로고
    • Expression of the MAL gene in the thyroid: The MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles
    • Martin-Belmonte F, Kremer L, Albar JP, Marazuela M, Alonso MA. Expression of the MAL gene in the thyroid: the MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles. Endocrinology 139: 2077-2084, 1998.
    • (1998) Endocrinology , vol.139 , pp. 2077-2084
    • Martin-Belmonte, F.1    Kremer, L.2    Albar, J.P.3    Marazuela, M.4    Alonso, M.A.5
  • 33
    • 13844289424 scopus 로고    scopus 로고
    • Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells
    • Meder D, Shevchenko A, Simons K, Fullekrug J. Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells. J Cell Biol 168: 303-313, 2005.
    • (2005) J Cell Biol , vol.168 , pp. 303-313
    • Meder, D.1    Shevchenko, A.2    Simons, K.3    Fullekrug, J.4
  • 34
    • 75549090700 scopus 로고    scopus 로고
    • Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium
    • Milenkovic L, Scott MP, Rohatgi R. Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium. J Cell Biol 187: 365-374, 2009.
    • (2009) J Cell Biol , vol.187 , pp. 365-374
    • Milenkovic, L.1    Scott, M.P.2    Rohatgi, R.3
  • 35
    • 0031770769 scopus 로고    scopus 로고
    • MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinases
    • Millan J, Alonso MA. MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinases. Eur J Immunol 28: 3675-3684, 1998.
    • (1998) Eur J Immunol , vol.28 , pp. 3675-3684
    • Millan, J.1    Alonso, M.A.2
  • 36
    • 0031589155 scopus 로고    scopus 로고
    • Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells
    • Millan J, Puertollano R, Fan L, Alonso MA. Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells. Biochem Biophys Res Commun 233: 707-712, 1997.
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 707-712
    • Millan, J.1    Puertollano, R.2    Fan, L.3    Alonso, M.A.4
  • 38
    • 0037334326 scopus 로고    scopus 로고
    • Polycystic kidney disease-the ciliary connection
    • Ong AC, Wheatley DN. Polycystic kidney disease-the ciliary connection. Lancet 361: 774-776, 2003.
    • (2003) Lancet , vol.361 , pp. 774-776
    • Ong, A.C.1    Wheatley, D.N.2
  • 39
    • 0036901166 scopus 로고    scopus 로고
    • Intraflagellar transport and cilia-dependent diseases
    • Pazour GJ, Rosenbaum JL. Intraflagellar transport and cilia-dependent diseases. Trends Cell Biol 12: 551-555, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 551-555
    • Pazour, G.J.1    Rosenbaum, J.L.2
  • 40
    • 34548177786 scopus 로고    scopus 로고
    • Centrioles want to move out and make cilia
    • Pearson CG, Culver BP, Winey M. Centrioles want to move out and make cilia. Dev Cell 13: 319-321, 2007.
    • (2007) Dev Cell , vol.13 , pp. 319-321
    • Pearson, C.G.1    Culver, B.P.2    Winey, M.3
  • 41
    • 0026669417 scopus 로고
    • Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture
    • Pietrini G, Matteoli M, Banker G, Caplan MJ. Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture. Proc Natl Acad Sci USA 89: 8414-8418, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8414-8418
    • Pietrini, G.1    Matteoli, M.2    Banker, G.3    Caplan, M.J.4
  • 42
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano R, Martin-Belmonte F, Millan J, de Marco MC, Albar JP, Kremer L, Alonso MA. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J Cell Biol 145: 141-151, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    de Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 43
    • 13544252818 scopus 로고    scopus 로고
    • Cystic renal neoplasia following conditional inactivation of apc in mouse renal tubular epithelium
    • Qian CN, Knol J, Igarashi P, Lin F, Zylstra U, Teh BT, Williams BO. Cystic renal neoplasia following conditional inactivation of apc in mouse renal tubular epithelium. J Biol Chem 280: 3938-3945, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 3938-3945
    • Qian, C.N.1    Knol, J.2    Igarashi, P.3    Lin, F.4    Zylstra, U.5    Teh, B.T.6    Williams, B.O.7
  • 44
    • 33845498084 scopus 로고    scopus 로고
    • Vesicle transport, cilium formation, and membrane specialization: The origins of a sensory organelle
    • Reiter JF, Mostov K. Vesicle transport, cilium formation, and membrane specialization: the origins of a sensory organelle. Proc Natl Acad Sci USA 103: 18383-18384, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18383-18384
    • Reiter, J.F.1    Mostov, K.2
  • 47
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons K, Wandinger-Ness A. Polarized sorting in epithelia. Cell 62: 207-210, 1990.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 49
    • 33746891890 scopus 로고    scopus 로고
    • The primary cilium as the cell's antenna: Signaling at a sensory organelle
    • Singla V, Reiter JF. The primary cilium as the cell's antenna: signaling at a sensory organelle. Science 313: 629-633, 2006.
    • (2006) Science , vol.313 , pp. 629-633
    • Singla, V.1    Reiter, J.F.2
  • 51
    • 80051689070 scopus 로고    scopus 로고
    • Polycystic kidney disease: Pathogenesis and potential therapies
    • Takiar V, Caplan MJ. Polycystic kidney disease: Pathogenesis and potential therapies. Biochim Biophys Acta 2010.
    • (2010) Biochim Biophys Acta
    • Takiar, V.1    Caplan, M.J.2
  • 53
    • 44449156338 scopus 로고    scopus 로고
    • Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis
    • Torkko JM, Manninen A, Schuck S, Simons K. Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis. J Cell Sci 121: 1193-1203, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 1193-1203
    • Torkko, J.M.1    Manninen, A.2    Schuck, S.3    Simons, K.4
  • 54
    • 0031952629 scopus 로고    scopus 로고
    • Protein targeting: The molecular basis of vectorial transport in the kidney
    • van Adelsberg J. Protein targeting: the molecular basis of vectorial transport in the kidney. Semin Nephrol 18: 152-166, 1998.
    • (1998) Semin Nephrol , vol.18 , pp. 152-166
    • van Adelsberg, J.1
  • 55
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • Vieira OV, Gaus K, Verkade P, Fullekrug J, Vaz WL, Simons K. FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells. Proc Natl Acad Sci USA 103: 18556-18561, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18556-18561
    • Vieira, O.V.1    Gaus, K.2    Verkade, P.3    Fullekrug, J.4    Vaz, W.L.5    Simons, K.6
  • 56
    • 1542378854 scopus 로고    scopus 로고
    • The autosomal recessive polycystic kidney disease protein is localized to primary cilia, with concentration in the basal body area
    • Wang S, Luo Y, Wilson PD, Witman GB, Zhou J. The autosomal recessive polycystic kidney disease protein is localized to primary cilia, with concentration in the basal body area. J Am Soc Nephrol 15: 592-602, 2004.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 592-602
    • Wang, S.1    Luo, Y.2    Wilson, P.D.3    Witman, G.B.4    Zhou, J.5
  • 57
    • 0042667181 scopus 로고    scopus 로고
    • From cilia to cyst
    • Watnick T, Germino G. From cilia to cyst. Nat Genet 34: 355-356, 2003.
    • (2003) Nat Genet , vol.34 , pp. 355-356
    • Watnick, T.1    Germino, G.2
  • 58
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • Yeaman C, Grindstaff KK, Nelson WJ. New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol Rev 79: 73-98, 1999.
    • (1999) Physiol Rev , vol.79 , pp. 73-98
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 62
    • 79959358443 scopus 로고    scopus 로고
    • The small GTPase Cdc42 is necessary for primary ciliogenesis in renal tubular epithelial cells
    • Zuo X, Fogelgren B, Lipschutz JH. The small GTPase Cdc42 is necessary for primary ciliogenesis in renal tubular epithelial cells. J Biol Chem 286: 22469-22477, 2011
    • (2011) J Biol Chem , vol.286 , pp. 22469-22477
    • Zuo, X.1    Fogelgren, B.2    Lipschutz, J.H.3


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