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Volumn 20, Issue 2, 2008, Pages 208-213

Regulation of membrane trafficking in polarized epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; CARRIER PROTEIN; GALECTIN 4; GLYCOLIPID; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; PROTEIN FAPP2; UNCLASSIFIED DRUG;

EID: 41549120213     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2008.01.003     Document Type: Review
Times cited : (60)

References (62)
  • 2
    • 16844374089 scopus 로고    scopus 로고
    • The building blocks for basolateral vesicles in polarized epithelial cells
    • Fölsch H. The building blocks for basolateral vesicles in polarized epithelial cells. Trends Cell Biol 15 (2005) 222-228
    • (2005) Trends Cell Biol , vol.15 , pp. 222-228
    • Fölsch, H.1
  • 3
    • 0036156444 scopus 로고    scopus 로고
    • Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes
    • Sheff D.R., Kroschewski R., and Mellman I. Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes. Mol Biol Cell 13 (2002) 262-275
    • (2002) Mol Biol Cell , vol.13 , pp. 262-275
    • Sheff, D.R.1    Kroschewski, R.2    Mellman, I.3
  • 4
    • 34347369621 scopus 로고    scopus 로고
    • Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains
    • This study suggests, that apical recycling endosomes may be a subdomain of common recycling endosomes.
    • Thompson A., Nessler R., Wisco D., Anderson E., Winckler B., and Sheff D. Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains. Mol Biol Cell 18 (2007) 2687-2697. This study suggests, that apical recycling endosomes may be a subdomain of common recycling endosomes.
    • (2007) Mol Biol Cell , vol.18 , pp. 2687-2697
    • Thompson, A.1    Nessler, R.2    Wisco, D.3    Anderson, E.4    Winckler, B.5    Sheff, D.6
  • 5
    • 0037383848 scopus 로고    scopus 로고
    • Polarized epithelial membrane traffic: conservation and plasticity
    • Mostov K., Su T., and ter Beest M. Polarized epithelial membrane traffic: conservation and plasticity. Nat Cell Biol 5 (2003) 287-293
    • (2003) Nat Cell Biol , vol.5 , pp. 287-293
    • Mostov, K.1    Su, T.2    ter Beest, M.3
  • 6
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S., Sarnataro D., Pillich R., Tivodar S., Nitsch L., and Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J Cell Biol 167 (2004) 699-709
    • (2004) J Cell Biol , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 7
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 8
    • 21044458257 scopus 로고    scopus 로고
    • Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells
    • Describes for the first time a sorting lectin, galectin-4, involved in clustering sphingolipids for apical delivery.
    • Delacour D., Gouyer V., Zanetta J.P., Drobecq H., Leteurtre E., Grard G., Moreau-Hannedouche O., Maes E., Pons A., Andre S., et al. Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells. J Cell Biol 169 (2005) 491-501. Describes for the first time a sorting lectin, galectin-4, involved in clustering sphingolipids for apical delivery.
    • (2005) J Cell Biol , vol.169 , pp. 491-501
    • Delacour, D.1    Gouyer, V.2    Zanetta, J.P.3    Drobecq, H.4    Leteurtre, E.5    Grard, G.6    Moreau-Hannedouche, O.7    Maes, E.8    Pons, A.9    Andre, S.10
  • 10
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Using RNAi-mediated knock down, the authors show that FAPP2 is necessary for efficient apical transport.
    • Vieira O.V., Verkade P., Manninen A., and Simons K. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J Cell Biol 170 (2005) 521-526. Using RNAi-mediated knock down, the authors show that FAPP2 is necessary for efficient apical transport.
    • (2005) J Cell Biol , vol.170 , pp. 521-526
    • Vieira, O.V.1    Verkade, P.2    Manninen, A.3    Simons, K.4
  • 12
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • In this interesting paper, the authors demonstrate a role for FAPP2 in transfer of glucosylceramide to the TGN, where it serves as precursor for sphingolipids.
    • D'Angelo G., Polishchuk E., Di Tullio G., Santoro M., Di Campli A., Godi A., West G., Bielawski J., Chuang C.C., van der Spoel A.C., et al. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449 (2007) 62-67. In this interesting paper, the authors demonstrate a role for FAPP2 in transfer of glucosylceramide to the TGN, where it serves as precursor for sphingolipids.
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1    Polishchuk, E.2    Di Tullio, G.3    Santoro, M.4    Di Campli, A.5    Godi, A.6    West, G.7    Bielawski, J.8    Chuang, C.C.9    van der Spoel, A.C.10
  • 13
    • 0035494465 scopus 로고    scopus 로고
    • KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes
    • Noda Y., Okada Y., Saito N., Setou M., Xu Y., Zhang Z., and Hirokawa N. KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes. J Cell Biol 155 (2001) 77-88
    • (2001) J Cell Biol , vol.155 , pp. 77-88
    • Noda, Y.1    Okada, Y.2    Saito, N.3    Setou, M.4    Xu, Y.5    Zhang, Z.6    Hirokawa, N.7
  • 14
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells
    • Lafont F., Burkhardt J.K., and Simons K. Involvement of microtubule motors in basolateral and apical transport in kidney cells. Nature 372 (1994) 801-803
    • (1994) Nature , vol.372 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 16
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont F., Lecat S., Verkade P., and Simons K. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J Cell Biol 142 (1998) 1413-1427
    • (1998) J Cell Biol , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 17
    • 28644444772 scopus 로고    scopus 로고
    • The role of syntaxins in the specificity of vesicle targeting in polarized epithelial cells
    • ter Beest M.B., Chapin S.J., Avrahami D., and Mostov K.E. The role of syntaxins in the specificity of vesicle targeting in polarized epithelial cells. Mol Biol Cell 16 (2005) 5784-5792
    • (2005) Mol Biol Cell , vol.16 , pp. 5784-5792
    • ter Beest, M.B.1    Chapin, S.J.2    Avrahami, D.3    Mostov, K.E.4
  • 19
    • 35548970161 scopus 로고    scopus 로고
    • Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelial cells
    • This interesting study demonstrates the involvement of different v-SNAREs in direct and indirect (transcytotic) apical delivery.
    • Pocard T., Le Bivic A., Galli T., and Zurzolo C. Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelial cells. J Cell Sci 120 (2007) 3309-3320. This interesting study demonstrates the involvement of different v-SNAREs in direct and indirect (transcytotic) apical delivery.
    • (2007) J Cell Sci , vol.120 , pp. 3309-3320
    • Pocard, T.1    Le Bivic, A.2    Galli, T.3    Zurzolo, C.4
  • 20
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T., Zahraoui A., Vaidyanathan V.V., Raposo G., Tian J.M., Karin M., Niemann H., and Louvard D. A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9 (1998) 1437-1448
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 21
    • 32944469481 scopus 로고    scopus 로고
    • Requirement for galectin-3 in apical protein sorting
    • Here a requirement for galectin-3 in sorting of non-raft cargos to the apical membrane is demonstrated.
    • Delacour D., Cramm-Behrens C.I., Drobecq H., Le Bivic A., Naim H.Y., and Jacob R. Requirement for galectin-3 in apical protein sorting. Curr Biol 16 (2006) 408-414. Here a requirement for galectin-3 in sorting of non-raft cargos to the apical membrane is demonstrated.
    • (2006) Curr Biol , vol.16 , pp. 408-414
    • Delacour, D.1    Cramm-Behrens, C.I.2    Drobecq, H.3    Le Bivic, A.4    Naim, H.Y.5    Jacob, R.6
  • 22
    • 33947214012 scopus 로고    scopus 로고
    • Apical sorting by galectin-3-dependent glycoprotein clustering
    • This study demonstrates that galectin-3 facilitates non-raft associated apical sorting by clustering glycoprotein into heterooligomers.
    • Delacour D., Greb C., Koch A., Salomonsson E., Leffler H., Le Bivic A., and Jacob R. Apical sorting by galectin-3-dependent glycoprotein clustering. Traffic 8 (2007) 379-388. This study demonstrates that galectin-3 facilitates non-raft associated apical sorting by clustering glycoprotein into heterooligomers.
    • (2007) Traffic , vol.8 , pp. 379-388
    • Delacour, D.1    Greb, C.2    Koch, A.3    Salomonsson, E.4    Leffler, H.5    Le Bivic, A.6    Jacob, R.7
  • 23
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • Vieira O.V., Gaus K., Verkade P., Fullekrug J., Vaz W.L., and Simons K. FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells. Proc Natl Acad Sci U S A 103 (2006) 18556-18561
    • (2006) Proc Natl Acad Sci U S A , 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
  • 24
    • 34848926858 scopus 로고    scopus 로고
    • Polarization-dependent selective transport to the apical membrane by KIF5B in MDCK cells
    • This elegant study demonstrates for the first time the involvement of a plus-end directed microtubule motor in apical transport.
    • Jaulin F., Xue X., Rodriguez-Boulan E., and Kreitzer G. Polarization-dependent selective transport to the apical membrane by KIF5B in MDCK cells. Dev Cell 13 (2007) 511-522. This elegant study demonstrates for the first time the involvement of a plus-end directed microtubule motor in apical transport.
    • (2007) Dev Cell , vol.13 , pp. 511-522
    • Jaulin, F.1    Xue, X.2    Rodriguez-Boulan, E.3    Kreitzer, G.4
  • 25
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes
    • Janvier K., Kato Y., Boehm M., Rose J.R., Martina J.A., Kim B.Y., Venkatesan S., and Bonifacino J.S. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes. J Cell Biol 163 (2003) 1281-1290
    • (2003) J Cell Biol , vol.163 , 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
  • 27
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Fölsch H., Ohno H., Bonifacino J.S., and Mellman I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99 (1999) 189-198
    • (1999) Cell , vol.99 , pp. 189-198
    • Fölsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 28
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Fölsch H., Pypaert M., Maday S., Pelletier L., and Mellman I. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 163 (2003) 351-362
    • (2003) J Cell Biol , vol.163 , pp. 351-362
    • Fölsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 29
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane
    • Gan Y., McGraw T.E., and Rodriguez-Boulan E. The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat Cell Biol 4 (2002) 605-609
    • (2002) Nat Cell Biol , vol.4 , pp. 605-609
    • Gan, Y.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 30
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang A.L., Taguchi T., Francis S., Fölsch H., Murrells L.J., Pypaert M., Warren G., and Mellman I. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J Cell Biol 167 (2004) 531-543
    • (2004) J Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Fölsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 32
    • 34248216451 scopus 로고    scopus 로고
    • v-SNARE cellubrevin is required for basolateral sorting of AP-1B-dependent cargo in polarized epithelial cells
    • In this study the authors classify basolateral cargos into those using a 'direct' or 'indirect' pathway.
    • Fields I.C., Shteyn E., Pypaert M., Proux-Gillardeaux V., Kang R.S., Galli T., and Fölsch H. v-SNARE cellubrevin is required for basolateral sorting of AP-1B-dependent cargo in polarized epithelial cells. J Cell Biol 177 (2007) 477-488. In this study the authors classify basolateral cargos into those using a 'direct' or 'indirect' pathway.
    • (2007) J Cell Biol , vol.177 , pp. 477-488
    • Fields, I.C.1    Shteyn, E.2    Pypaert, M.3    Proux-Gillardeaux, V.4    Kang, R.S.5    Galli, T.6    Fölsch, H.7
  • 33
    • 33846785478 scopus 로고    scopus 로고
    • AP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells
    • This study confirms a role for AP-1B in basolateral sorting using RNAi-mediated knock down of μ1B.
    • Gravotta D., Deora A., Perret E., Oyanadel C., Soza A., Schreiner R., Gonzalez A., and Rodriguez-Boulan E. AP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells. Proc Natl Acad Sci U S A 104 (2007) 1564-1569. This study confirms a role for AP-1B in basolateral sorting using RNAi-mediated knock down of μ1B.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1564-1569
    • Gravotta, D.1    Deora, A.2    Perret, E.3    Oyanadel, C.4    Soza, A.5    Schreiner, R.6    Gonzalez, A.7    Rodriguez-Boulan, E.8
  • 34
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Fölsch H., Pypaert M., Schu P., and Mellman I. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J Cell Biol 152 (2001) 595-606
    • (2001) J Cell Biol , vol.152 , pp. 595-606
    • Fölsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 36
    • 37249016585 scopus 로고    scopus 로고
    • Dimeric PKD regulates membrane fission to form transport carriers at the TGN
    • Bossard C., Bresson D., Polishchuk R.S., and Malhotra V. Dimeric PKD regulates membrane fission to form transport carriers at the TGN. J Cell Biol 179 (2007) 1123-1131
    • (2007) J Cell Biol , vol.179 , pp. 1123-1131
    • Bossard, C.1    Bresson, D.2    Polishchuk, R.S.3    Malhotra, V.4
  • 37
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff K.K., Yeaman C., Anandasabapathy N., Hsu S.C., Rodriguez-Boulan E., Scheller R.H., and Nelson W.J. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93 (1998) 731-740
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 38
    • 1242284588 scopus 로고    scopus 로고
    • Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells
    • Yeaman C., Grindstaff K.K., and Nelson W.J. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J Cell Sci 117 (2004) 559-570
    • (2004) J Cell Sci , vol.117 , pp. 559-570
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 39
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • Munson M., and Novick P. The exocyst defrocked, a framework of rods revealed. Nat Struct Mol Biol 13 (2006) 577-581
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 577-581
    • Munson, M.1    Novick, P.2
  • 40
    • 21844443829 scopus 로고    scopus 로고
    • Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase
    • Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H., and Brunger A.T. Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J 24 (2005) 2064-2074
    • (2005) EMBO J , vol.24 , pp. 2064-2074
    • Jin, R.1    Junutula, J.R.2    Matern, H.T.3    Ervin, K.E.4    Scheller, R.H.5    Brunger, A.T.6
  • 44
    • 27144456598 scopus 로고    scopus 로고
    • Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
    • Wu S., Mehta S.Q., Pichaud F., Bellen H.J., and Quiocho F.A. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat Struct Mol Biol 12 (2005) 879-885
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 879-885
    • Wu, S.1    Mehta, S.Q.2    Pichaud, F.3    Bellen, H.J.4    Quiocho, F.A.5
  • 45
    • 34948831499 scopus 로고    scopus 로고
    • Exocyst requirement for endocytic traffic directed toward the apical and basolateral poles of polarized MDCK cells
    • Oztan A., Silvis M., Weisz O.A., Bradbury N.A., Hsu S.C., Goldenring J.R., Yeaman C., and Apodaca G. Exocyst requirement for endocytic traffic directed toward the apical and basolateral poles of polarized MDCK cells. Mol Biol Cell 18 (2007) 3978-3992
    • (2007) Mol Biol Cell , vol.18 , pp. 3978-3992
    • Oztan, A.1    Silvis, M.2    Weisz, O.A.3    Bradbury, N.A.4    Hsu, S.C.5    Goldenring, J.R.6    Yeaman, C.7    Apodaca, G.8
  • 46
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • Müsch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E., and Brennwald P.J. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol Biol Cell 13 (2002) 158-168
    • (2002) Mol Biol Cell , vol.13 , pp. 158-168
    • Müsch, A.1    Cohen, D.2    Yeaman, C.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 47
    • 0242298589 scopus 로고    scopus 로고
    • The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells
    • Ang A.L., Fölsch H., Koivisto U.M., Pypaert M., and Mellman I. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. J Cell Biol 163 (2003) 339-350
    • (2003) J Cell Biol , vol.163 , pp. 339-350
    • Ang, A.L.1    Fölsch, H.2    Koivisto, U.M.3    Pypaert, M.4    Mellman, I.5
  • 48
    • 33745596421 scopus 로고    scopus 로고
    • Rab10 regulates membrane transport through early endosomes of polarized Madin-Darby canine kidney cells
    • Babbey C.M., Ahktar N., Wang E., Chen C.C., Grant B.D., and Dunn K.W. Rab10 regulates membrane transport through early endosomes of polarized Madin-Darby canine kidney cells. Mol Biol Cell 17 (2006) 3156-3175
    • (2006) Mol Biol Cell , vol.17 , pp. 3156-3175
    • Babbey, C.M.1    Ahktar, N.2    Wang, E.3    Chen, C.C.4    Grant, B.D.5    Dunn, K.W.6
  • 49
    • 33845537749 scopus 로고    scopus 로고
    • Rab10 is involved in basolateral transport in polarized Madin-Darby canine kidney cells
    • Schuck S., Gerl M.J., Ang A., Manninen A., Keller P., Mellman I., and Simons K. Rab10 is involved in basolateral transport in polarized Madin-Darby canine kidney cells. Traffic 8 (2007) 47-60
    • (2007) Traffic , vol.8 , pp. 47-60
    • Schuck, S.1    Gerl, M.J.2    Ang, A.3    Manninen, A.4    Keller, P.5    Mellman, I.6    Simons, K.7
  • 50
    • 1542374119 scopus 로고    scopus 로고
    • Parsing the polarity code
    • Macara I.G. Parsing the polarity code. Nat Rev Mol Cell Biol 5 (2004) 220-231
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 220-231
    • Macara, I.G.1
  • 51
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski R., Hall A., and Mellman I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat Cell Biol 1 (1999) 8-13
    • (1999) Nat Cell Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 53
    • 34247148026 scopus 로고    scopus 로고
    • Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells
    • Through expression of dominant-negative tail fragments, this study demonstrates that the Rab8 effector myosin VI partakes in the AP-1B pathway.
    • Au J.S., Puri C., Ihrke G., Kendrick-Jones J., and Buss F. Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells. J Cell Biol 177 (2007) 103-114. Through expression of dominant-negative tail fragments, this study demonstrates that the Rab8 effector myosin VI partakes in the AP-1B pathway.
    • (2007) J Cell Biol , vol.177 , pp. 103-114
    • Au, J.S.1    Puri, C.2    Ihrke, G.3    Kendrick-Jones, J.4    Buss, F.5
  • 54
    • 0033697037 scopus 로고    scopus 로고
    • A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex
    • Nakagawa T., Setou M., Seog D., Ogasawara K., Dohmae N., Takio K., and Hirokawa N. A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. Cell 103 (2000) 569-581
    • (2000) Cell , vol.103 , pp. 569-581
    • Nakagawa, T.1    Setou, M.2    Seog, D.3    Ogasawara, K.4    Dohmae, N.5    Takio, K.6    Hirokawa, N.7
  • 55
    • 33846611043 scopus 로고    scopus 로고
    • Type Igamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with micro1B adaptin
    • This interesting study links a phosphatidylinositide-5-kinase to AP-1B and E-cadherin trafficking.
    • Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., and Anderson R.A. Type Igamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with micro1B adaptin. J Cell Biol 176 (2007) 343-353. This interesting study links a phosphatidylinositide-5-kinase to AP-1B and E-cadherin trafficking.
    • (2007) J Cell Biol , vol.176 , pp. 343-353
    • Ling, K.1    Bairstow, S.F.2    Carbonara, C.3    Turbin, D.A.4    Huntsman, D.G.5    Anderson, R.A.6
  • 56
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen T., Honing S., Icking A., Tikkanen R., and Hunziker W. AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nat Cell Biol 4 (2002) 154-159
    • (2002) Nat Cell Biol , vol.4 , pp. 154-159
    • Simmen, T.1    Honing, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 58
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involved in primary cilium formation
    • •], these studies demonstrate an involvement of Rab8a in formation of the primary cilium.
    • •], these studies demonstrate an involvement of Rab8a in formation of the primary cilium.
    • (2007) J Cell Biol
    • Yoshimura, S.I.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.