메뉴 건너뛰기




Volumn 119, Issue 14, 2006, Pages 2995-3007

Molecular determinants for differential membrane trafficking of PMCA1 and PMCA2 in mammalian hair cells

Author keywords

Alternative splicing; Inner ear explant; Intracellular loop; Leucine isoleucine signal; Stereocilia

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; CELL MEMBRANE PROTEIN; ISOLEUCINE; ISOPROTEIN; LEUCINE; MOLECULAR MARKER;

EID: 33746786784     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03030     Document Type: Article
Times cited : (58)

References (54)
  • 2
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti, B., Kosen, P. A., Kuntz, I. D., Cohen, F. E. and Mostov, K. E. (1993). Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. J. Cell Biol. 123, 1149-1160.
    • (1993) J. Cell Biol. , vol.123 , pp. 1149-1160
    • Aroeti, B.1    Kosen, P.A.2    Kuntz, I.D.3    Cohen, F.E.4    Mostov, K.E.5
  • 3
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino, J. S. and Dell'Angelica, E. C. (1999). Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145, 923-926.
    • (1999) J. Cell Biol. , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 4
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S. and Traub, L. M. (2003). Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 5
    • 0038381495 scopus 로고    scopus 로고
    • 2+-ATPase isoform 2 alters its membrane targeting
    • 2+-ATPase isoform 2 alters its membrane targeting. J. Biol. Chem. 278, 18464-18470.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18464-18470
    • Chicka, M.C.1    Strehler, E.E.2
  • 6
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang, J. Z. and Sung, C. H. (1998). The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J. Cell Biol. 142, 1245-1256.
    • (1998) J. Cell Biol. , vol.142 , pp. 1245-1256
    • Chuang, J.Z.1    Sung, C.H.2
  • 7
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • Cohen, A. R., Woods, D. F., Marfatia, S. M., Walther, Z., Chishti, A. H. and Anderson, J. M. (1998). Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J. Cell Biol. 142, 129-138.
    • (1998) J. Cell Biol. , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3    Walther, Z.4    Chishti, A.H.5    Anderson, J.M.6
  • 8
    • 4344713234 scopus 로고    scopus 로고
    • The basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium
    • Deora, A. A., Gravotta, D., Kreitzer, G., Hu, J., Bok, D. and Rodriguez-Boulan, E. (2004). The basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium. Mol. Biol. Cell 15, 4148-4165.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4148-4165
    • Deora, A.A.1    Gravotta, D.2    Kreitzer, G.3    Hu, J.4    Bok, D.5    Rodriguez-Boulan, E.6
  • 10
    • 0026710613 scopus 로고
    • 2+ pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid
    • 2+ pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid. J. Biol. Chem. 267, 11800-11805.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11800-11805
    • Filoteo, A.G.1    Enyedi, A.2    Penniston, J.T.3
  • 11
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Folsch, H., Ohno, H., Bonifacino, J. S. and Mellman, I. (1999). A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99, 189-198.
    • (1999) Cell , vol.99 , pp. 189-198
    • Folsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 12
    • 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. (2002). The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat. Cell Biol. 4, 605-609.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 605-609
    • Gan, Y.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 14
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker, W. and Fumey, C. (1994). A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J. 13, 2963-2969.
    • (1994) EMBO J. , vol.13 , pp. 2963-2969
    • Hunziker, W.1    Fumey, C.2
  • 15
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. (2001). Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13, 470-477.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 16
    • 0034008665 scopus 로고    scopus 로고
    • Structural determinants required for apical sorting of an intestinal brush-border membrane protein
    • Jacob, R., Alfalah, M., Grunberg, J., Obendorf, M. and Naim, H. Y. (2000). Structural determinants required for apical sorting of an intestinal brush-border membrane protein. J. Biol. Chem. 275, 6566-6572.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6566-6572
    • Jacob, R.1    Alfalah, M.2    Grunberg, J.3    Obendorf, M.4    Naim, H.Y.5
  • 17
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigmal 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. (2003). Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigmal and AP-3 delta-sigma3 hemicomplexes. J. Cell Biol. 163, 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
  • 19
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller, P. and Simons, K. (1997). Post-Golgi biosynthetic trafficking. J. Cell Sci. 110, 3001-3009.
    • (1997) J. Cell Sci. , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 20
    • 33644849472 scopus 로고    scopus 로고
    • The cytosolic C-terminus of the peptide transporter PEPT2 is involved in apical membrane localization of the protein
    • Klapper, M., Daniel, H. and Doering, F. (2006). The cytosolic C-terminus of the peptide transporter PEPT2 is involved in apical membrane localization of the protein. Am. J. Physiol. Cell Physiol. 290, C472-C483.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Klapper, M.1    Daniel, H.2    Doering, F.3
  • 21
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu, A., Avalos, R. T., Sanderson, C. M. and Nayak, D. P. (1996). Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70, 6508-6515.
    • (1996) J. Virol. , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 22
    • 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, M. J., Sibarita, J. B., Aresta, S., Murthy, M., Schwarz, T., Camonis, J. and Bellaiche, Y. (2005). Drosophila exocyst components Sec5, Sec6, and Sec15 regulate DE-Cadherin trafficking from recycling endosomes to the plasma membrane. Dev. Cell 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
  • 24
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin, S., Naim, H. Y., Rodriguez, A. C. and Roth, M. G. (1998). Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell Biol. 142, 51-57.
    • (1998) J. Cell Biol. , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 25
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti, M. P., Caras, I. W., Davitz, M. A. and Rodriguez-Boulan, E. (1989). A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109, 2145-2156.
    • (1989) J. Cell Biol. , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 26
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • Lock, J. G. and Stow, J. L. (2005). Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin. Mol. Biol. Cell 16, 1744-1755.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 27
    • 0030479863 scopus 로고    scopus 로고
    • The polarity of the plasma membrane protein RET-PE2 in retinal pigment epithelium is developmentally regulated
    • Marmorstein, A. D., Bonilha, V. L., Chiflet, S., Neill, J. M. and Rodriguez-Boulan, E. (1996). The polarity of the plasma membrane protein RET-PE2 in retinal pigment epithelium is developmentally regulated. J. Cell Sci. 109, 3025-3034.
    • (1996) J. Cell Sci. , vol.109 , pp. 3025-3034
    • Marmorstein, A.D.1    Bonilha, V.L.2    Chiflet, S.3    Neill, J.M.4    Rodriguez-Boulan, E.5
  • 28
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • Matter, K., Hunziker, W. and Mellman, I. (1992). Basolateral sorting of LDL receptor in MDCK cells: the cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell 71, 741-753.
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 29
    • 0035933872 scopus 로고    scopus 로고
    • A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Miranda, K. C., Khromykh, T., Christy, P., Le, T. L., Gottardi, C. J., Yap, A. S., Stow, J. L. and Teasdale, R. D. (2001). A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells. J. Biol. Chem. 276, 22565-22572.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22565-22572
    • Miranda, K.C.1    Khromykh, T.2    Christy, P.3    Le, T.L.4    Gottardi, C.J.5    Yap, A.S.6    Stow, J.L.7    Teasdale, R.D.8
  • 31
    • 0035575592 scopus 로고    scopus 로고
    • Protein trafficking in the exocytic pathway of polarized epithelial cells
    • Nelson, W. J. and Yeaman, C. (2001). Protein trafficking in the exocytic pathway of polarized epithelial cells. Trends Cell Biol. 11, 483-486.
    • (2001) Trends Cell Biol. , vol.11 , pp. 483-486
    • Nelson, W.J.1    Yeaman, C.2
  • 32
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno, H., Aguilar, R. C., Yeh, D., Taura, D., Saito, T. and Bonifacino, J. S. (1998). The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J. Biol. Chem. 273, 25915-25921.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 34
    • 23844481103 scopus 로고    scopus 로고
    • The apical targeting signal of the P2Y2 receptor is located in its first extracellular loop
    • Qi, A. D., Wolff, S. C. and Nicholas, R. A. (2005). The apical targeting signal of the P2Y2 receptor is located in its first extracellular loop. J. Biol. Chem. 280, 29169-29175.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29169-29175
    • Qi, A.D.1    Wolff, S.C.2    Nicholas, R.A.3
  • 35
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport, I., Chen, Y. C., Cupers, P., Shoelson, S. E. and Kirchhausen, T. (1998). Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17, 2148-2155.
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 36
    • 0037374279 scopus 로고    scopus 로고
    • An evolutionarily conserved dileucine motif in Shal K+ channels mediates dendritic targeting
    • Rivera, J. F., Ahmad, S., Quick, M. W., Liman, E. R. and Arnold, D. B. (2003). An evolutionarily conserved dileucine motif in Shal K+ channels mediates dendritic targeting. Nat. Neurosci. 6, 243-250.
    • (2003) Nat. Neurosci. , vol.6 , pp. 243-250
    • Rivera, J.F.1    Ahmad, S.2    Quick, M.W.3    Liman, E.R.4    Arnold, D.B.5
  • 37
    • 0034708439 scopus 로고    scopus 로고
    • The cytoplasmic tail of CD1d contains two overlapping basolateral sorting signals
    • Rodionov, D. G., Nordeng, T. W., Kongsvik, T. L. and Bakke, O. (2000). The cytoplasmic tail of CD1d contains two overlapping basolateral sorting signals. J. Biol. Chem. 275, 8279-8282.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8279-8282
    • Rodionov, D.G.1    Nordeng, T.W.2    Kongsvik, T.L.3    Bakke, O.4
  • 38
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan, E. and Gonzalez, A. (1999). Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol. 9, 291-294.
    • (1999) Trends Cell Biol. , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 39
    • 0032544612 scopus 로고    scopus 로고
    • LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia
    • Rongo, C., Whitfield, C. W., Rodal, A., Kim, S. K. and Kaplan, J. M. (1998). LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell 94, 751-759.
    • (1998) Cell , vol.94 , pp. 751-759
    • Rongo, C.1    Whitfield, C.W.2    Rodal, A.3    Kim, S.K.4    Kaplan, J.M.5
  • 40
    • 0032500602 scopus 로고    scopus 로고
    • Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Roush, D. L., Gottardi, C. J., Naim, H. Y., Roth, M. G. and Caplan, M. J. (1998). Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells. J. Biol. Chem. 273, 26862-26869.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26862-26869
    • Roush, D.L.1    Gottardi, C.J.2    Naim, H.Y.3    Roth, M.G.4    Caplan, M.J.5
  • 41
    • 1642322799 scopus 로고    scopus 로고
    • An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal
    • Rzadzinska, A. K., Schneider, M. E., Davies, C., Riordan, G. P. and Kachar, B. (2004). An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal. J. Cell Biol. 164, 887-897.
    • (2004) J. Cell Biol. , vol.164 , pp. 887-897
    • Rzadzinska, A.K.1    Schneider, M.E.2    Davies, C.3    Riordan, G.P.4    Kachar, B.5
  • 42
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele, P., Peranen, J. and Simons, K. (1995). N-glycans as apical sorting signals in epithelial cells. Nature 378, 96-98.
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 44
    • 0032913573 scopus 로고    scopus 로고
    • Basolateral sorting of furin in MDCK cells requires a phenylalanine-isoleucine motif together with an acidic amino acid cluster
    • Simmen, T., Nobile, M., Bonifacino, J. S. and Hunziker, W. (1999). Basolateral sorting of furin in MDCK cells requires a phenylalanine-isoleucine motif together with an acidic amino acid cluster. Mol. Cell. Biol. 19, 3136-3144.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3136-3144
    • Simmen, T.1    Nobile, M.2    Bonifacino, J.S.3    Hunziker, W.4
  • 45
    • 0030907201 scopus 로고    scopus 로고
    • Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells
    • Simonsen, A., Stang, E., Bremnes, B., Roe, M., Prydz, K. and Bakke, O. (1997). Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells. J. Cell Sci. 110, 597-609.
    • (1997) J. Cell Sci. , vol.110 , pp. 597-609
    • Simonsen, A.1    Stang, E.2    Bremnes, B.3    Roe, M.4    Prydz, K.5    Bakke, O.6
  • 46
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske, J. S., Kaech, S. M., Harp, S. A. and Kim, S. K. (1996). LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85, 195-204.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 49
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler, E. E. and Zacharias, D. A. (2001). Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81, 21-50.
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 50
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan, L., Molloy, S. S., Thomas, L., Liu, G., Xiang, Y., Rybak, S. L. and Thomas, G. (1998). PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 94, 205-216.
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1    Molloy, S.S.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Rybak, S.L.6    Thomas, G.7
  • 51
    • 3042547588 scopus 로고    scopus 로고
    • Low endolymph calcium concentrations in deafwaddler2J mice suggest that PMCA2 contributes to endolymph calcium maintenance
    • Wood, J. D., Muchinsky, S. J., Filoteo, A. G., Penniston, J. T. and Tempel, B. L. (2004). Low endolymph calcium concentrations in deafwaddler2J mice suggest that PMCA2 contributes to endolymph calcium maintenance. J. Assoc. Res. Otolaryngol. 5, 99-110.
    • (2004) J. Assoc. Res. Otolaryngol. , vol.5 , pp. 99-110
    • Wood, J.D.1    Muchinsky, S.J.2    Filoteo, A.G.3    Penniston, J.T.4    Tempel, B.L.5
  • 53
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman, C., Le Gall, A. H., Baldwin, A. N., Monlauzeur, L., Le Bivic, A. and Rodriguez-Boulan, E. (1997). The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139, 929-940.
    • (1997) J. Cell Biol. , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 54
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • Yeaman, C., Grindstaff, K. K. and Nelson, W. J. (1999). New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol. Rev. 79, 73-98.
    • (1999) Physiol. Rev. , vol.79 , pp. 73-98
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.