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Volumn 7, Issue 11, 2006, Pages 1495-1502

Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin

Author keywords

Apical transport; Cytoplasmic dynein; Rhodopsin; Tctex 1

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; MUTANT PROTEIN; RHODOPSIN; SERINE;

EID: 33749510646     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2006.00482.x     Document Type: Article
Times cited : (37)

References (33)
  • 1
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells
    • Lafont F, Burkhardt JK, Simons K. Involvement of microtubule motors in basolateral and apical transport in kidney cells. Nature 1994; 372: 801-803.
    • (1994) Nature , vol.372 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 2
    • 0035954436 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport
    • Tai AW, Chuang J-Z, Sung C-H. Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport. J Cell Biol 2001; 153: 1499-1509.
    • (2001) J Cell Biol , vol.153 , pp. 1499-1509
    • Tai, A.W.1    Chuang, J.-Z.2    Sung, C.-H.3
  • 3
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath KR, Trimbur GM, Burgess DR. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J Cell Biol 1994; 126: 661-675.
    • (1994) J Cell Biol , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 5
    • 0028986631 scopus 로고
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Waterman-Storer CM, Karki S, Holzbaur EL. The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc Natl Acad Sci U S A 1995; 92: 1634-1638.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 6
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan V, Stankewich MC, Steffen W, Morrow JS, Holzbaur EL, Schnapp BJ. Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids. Mol Cell 2001; 7: 173-183.
    • (2001) Mol Cell , vol.7 , pp. 173-183
    • Muresan, V.1    Stankewich, M.C.2    Steffen, W.3    Morrow, J.S.4    Holzbaur, E.L.5    Schnapp, B.J.6
  • 8
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARPI) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran EA, Tokito MK, Karki S, Holzbaur ELF. Centractin (ARPI) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J Cell Biol 1996; 135: 1815-1829.
    • (1996) J Cell Biol , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 10
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan PS, Leszyk JD, Vaughan KT. Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin. J Biol Chem 2001; 276: 26171-26179.
    • (2001) J Biol Chem , vol.276 , pp. 26171-26179
    • Vaughan, P.S.1    Leszyk, J.D.2    Vaughan, K.T.3
  • 12
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai AW, Chuang J-Z, Bode C, Wolfrum U, Sung C-H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 1999; 97: 877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.-Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.-H.5
  • 13
    • 22044434335 scopus 로고    scopus 로고
    • Dynein anchors its mRNA cargo after apical transport in the Drosophila blastoderm embryo
    • Delanoue R, Davis I. Dynein anchors its mRNA cargo after apical transport in the Drosophila blastoderm embryo. Cell 2005; 122: 97-106.
    • (2005) Cell , vol.122 , pp. 97-106
    • Delanoue, R.1    Davis, I.2
  • 14
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang J-Z, Sung C-H. The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J Cell Biol 1998; 142: 1245-1256.
    • (1998) J Cell Biol , vol.142 , pp. 1245-1256
    • Chuang, J.-Z.1    Sung, C.-H.2
  • 15
    • 0035957959 scopus 로고    scopus 로고
    • Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain
    • Mok YK, Lo KW, Zhang M. Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain. J Biol Chem 2001; 276: 14067-14074.
    • (2001) J Biol Chem , vol.276 , pp. 14067-14074
    • Mok, Y.K.1    Lo, K.W.2    Zhang, M.3
  • 16
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal BM, Shpetner HS, Vallee RB. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol 1987; 105: 1273-1282.
    • (1987) J Cell Biol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 17
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer TA, Sheetz MP. Two activators of microtubule-based vesicle transport. J Cell Biol 1991; 115: 1309-1318.
    • (1991) J Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 18
    • 2342599664 scopus 로고    scopus 로고
    • Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway
    • Polishchuk R, Di Pentima A, Lippincott-Schwartz J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat Cell Biol 2004; 6: 297-307.
    • (2004) Nat Cell Biol , vol.6 , pp. 297-307
    • Polishchuk, R.1    Di Pentima, A.2    Lippincott-Schwartz, J.3
  • 19
    • 0038066606 scopus 로고    scopus 로고
    • An improved rhodopsin/EGFP fusion protein for use in the generation of transgenic Xenopus laevis
    • Jin S, McKee TD, Oprian DD. An improved rhodopsin/EGFP fusion protein for use in the generation of transgenic Xenopus laevis. FEBS Lett 2003; 542: 142-146.
    • (2003) FEBS Lett , vol.542 , pp. 142-146
    • Jin, S.1    McKee, T.D.2    Oprian, D.D.3
  • 20
    • 0037743559 scopus 로고    scopus 로고
    • Opsin activation as a cause of congenital night blindness
    • Jin S, Cornwall MC, Oprian DD. Opsin activation as a cause of congenital night blindness. Nat Neurosci 2003; 6: 731-735.
    • (2003) Nat Neurosci , vol.6 , pp. 731-735
    • Jin, S.1    Cornwall, M.C.2    Oprian, D.D.3
  • 21
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 2001; 20: 2171-2179.
    • (2001) EMBO J , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 23
    • 21344471112 scopus 로고    scopus 로고
    • The dynein light chain Tctex-1 has a dynein-independent role in actin remodeling during neurite outgrowth
    • Chuang JZ, Yeh TY, Bollati F, Conde C, Canavosio F, Caceres A, Sung CH. The dynein light chain Tctex-1 has a dynein-independent role in actin remodeling during neurite outgrowth. Dev Cell 2005; 9: 75-86.
    • (2005) Dev Cell , vol.9 , pp. 75-86
    • Chuang, J.Z.1    Yeh, T.Y.2    Bollati, F.3    Conde, C.4    Canavosio, F.5    Caceres, A.6    Sung, C.H.7
  • 24
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey SR, Snyder SH. PIN: An associated protein inhibitor of neuronal nitric oxide synthase. Science 1996; 274: 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 25
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung C-H, Schneider BG, Agarwal N, Papermaster DS, Nathans J. Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci U S A 1991; 88: 8840-8844.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8840-8844
    • Sung, C.-H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 26
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa: Clustering of functional classes along the polypeptide chain
    • Sung C-H, Davenport CM, Nathans J. Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa: Clustering of functional classes along the polypeptide chain. J Biol Chem 1993; 268: 26645-26649.
    • (1993) J Biol Chem , vol.268 , pp. 26645-26649
    • Sung, C.-H.1    Davenport, C.M.2    Nathans, J.3
  • 27
    • 24344438985 scopus 로고    scopus 로고
    • Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway
    • Yeh TY, Chuang JZ, Sung CH. Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway. J Cell Sci 2005; 118: 3431-3443.
    • (2005) J Cell Sci , vol.118 , pp. 3431-3443
    • Yeh, T.Y.1    Chuang, J.Z.2    Sung, C.H.3
  • 28
    • 0030614352 scopus 로고    scopus 로고
    • NH2-terminal deletion of b-catenin results in stable colocalization of mutant-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion
    • Barth AI, Pollack AL, Altschuler V, Mostov KE, Nelson WJ. NH2-terminal deletion of b-catenin results in stable colocalization of mutant-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion. J Cell Biol 1997; 136: 693-706.
    • (1997) J Cell Biol , vol.136 , pp. 693-706
    • Barth, A.I.1    Pollack, A.L.2    Altschuler, V.3    Mostov, K.E.4    Nelson, W.J.5
  • 29
    • 0032584612 scopus 로고    scopus 로고
    • Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity
    • Tai AW, Chuang J-Z, Sung C-H. Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity. J Biol Chem 1998; 273: 19639-19649.
    • (1998) J Biol Chem , vol.273 , pp. 19639-19649
    • Tai, A.W.1    Chuang, J.-Z.2    Sung, C.-H.3
  • 30
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases
    • Jou TS, Schneeberger EE, Nelson WJ. Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases. J Cell Biol 1998; 142: 101-115.
    • (1998) J Cell Biol , vol.142 , pp. 101-115
    • Jou, T.S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 31
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda MS, Whitney JA, Flores C, Gonzalez S, Cereijido M, Matter K. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 1996; 134: 1031-1049.
    • (1996) J Cell Biol , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 32
    • 1442358790 scopus 로고    scopus 로고
    • Mammalian PAR-1 determines epithelial lumen polarity by organizing the microtubule cytoskeleton
    • Cohen D, Brennwald PJ, Rodriguez-Boulan E, Musch A. Mammalian PAR-1 determines epithelial lumen polarity by organizing the microtubule cytoskeleton. J Cell Biol 2004; 164: 717-727.
    • (2004) J Cell Biol , vol.164 , pp. 717-727
    • Cohen, D.1    Brennwald, P.J.2    Rodriguez-Boulan, E.3    Musch, A.4


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