메뉴 건너뛰기




Volumn 13, Issue 12, 2002, Pages 4317-4332

Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; LYSOSOME PROTEIN; PROTEIN RAB34; RAB PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; COMPLEMENTARY DNA; GLUTATHIONE TRANSFERASE; LYSINE; RAB PROTEIN, TRITICUM AESTIVUM; RAB34 PROTEIN, MOUSE; RILP PROTEIN, HUMAN; RILP PROTEIN, MOUSE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; VEGETABLE PROTEIN;

EID: 0036915823     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-05-0280     Document Type: Article
Times cited : (105)

References (48)
  • 1
    • 0034698202 scopus 로고    scopus 로고
    • Rabl recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan, B.B., Moyer, B.D., and Balch, W.E. (2000). Rabl recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion. Science 289, 444-448.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 2
    • 0033535617 scopus 로고    scopus 로고
    • A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins
    • Barr, F.A. (1999). A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr. Biol. 9, 381-384.
    • (1999) Curr. Biol. , vol.9 , pp. 381-384
    • Barr, F.A.1
  • 3
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock, J.B., Matern, H.T., Peden, A.A., and Scheller, R.H. (2001). A genomic perspective on membrane compartment organization. Nature 409, 839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 4
    • 0026744303 scopus 로고
    • The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C., Parton, R.G., Mather, I.H., Stunnenberg, H., Simons, K., Hoflack, B., and Zerial, M. (1992). The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 5
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo, G., Alifano, P., Roberti, V., Bruni, C.B., and Bucci, C. (2001). Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes. EMBO J. 20, 683-693.
    • (2001) EMBO J. , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 7
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • Carroll, K.S., Hanna, J., Simon, I., Krise, J., Barbero, P., and Pfeffer, S.R. (2001). Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 292, 1373-1376.
    • (2001) Science , vol.292 , pp. 1373-1376
    • Carroll, K.S.1    Hanna, J.2    Simon, I.3    Krise, J.4    Barbero, P.5    Pfeffer, S.R.6
  • 9
    • 0033180113 scopus 로고    scopus 로고
    • The role of ARF and Rab GTPases in membrane transport
    • Chavrier, P., and Goud, B. (1999). The role of ARF and Rab GTPases in membrane transport. Curr. Opin. Cell Biol. 11, 466-475.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 466-475
    • Chavrier, P.1    Goud, B.2
  • 10
    • 0034044580 scopus 로고    scopus 로고
    • Multiple aspects of Rab protein action in the secretory pathway: Focus on Rab3 and Rab6
    • Darchen, F., and Goud, B. (2000). Multiple aspects of Rab protein action in the secretory pathway: Focus on Rab3 and Rab6. Biochimie 82, 375-384.
    • (2000) Biochimie , vol.82 , pp. 375-384
    • Darchen, F.1    Goud, B.2
  • 13
    • 0031975699 scopus 로고    scopus 로고
    • The Golgi apparatus: 100 years of progress and controversy
    • Farquhar, M.G., and Palade, G.E. (1998). The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol. 8, 2-10.
    • (1998) Trends Cell Biol. , vol.8 , pp. 2-10
    • Farquhar, M.G.1    Palade, G.E.2
  • 14
    • 0035809911 scopus 로고    scopus 로고
    • A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton
    • Gao, Y., and Sztul, E. (2001). A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton. J. Cell Biol. 152, 877-894.
    • (2001) J. Cell Biol. , vol.152 , pp. 877-894
    • Gao, Y.1    Sztul, E.2
  • 15
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. (2001). The endocytic pathway: A mosaic of domains. Nat. Rev. Mol. Cell Biol. 2, 721-730.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 18
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 20
    • 0036171544 scopus 로고    scopus 로고
    • Motor-cargo interactions: The key to transport specificity
    • Karcher, R.L., Deacon, S.W., and Gelfand, V.I. (2002). Motor-cargo interactions: The key to transport specificity. Trends Cell Biol. 12, 21-27.
    • (2002) Trends Cell Biol. , vol.12 , pp. 21-27
    • Karcher, R.L.1    Deacon, S.W.2    Gelfand, V.I.3
  • 21
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localization domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen, L., Teasdale, R.D., van Vliet, C., and Gleeson, P.A. (1999). A novel Golgi-localization domain shared by a class of coiled-coil peripheral membrane proteins. Curt. Biol. 9, 385-388.
    • (1999) Curt. Biol. , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    Van Vliet, C.3    Gleeson, P.A.4
  • 22
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., Donaldson, J.G., and Lippincott-Schwartz, J. (1992). Brefeldin A: Insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 23
    • 0035223205 scopus 로고    scopus 로고
    • Asymmetric cell division during animal development
    • Knoblich, J.A. (2001). Asymmetric cell division during animal development. Nat. Rev. Mol. Cell. Biol. 2, 11-20.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 11-20
    • Knoblich, J.A.1
  • 24
    • 0026601916 scopus 로고
    • Immunotocalization of cytoplasmic dynein to lysosomes in cultured cells
    • Lin, S.X., and Collins, C.A. (1992). Immunotocalization of cytoplasmic dynein to lysosomes in cultured cells. J. Cell Sci. 101, 125-137.
    • (1992) J. Cell Sci. , vol.101 , pp. 125-137
    • Lin, S.X.1    Collins, C.A.2
  • 25
    • 0032005206 scopus 로고    scopus 로고
    • Cytoskeletal proteins and Golgi dynamics
    • Lippincott-Schwartz, J. (1998). Cytoskeletal proteins and Golgi dynamics. Curr. Opin. Cell Biol. 10, 52-59.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 52-59
    • Lippincott-Schwartz, J.1
  • 26
    • 0030060309 scopus 로고    scopus 로고
    • The mammalian ARF-like protein (Arll) is associated with the Golgi complex
    • Lowe, S.L., Wong, S.H., and Hong, W. (1996). The mammalian ARF-like protein (Arll) is associated with the Golgi complex. J. Cell Sci. 109, 209-220.
    • (1996) J. Cell Sci. , vol.109 , pp. 209-220
    • Lowe, S.L.1    Wong, S.H.2    Hong, W.3
  • 27
    • 0035691916 scopus 로고    scopus 로고
    • Regulation of Golgi structure and function by ARF-like protein 1 (Arl1)
    • Lu, L., Horstmann, H., Ng, C., and Hong, W. (2001). Regulation of Golgi structure and function by ARF-like protein 1 (Arl1). J. Cell Sci. 114, 4543-4555.
    • (2001) J. Cell Sci. , vol.114 , pp. 4543-4555
    • Lu, L.1    Horstmann, H.2    Ng, C.3    Hong, W.4
  • 28
    • 0035490904 scopus 로고    scopus 로고
    • The melanosome: Membrane dynamics in black and white
    • Marks, M.S., and Seabra, M.C. (2001). The melanosome: Membrane dynamics in black and white. Nat. Rev. Mol. Cell Biol 2, 738-748.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 738-748
    • Marks, M.S.1    Seabra, M.C.2
  • 29
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. (1996). Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 30
    • 0033608167 scopus 로고    scopus 로고
    • Cloning and characterization of a novel Rab-family gene, Rab36, within the region at 22q11.2 that is homozygously deleted in malignant rhabdoid tumors
    • Mori, T., Fukuda, Y., Kuroda, H., Matsumura, T., Ota, S., Sugimoto, T., Nakamura, Y., and Inazawa, J. (1999). Cloning and characterization of a novel Rab-family gene, Rab36, within the region at 22q11.2 that is homozygously deleted in malignant rhabdoid tumors. Biochem. Biophys. Res. Commun. 254, 594-600.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 594-600
    • Mori, T.1    Fukuda, Y.2    Kuroda, H.3    Matsumura, T.4    Ota, S.5    Sugimoto, T.6    Nakamura, Y.7    Inazawa, J.8
  • 31
    • 0026279767 scopus 로고
    • Molecular cloning of a member of a new class of low-molecular-weight GTP-binding proteins
    • Morimoto, B.H., Chuang, C.C., and Koshland, D.E., Jr. (1991). Molecular cloning of a member of a new class of low-molecular-weight GTP-binding proteins. Genes Dev. 5, 2386-2391.
    • (1991) Genes Dev. , vol.5 , pp. 2386-2391
    • Morimoto, B.H.1    Chuang, C.C.2    Koshland D.E., Jr.3
  • 32
    • 0035024551 scopus 로고    scopus 로고
    • Rabl interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
    • Moyer, B.D., Allan, B.B., and Balch, W.E. (2001). Rabl interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic 2, 268-276.
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 33
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain: A novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro, S., and Nichols, B.J. (1999). The GRIP domain: A novel Golgi-targeting domain found in several coiled-coil proteins. Curr. Biol. 9, 377-380.
    • (1999) Curr. Biol. , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 35
    • 0035798385 scopus 로고    scopus 로고
    • Evolution of the Rab family of small GTP-binding proteins
    • Pereira-Leal, J.B., and Seabra, M.C. (2000). Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol. 313, 889-901.
    • (2000) J. Mol. Biol. , vol.313 , pp. 889-901
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 36
    • 0030693642 scopus 로고    scopus 로고
    • The Beige/Chediak-Higashi syndrome gene encodes a widely expressed cytosolic protein
    • Perou, C.M., Leslie, J.D., Green, W., Li, L., Ward, D.M., and Kaplan, J. (1997). The Beige/Chediak-Higashi syndrome gene encodes a widely expressed cytosolic protein. J. Biol. Chem. 272, 29790-29794.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29790-29794
    • Perou, C.M.1    Leslie, J.D.2    Green, W.3    Li, L.4    Ward, D.M.5    Kaplan, J.6
  • 37
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • Pfeffer, S.R. (2001). Rab GTPases: Specifying and deciphering organelle identity and function. Trends Cell Biol. 11, 487-491.
    • (2001) Trends Cell Biol. , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 38
    • 0035425411 scopus 로고    scopus 로고
    • Ypt and Rab GTPases: Insight into functions through novel interactions
    • Segev, N. (2001). Ypt and Rab GTPases: Insight into functions through novel interactions. Curr. Opin. Cell Biol. 13, 500-511.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 500-511
    • Segev, N.1
  • 39
    • 0035842903 scopus 로고    scopus 로고
    • A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
    • Short, B., Preisinger, C., Korner, R., Kopajtich, R., Byron, O., and Barr, F.A. (2001). A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J. Cell Biol. 155, 877-883.
    • (2001) J. Cell Biol. , vol.155 , pp. 877-883
    • Short, B.1    Preisinger, C.2    Korner, R.3    Kopajtich, R.4    Byron, O.5    Barr, F.A.6
  • 40
  • 41
    • 0029822023 scopus 로고    scopus 로고
    • Rab2 is essential for the maturation of pre-Golgi intermediates
    • Tisdale, E.J., and Balch, W.E. (1996). Rab2 is essential for the maturation of pre-Golgi intermediates. J. Biol. Chem. 271, 29372-29379.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29372-29379
    • Tisdale, E.J.1    Balch, W.E.2
  • 42
    • 0035900422 scopus 로고    scopus 로고
    • Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER
    • Valsdottir, R., Hashimoto, H., Ashman, K., Koda, T., Storrie, B., and Nilsson, T. (2001). Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. FEBS Lett. 508, 201-209.
    • (2001) FEBS Lett. , vol.508 , pp. 201-209
    • Valsdottir, R.1    Hashimoto, H.2    Ashman, K.3    Koda, T.4    Storrie, B.5    Nilsson, T.6
  • 45
    • 1842297531 scopus 로고    scopus 로고
    • GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbetl
    • Xu, Y., Wong, S.H., Zhang, T., Subramaniam, V.N., and Hong, W. (1997). GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbetl. J. Biol. Chem. 272, 20162-20166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20162-20166
    • Xu, Y.1    Wong, S.H.2    Zhang, T.3    Subramaniam, V.N.4    Hong, W.5
  • 46
    • 0034944422 scopus 로고    scopus 로고
    • SNX3 regulates endosomal function through its PX-domain-mediated interaction with Ptdlns(3)P
    • Xu, Y., Hortsman, H., Seer, L., Wong, S.H., and Hong, W. (2001). SNX3 regulates endosomal function through its PX-domain-mediated interaction with Ptdlns(3)P. Nature Cell Biol. 3, 658-666.
    • (2001) Nature Cell Biol. , vol.3 , pp. 658-666
    • Xu, Y.1    Hortsman, H.2    Seer, L.3    Wong, S.H.4    Hong, W.5
  • 47
  • 48
    • 0034607684 scopus 로고    scopus 로고
    • Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding
    • Zhu, X., Boman, A.L., Kuai, J., Cieplak, W., and Kahn, R.A. (2000). Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding. J. Biol. Chem. 275, 13465-13475.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13465-13475
    • Zhu, X.1    Boman, A.L.2    Kuai, J.3    Cieplak, W.4    Kahn, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.