메뉴 건너뛰기




Volumn 13, Issue 5, 2003, Pages

Membrane traffic: Arl GTPases get a GRIP on the Golgi

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0037418582     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(03)00116-7     Document Type: Review
Times cited : (36)

References (20)
  • 1
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte, J.R. and Munro, S. (2002). Vesicle tethering complexes in membrane traffic. J. Cell Sci. 115, 2627-2637.
    • (2002) J. Cell Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 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
    • 0033535542 scopus 로고    scopus 로고
    • A novel golgi-localisation 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-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr. Biol. 9, 385-388.
    • (1999) Curr. Biol. , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    Van Vliet, C.3    Gleeson, P.A.4
  • 4
    • 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
  • 5
    • 0037418595 scopus 로고    scopus 로고
    • The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle tethering factors at the Golgi apparatus
    • Panic, B., Whyte, J.R.C., and Munro, S. (2003). The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle tethering factors at the Golgi apparatus. Curr. Biol. 13, this issue.
    • (2003) Curr. Biol. , vol.13 , Issue.THIS ISSUE
    • Panic, B.1    Whyte, J.R.C.2    Munro, S.3
  • 6
    • 0037418580 scopus 로고    scopus 로고
    • Golgi recruitment of GRIP domain proteins by ARF-like GTPase 1 (Arl1p) is regulated by Arf-like GTPase 3 (Arl3p)
    • Gangi Setty, S.R., Shin, M.E., Yoshino, A., Marks, M.S. and Burd, C.G. (2003). Golgi Recruitment of GRIP domain proteins by ARF-like GTPase 1 (Arl1p) is regulated by Arf-like GTPase 3 (Arl3p). Curr. Biol. 13, this issue.
    • (2003) Curr. Biol. , vol.13 , Issue.THIS ISSUE
    • Gangi Setty, S.R.1    Shin, M.E.2    Yoshino, A.3    Marks, M.S.4    Burd, C.G.5
  • 7
    • 0033524931 scopus 로고    scopus 로고
    • Characterization of a novel ADP-ribosylation factor-like protein (yARL3) in Saccharomyces cerevisiae
    • Huang, C.F., Buu, L.M., Yu, W.L. and Lee, F.J. (1999). Characterization of a novel ADP-ribosylation factor-like protein (yARL3) in Saccharomyces cerevisiae. J. Biol. Chem. 274, 3819-3827.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3819-3827
    • Huang, C.F.1    Buu, L.M.2    Yu, W.L.3    Lee, F.J.4
  • 8
    • 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
  • 10
    • 0035933796 scopus 로고    scopus 로고
    • ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: Characterizing ARL1-binding proteins
    • Van Valkenburgh, H., Shern, J.F., Sharer, J.D., Zhu, X. and Kahn, R.A. (2001). ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins. J. Biol. Chem. 276, 22826-22837.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22826-22837
    • Van Valkenburgh, H.1    Shern, J.F.2    Sharer, J.D.3    Zhu, X.4    Kahn, R.A.5
  • 11
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato, S., Renault, L. and Cherfils, J. (2002). Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep. 3, 1035-1041.
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 12
    • 0036173902 scopus 로고    scopus 로고
    • Embryonic lethality caused by apoptosis during gastrulation in mice lacking the gene of the ADP-ribosylation factor-related protein 1
    • Mueller, A.G., Moser, M., Kluge, R., Leder, S., Blum, M., Buttner, R., Joost, H.G. and Schurmann, A. (2002). Embryonic lethality caused by apoptosis during gastrulation in mice lacking the gene of the ADP-ribosylation factor-related protein 1. Mol. Cell. Biol. 22, 1488-1494.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1488-1494
    • Mueller, A.G.1    Moser, M.2    Kluge, R.3    Leder, S.4    Blum, M.5    Buttner, R.6    Joost, H.G.7    Schurmann, A.8
  • 14
    • 0026666672 scopus 로고
    • Human autoantibodies as reagents to conserved Golgi components: Characterization of a peripheral, 230-kDa compartment-specific Golgi protein
    • Kooy, J., Toh, B.H., Pettitt, J.M., Erlich, R. and Gleeson, P.A. (1992). Human autoantibodies as reagents to conserved Golgi components: Characterization of a peripheral, 230-kDa compartment-specific Golgi protein. J. Biol. Chem. 267, 20255-20263.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20255-20263
    • Kooy, J.1    Toh, B.H.2    Pettitt, J.M.3    Erlich, R.4    Gleeson, P.A.5
  • 15
    • 0037423287 scopus 로고    scopus 로고
    • GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
    • Luke, M.R., Kjer-Nielsen, L., Brown, D.L., Stow, J.L. and Gleeson, P.A. (2003). GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J. Biol. Chem. 278, 4216-4226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4216-4226
    • Luke, M.R.1    Kjer-Nielsen, L.2    Brown, D.L.3    Stow, J.L.4    Gleeson, P.A.5
  • 16
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • Shorter, J., Beard, M.B., Seemann, J., Dirac-Svejstrup, A.B. and Warren, G. (2002). Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J. Cell Biol. 157, 45-62.
    • (2002) J. Cell Biol. , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seemann, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 17
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear, E. and Stevens, T.H. (2000). Vps52p, Vps53p and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol. Biol. Cell 11, 305-323.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 18
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou, S. and Pelham, H.R. (2001). An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J. 20, 5991-5998.
    • (2001) EMBO J. , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 19
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz, D., Medkova, M., Walch-Solimena, C. and Novick, P. (2002). Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J. Cell Biol. 157, 1005-1015.
    • (2002) J. Cell Biol. , vol.157 , pp. 1005-1015
    • Ortiz, D.1    Medkova, M.2    Walch-Solimena, C.3    Novick, P.4
  • 20
    • 0036736141 scopus 로고    scopus 로고
    • A Ypt32p exchange factor is a putative effector of Ypt1p
    • Wang, W. and Ferro-Novick, S. (2002). A Ypt32p exchange factor is a putative effector of Ypt1p. Mol. Biol. Cell 13, 3336-3343.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3336-3343
    • Wang, W.1    Ferro-Novick, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.