메뉴 건너뛰기




Volumn 2, Issue 1, 2011, Pages 74-85

HID-1 is a peripheral membrane protein primarily associated with the medial- and trans- Golgi apparatus

Author keywords

fluorescent recovery after photobleaching; Golgi; HID 1; N myristoylation; peripheral membrane protein

Indexed keywords

BREFELDIN A; MEMBRANE PROTEIN; PROTEIN HID 1; UNCLASSIFIED DRUG;

EID: 79953254437     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-011-1008-3     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 0141566672 scopus 로고    scopus 로고
    • Isolation and characterization of high-temperature-induced Dauer formation mutants in Caenorhabditis elegans
    • Ailion, M., and Thomas, J. H. (2003). Isolation and characterization of high-temperature-induced Dauer formation mutants in Caenorhabditis elegans. Genetics 165, 127-144.
    • (2003) Genetics , vol.165 , pp. 127-144
    • Ailion, M.1    Thomas, J.H.2
  • 2
    • 55549089615 scopus 로고    scopus 로고
    • Large ARF guanine nucleotide exchange factors in membrane trafficking
    • Anders, N., and Jürgens, G. (2008). Large ARF guanine nucleotide exchange factors in membrane trafficking. Cell Mol Life Sci 65, 3433-3445.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3433-3445
    • Anders, N.1    Jürgens, G.2
  • 3
    • 0032538315 scopus 로고    scopus 로고
    • Cell nonautonomy of C. elegans daf-2 function in the regulation of diapause and life span
    • Apfeld, J., and Kenyon, C. (1998). Cell nonautonomy of C. elegans daf-2 function in the regulation of diapause and life span. Cell 95, 199-210.
    • (1998) Cell , vol.95 , pp. 199-210
    • Apfeld, J.1    Kenyon, C.2
  • 4
    • 0034015979 scopus 로고    scopus 로고
    • A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegans
    • Birnby, D. A., Link, E. M., Vowels, J. J., Tian, H., Colacurcio, P. L., and Thomas, J. H. (2000). A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegans. Genetics 155, 85-104.
    • (2000) Genetics , vol.155 , pp. 85-104
    • Birnby, D.A.1    Link, E.M.2    Vowels, J.J.3    Tian, H.4    Colacurcio, P.L.5    Thomas, J.H.6
  • 6
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport
    • Campellone, K. G., Webb, N. J., Znameroski, E. A., and Welch, M. D. (2008). WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 134, 148-161.
    • (2008) Cell , vol.134 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 7
    • 0016766716 scopus 로고
    • The dauerlarva, a postembryonic developmental variant of the nematode Caenorhabditis elegans
    • Cassada, R. C., and Russell, R. L. (1975). The dauerlarva, a postembryonic developmental variant of the nematode Caenorhabditis elegans. Dev Biol 46, 326-342.
    • (1975) Dev Biol , vol.46 , pp. 326-342
    • Cassada, R.C.1    Russell, R.L.2
  • 8
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi, J., Chen, J., Schreiber, S. L., and Clardy, J. (1996). Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science 273, 239-242.
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 9
    • 0037317409 scopus 로고    scopus 로고
    • Mental retardation and abnormal skeletal development (Dyggve-Melchior-Clausen dysplasia) due to mutations in a novel, evolutionarily conserved gene
    • Cohn, D. H., Ehtesham, N., Krakow, D., Unger, S., Shanske, A., Reinker, K., Powell, B. R., and Rimoin, D. L. (2003). Mental retardation and abnormal skeletal development (Dyggve-Melchior-Clausen dysplasia) due to mutations in a novel, evolutionarily conserved gene. Am J Hum Genet 72, 419-428.
    • (2003) Am J Hum Genet , vol.72 , pp. 419-428
    • Cohn, D.H.1    Ehtesham, N.2    Krakow, D.3    Unger, S.4    Shanske, A.5    Reinker, K.6    Powell, B.R.7    Rimoin, D.L.8
  • 10
    • 0031915371 scopus 로고    scopus 로고
    • N-ethylmaleimide-sensitive factor-dependent alpha-SNAP release, an early event in the docking/fusion process, is not regulated by Rab GTPases
    • Colombo, M. I., Gelberman, S. C., Whiteheart, S. W., and Stahl, P. D. (1998). N-ethylmaleimide-sensitive factor-dependent alpha-SNAP release, an early event in the docking/fusion process, is not regulated by Rab GTPases. J Biol Chem 273, 1334-1338.
    • (1998) J Biol Chem , vol.273 , pp. 1334-1338
    • Colombo, M.I.1    Gelberman, S.C.2    Whiteheart, S.W.3    Stahl, P.D.4
  • 13
    • 33751005265 scopus 로고    scopus 로고
    • Regulating cell surface glycosylation with a small-molecule switch
    • Dube, D. H., de Graffenried, C. L., and Kohler, J. J. (2006). Regulating cell surface glycosylation with a small-molecule switch. Methods Enzymol 415, 213-229.
    • (2006) Methods Enzymol , vol.415 , pp. 213-229
    • Dube, D.H.1    de Graffenried, C.L.2    Kohler, J.J.3
  • 16
    • 0028132043 scopus 로고
    • Targeting of proteins to the Golgi apparatus
    • Gleeson, P. A., Teasdale, R. D., and Burke, J. (1994). Targeting of proteins to the Golgi apparatus. Glycoconj J 11, 381-394.
    • (1994) Glycoconj J , vol.11 , pp. 381-394
    • Gleeson, P.A.1    Teasdale, R.D.2    Burke, J.3
  • 17
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence
    • Humphrey, J. S., Peters, P. J., Yuan, L. C., and Bonifacino, J. S. (1993). Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence. J Cell Biol 120, 1123-1135.
    • (1993) J Cell Biol , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 18
    • 0033767237 scopus 로고    scopus 로고
    • Suppressors of transforming growth factor-beta pathway mutants in the Caenorhabditis elegans dauer formation pathway
    • Inoue, T., and Thomas, J. H. (2000a). Suppressors of transforming growth factor-beta pathway mutants in the Caenorhabditis elegans dauer formation pathway. Genetics 156, 1035-1046.
    • (2000) Genetics , vol.156 , pp. 1035-1046
    • Inoue, T.1    Thomas, J.H.2
  • 19
    • 0033983344 scopus 로고    scopus 로고
    • Targets of TGF-beta signaling in Caenorhabditis elegans dauer formation
    • Inoue, T., and Thomas, J. H. (2000b). Targets of TGF-beta signaling in Caenorhabditis elegans dauer formation. Dev Biol 217, 192-204.
    • (2000) Dev Biol , vol.217 , pp. 192-204
    • Inoue, T.1    Thomas, J.H.2
  • 20
    • 0026802406 scopus 로고
    • Characterization of early and late endocytic compartments of the transferrin cycle. Transferrin receptor antibody blocks erythroid differentiation by trapping the receptor in the early endosome
    • Killisch, I., Steinlein, P., Römisch, K., Hollinshead, R., Beug, H., and Griffiths, G. (1992). Characterization of early and late endocytic compartments of the transferrin cycle. Transferrin receptor antibody blocks erythroid differentiation by trapping the receptor in the early endosome. J Cell Sci 103, 211-232.
    • (1992) J Cell Sci , vol.103 , pp. 211-232
    • Killisch, I.1    Steinlein, P.2    Römisch, K.3    Hollinshead, R.4    Beug, H.5    Griffiths, G.6
  • 21
    • 0032981705 scopus 로고    scopus 로고
    • The Golgi-targeting sequence of the peripheral membrane protein p230
    • Kjer-Nielsen, L., van Vliet, C., Erlich, R., Toh, B. H., and Gleeson, P. A. (1999). The Golgi-targeting sequence of the peripheral membrane protein p230. J Cell Sci 112, 1645-1654.
    • (1999) J Cell Sci , vol.112 , pp. 1645-1654
    • Kjer-Nielsen, L.1    van Vliet, C.2    Erlich, R.3    Toh, B.H.4    Gleeson, P.A.5
  • 23
    • 0035805642 scopus 로고    scopus 로고
    • The transmembrane domain of syntaxin 1A is critical for cytoplasmic domain protein-protein interactions
    • Lewis, J. L., Dong, M., Earles, C. A., and Chapman, E. R. (2001). The transmembrane domain of syntaxin 1A is critical for cytoplasmic domain protein-protein interactions. J Biol Chem 276, 15458-15465.
    • (2001) J Biol Chem , vol.276 , pp. 15458-15465
    • Lewis, J.L.1    Dong, M.2    Earles, C.A.3    Chapman, E.R.4
  • 24
    • 0034726746 scopus 로고    scopus 로고
    • Mouse prenylated Rab acceptor is a novel Golgi membrane protein
    • Liang, Z., and Li, G. (2000). Mouse prenylated Rab acceptor is a novel Golgi membrane protein. Biochem Biophys Res Commun 275, 509-516.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 509-516
    • Liang, Z.1    Li, G.2
  • 25
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., Yuan, L., Tipper, C., Amherdt, M., Orci, L., and Klausner, R. D. (1991). Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67, 601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 27
    • 34250663574 scopus 로고    scopus 로고
    • The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology
    • Lorenz, H., Hailey, D. W., Wunder, C., and Lippincott-Schwartz, J. (2006). The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology. Nat Protoc 1, 276-279.
    • (2006) Nat Protoc , vol.1 , pp. 276-279
    • Lorenz, H.1    Hailey, D.W.2    Wunder, C.3    Lippincott-Schwartz, J.4
  • 28
    • 52449084681 scopus 로고    scopus 로고
    • Characterization of the topology and functional domains of RKTG
    • Luo, X., Feng, L., Jiang, X., Xiao, F., Wang, Z., Feng, G. S., and Chen, Y. (2008). Characterization of the topology and functional domains of RKTG. Biochem J 414, 399-406.
    • (2008) Biochem J , vol.414 , pp. 399-406
    • Luo, X.1    Feng, L.2    Jiang, X.3    Xiao, F.4    Wang, Z.5    Feng, G.S.6    Chen, Y.7
  • 29
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio, J. P., Brake, B., Banting, G., Howell, K. E., Braghetta, P., and Stanley, K. K. (1990). Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem J 270, 97-102.
    • (1990) Biochem J , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 33
  • 34
    • 76249107656 scopus 로고    scopus 로고
    • Rapid inactivation of proteins by rapamycin-induced rerouting to mitochondria
    • Robinson, M. S., Sahlender, D. A., and Foster, S. D. (2010). Rapid inactivation of proteins by rapamycin-induced rerouting to mitochondria. Dev Cell 18, 324-331.
    • (2010) Dev Cell , vol.18 , pp. 324-331
    • Robinson, M.S.1    Sahlender, D.A.2    Foster, S.D.3
  • 35
    • 0025061678 scopus 로고
    • Molecular cloning and overexpression of the human FK506-binding protein FKBP
    • Standaert, R. F., Galat, A., Verdine, G. L., and Schreiber, S. L. (1990). Molecular cloning and overexpression of the human FK506-binding protein FKBP. Nature 346, 671-674.
    • (1990) Nature , vol.346 , pp. 671-674
    • Standaert, R.F.1    Galat, A.2    Verdine, G.L.3    Schreiber, S.L.4
  • 36
    • 33845310879 scopus 로고    scopus 로고
    • Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels
    • Suh, B. C., Inoue, T., Meyer, T., and Hille, B. (2006). Rapid chemically induced changes of PtdIns(4, 5)P2 gate KCNQ ion channels. Science 314, 1454-1457.
    • (2006) Science , vol.314 , pp. 1454-1457
    • Suh, B.C.1    Inoue, T.2    Meyer, T.3    Hille, B.4
  • 37
    • 0035837327 scopus 로고    scopus 로고
    • The transmembrane domain of syntaxin 1A negatively regulates voltage-sensitive Ca(2 +) channels
    • Trus, M., Wiser, O., Goodnough, M. C., and Atlas, D. (2001). The transmembrane domain of syntaxin 1A negatively regulates voltage-sensitive Ca(2 +) channels. Neuroscience 104, 599-607.
    • (2001) Neuroscience , vol.104 , pp. 599-607
    • Trus, M.1    Wiser, O.2    Goodnough, M.C.3    Atlas, D.4
  • 38
    • 0026674071 scopus 로고
    • A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack
    • Waters, M. G., Clary, D. O., and Rothman, J. E. (1992). A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack. J Cell Biol 118, 1015-1026.
    • (1992) J Cell Biol , vol.118 , pp. 1015-1026
    • Waters, M.G.1    Clary, D.O.2    Rothman, J.E.3
  • 39
    • 76649115299 scopus 로고    scopus 로고
    • Protein myristoylation in health and disease
    • Wright, M. H., Heal, W. P., Mann, D. J., and Tate, E. W. (2009). Protein myristoylation in health and disease. J Chem Biol 3, 19-35.
    • (2009) J Chem Biol , vol.3 , pp. 19-35
    • Wright, M.H.1    Heal, W.P.2    Mann, D.J.3    Tate, E.W.4
  • 40
    • 0029067675 scopus 로고
    • Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domaindependent homodimerization and association with alpha- and beta-tubulins
    • Yamaguchi, N., and Fukuda, M. N. (1995). Golgi retention mechanism of beta-1, 4-galactosyltransferase. Membrane-spanning domaindependent homodimerization and association with alpha- and beta-tubulins. J Biol Chem 270, 12170-12176.
    • (1995) J Biol Chem , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 42
    • 0022749229 scopus 로고
    • The transmembrane segment of the human transferrin receptor functions as a signal peptide
    • Zerial, M., Melancon, P., Schneider, C., and Garoff, H. (1986). The transmembrane segment of the human transferrin receptor functions as a signal peptide. EMBO J 5, 1543-1550.
    • (1986) EMBO J , vol.5 , pp. 1543-1550
    • Zerial, M.1    Melancon, P.2    Schneider, C.3    Garoff, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.