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Volumn 130, Issue 3, 2017, Pages 602-613

PIGN prevents protein aggregation in the endoplasmic reticulum independently of its function in the GPI synthesis

Author keywords

Endoplasmic reticulum; GPI; MCAHS1 patients; PIGN; Protein aggregation

Indexed keywords

ALANINE; ARGININE; CD59 ANTIGEN; COLLAGEN TYPE 4; EMB 9 PROTEIN; ETHANOLAMINE PHOSPHOTRANSFERASE; GLYCOSYLPHOSPHATIDYLINOSITOL; GREEN FLUORESCENT PROTEIN; HISTIDINE; L SELECTIN; OS156 PROTEIN; PIGN PROTEIN; PROTEIN; UNCLASSIFIED DRUG; CAENORHABDITIS ELEGANS PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL ETHANOLAMINE PHOSPHATE TRANSFERASE 1, HUMAN; PHOSPHOTRANSFERASE; PROTEIN AGGREGATE;

EID: 85012014137     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.196717     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. and Helenius, A. (1992). Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356, 260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 2
    • 84925944413 scopus 로고    scopus 로고
    • Exome sequencing identifies a recessive PIGN splice site mutation as a cause of syndromic congenital diaphragmatic hernia
    • Brady, P. D., Moerman, P., De Catte, L., Deprest, J., Devriendt, K. and Vermeesch, J. R. (2014). Exome sequencing identifies a recessive PIGN splice site mutation as a cause of syndromic congenital diaphragmatic hernia. Eur. J. Med. Genet. 57, 487-493.
    • (2014) Eur. J. Med. Genet , vol.57 , pp. 487-493
    • Brady, P.D.1    Moerman, P.2    De Catte, L.3    Deprest, J.4    Devriendt, K.5    Vermeesch, J.R.6
  • 3
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974). The genetics of Caenorhabditis elegans. Genetics 77, 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 6
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes
    • de Silva, A., Braakman, I. and Helenius, A. (1993). Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. 120, 647-655.
    • (1993) J. Cell Biol , vol.120 , pp. 647-655
    • de Silva, A.1    Braakman, I.2    Helenius, A.3
  • 7
    • 84884904381 scopus 로고    scopus 로고
    • Engineering the Caenorhabditis elegans genome using Cas9-triggered homologous recombination
    • Dickinson, D. J., Ward, J. D., Reiner, D. J. and Goldstein, B. (2013). Engineering the Caenorhabditis elegans genome using Cas9-triggered homologous recombination. Nat. Methods 10, 1028-1034.
    • (2013) Nat. Methods , vol.10 , pp. 1028-1034
    • Dickinson, D.J.1    Ward, J.D.2    Reiner, D.J.3    Goldstein, B.4
  • 8
    • 33746627569 scopus 로고    scopus 로고
    • Factors regulating the abundance and localization of synaptobrevin in the plasma membrane
    • Dittman, J. S. and Kaplan, J. M. (2006). Factors regulating the abundance and localization of synaptobrevin in the plasma membrane. Proc. Natl. Acad. Sci. USA 103, 11399-11404.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11399-11404
    • Dittman, J.S.1    Kaplan, J.M.2
  • 9
    • 0025119643 scopus 로고
    • Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels
    • Dorner, A. J., Wasley, L. C. and Kaufman, R. J. (1990). Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels. Proc. Natl. Acad. Sci. USA 87, 7429-7432.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7429-7432
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 10
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • Espenshade, P., Gimeno, R. E., Holzmacher, E., Teung, P. and Kaiser, C. A. (1995). Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J. Cell Biol. 131, 311-324.
    • (1995) J. Cell Biol , vol.131 , pp. 311-324
    • Espenshade, P.1    Gimeno, R.E.2    Holzmacher, E.3    Teung, P.4    Kaiser, C.A.5
  • 11
    • 0035031192 scopus 로고    scopus 로고
    • Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog
    • Fares, H. and Greenwald, I. (2001). Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog. Nat. Genet. 28, 64-68.
    • (2001) Nat. Genet , vol.28 , pp. 64-68
    • Fares, H.1    Greenwald, I.2
  • 12
    • 70349842313 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol Anchors
    • (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G. W. Hart and M. E. Etzler). Chapter 11. NY: Cold Spring Harbor
    • Ferguson, M.A. J., Kinoshita, T. andHart, G.W. (2009).Glycosylphosphatidylinositol Anchors. In Essentials of Glycobiology (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G. W. Hart and M. E. Etzler). Chapter 11. NY: Cold Spring Harbor. (https://www.ncbi.nlm.nih.gov/books/NBK1966/)
    • (2009) Essentials of Glycobiology
    • Ferguson, M.A.J.1    Kinoshita T.andHart, G.W.2
  • 13
    • 84955710017 scopus 로고    scopus 로고
    • Genotypephenotype correlation of congenital anomalies in multiple congenital anomalies hypotonia seizures syndrome (MCAHS1)/PIGN-related epilepsy
    • Fleming, L., Lemmon, M., Beck, N., Johnson, M., Mu, W., Murdock, D., Bodurtha, J., Hoover-Fong, J., Cohn, R., Bosemani, T. et al. (2015). Genotypephenotype correlation of congenital anomalies in multiple congenital anomalies hypotonia seizures syndrome (MCAHS1)/PIGN-related epilepsy. Am. J. Med. Genet. A 170A, 77-86.
    • (2015) Am. J. Med. Genet. A , vol.170A , pp. 77-86
    • Fleming, L.1    Lemmon, M.2    Beck, N.3    Johnson, M.4    Mu, W.5    Murdock, D.6    Bodurtha, J.7    Hoover-Fong, J.8    Cohn, R.9    Bosemani, T.10
  • 14
    • 0345251965 scopus 로고    scopus 로고
    • MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast
    • Gaynor, E. C., Mondesert, G., Grimme, S. J., Reed, S. I., Orlean, P. and Emr, S. D. (1999). MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol. Biol. Cell 10, 627-648.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 627-648
    • Gaynor, E.C.1    Mondesert, G.2    Grimme, S.J.3    Reed, S.I.4    Orlean, P.5    Emr, S.D.6
  • 15
    • 0030989696 scopus 로고    scopus 로고
    • Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it
    • Graham, P. L., Johnson, J. J., Wang, S., Sibley, M. H., Gupta, M. C. and Kramer, J. M. (1997). Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it. J. Cell Biol. 137, 1171-1183.
    • (1997) J. Cell Biol , vol.137 , pp. 1171-1183
    • Graham, P.L.1    Johnson, J.J.2    Wang, S.3    Sibley, M.H.4    Gupta, M.C.5    Kramer, J.M.6
  • 16
    • 84855444621 scopus 로고    scopus 로고
    • Modern electron microscopy methods for C. elegans
    • Hall, D. H., Hartwieg, E. and Nguyen, K. C. Q. (2012). Modern electron microscopy methods for C. elegans. Methods Cell Biol. 107, 93-149.
    • (2012) Methods Cell Biol , vol.107 , pp. 93-149
    • Hall, D.H.1    Hartwieg, E.2    Nguyen, K.C.Q.3
  • 17
    • 0028965528 scopus 로고
    • In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum
    • Hendershot, L. M., Wei, J. Y., Gaut, J. R., Lawson, B., Freiden, P. J. and Murti, K. G. (1995). In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell 6, 283-296.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 283-296
    • Hendershot, L.M.1    Wei, J.Y.2    Gaut, J.R.3    Lawson, B.4    Freiden, P.J.5    Murti, K.G.6
  • 18
    • 0033521023 scopus 로고    scopus 로고
    • Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol
    • Hong, Y., Maeda, Y., Watanabe, R., Ohishi, K., Mishkind, M., Riezman, H. and Kinoshita, T. (1999). Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol. J. Biol. Chem. 274, 35099-35106.
    • (1999) J. Biol. Chem , vol.274 , pp. 35099-35106
    • Hong, Y.1    Maeda, Y.2    Watanabe, R.3    Ohishi, K.4    Mishkind, M.5    Riezman, H.6    Kinoshita, T.7
  • 19
    • 79957895829 scopus 로고    scopus 로고
    • Basement membrane sliding and targeted adhesion remodels tissue boundaries during uterine-vulval attachment in Caenorhabditis elegans
    • Ihara, S., Hagedorn, E. J., Morrissey, M. A., Chi, Q., Motegi, F., Kramer, J. M. and Sherwood, D. R. (2011). Basement membrane sliding and targeted adhesion remodels tissue boundaries during uterine-vulval attachment in Caenorhabditis elegans. Nat. Cell Biol. 13, 641-651.
    • (2011) Nat. Cell Biol , vol.13 , pp. 641-651
    • Ihara, S.1    Hagedorn, E.J.2    Morrissey, M.A.3    Chi, Q.4    Motegi, F.5    Kramer, J.M.6    Sherwood, D.R.7
  • 20
    • 30544454767 scopus 로고    scopus 로고
    • The role of the laminin beta subunit in laminin heterotrimer assembly and basement membrane function and development in C. elegans
    • Kao, G., Huang, C.-C., Hedgecock, E. M., Hall, D. H. and Wadsworth, W. G. (2006). The role of the laminin beta subunit in laminin heterotrimer assembly and basement membrane function and development in C. elegans. Dev. Biol. 290, 211-219.
    • (2006) Dev. Biol , vol.290 , pp. 211-219
    • Kao, G.1    Huang, C.-C.2    Hedgecock, E.M.3    Hall, D.H.4    Wadsworth, W.G.5
  • 21
    • 84955666376 scopus 로고    scopus 로고
    • A PIGN mutation responsible for multiple congenital anomalies-hypotonia-seizures syndrome 1 (MCAHS1) in an Israeli-Arab family
    • Khayat, M., Tilghman, J. M., Chervinsky, I., Zalman, L., Chakravarti, A. and Shalev, S. A. (2015). A PIGN mutation responsible for multiple congenital anomalies-hypotonia-seizures syndrome 1 (MCAHS1) in an Israeli-Arab family. Am. J. Med. Genet. A 170A, 176-182.
    • (2015) Am. J. Med. Genet. A , vol.170A , pp. 176-182
    • Khayat, M.1    Tilghman, J.M.2    Chervinsky, I.3    Zalman, L.4    Chakravarti, A.5    Shalev, S.A.6
  • 22
    • 55949115370 scopus 로고    scopus 로고
    • Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress
    • Kinoshita, T., Fujita, M. and Maeda, Y. (2008). Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress. J. Biochem. 144, 287-294.
    • (2008) J. Biochem , vol.144 , pp. 287-294
    • Kinoshita, T.1    Fujita, M.2    Maeda, Y.3
  • 23
    • 0028818537 scopus 로고
    • Identification and cloning of unc-119, a gene expressed in the Caenorhabditis elegans nervous system
    • Maduro, M. and Pilgrim, D. (1995). Identification and cloning of unc-119, a gene expressed in the Caenorhabditis elegans nervous system. Genetics 141, 977-988.
    • (1995) Genetics , vol.141 , pp. 977-988
    • Maduro, M.1    Pilgrim, D.2
  • 24
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T. and Helenius, A. (1992). Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117, 505-513.
    • (1992) J. Cell Biol , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 27
    • 0025942107 scopus 로고
    • Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences
    • Mello, C. C., Kramer, J. M., Stinchcomb, D. and Ambros, V. (1991). Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences. EMBO J. 10, 3959-3970.
    • (1991) EMBO J , vol.10 , pp. 3959-3970
    • Mello, C.C.1    Kramer, J.M.2    Stinchcomb, D.3    Ambros, V.4
  • 30
    • 0034705575 scopus 로고    scopus 로고
    • A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans
    • Nishiwaki, K., Hisamoto, N. and Matsumoto, K. (2000). A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans. Science 288, 2205-2208.
    • (2000) Science , vol.288 , pp. 2205-2208
    • Nishiwaki, K.1    Hisamoto, N.2    Matsumoto, K.3
  • 33
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao, R. V. and Bredesen, D. E. (2004). Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr. Opin. Cell Biol. 16, 653-662.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 34
    • 0036000025 scopus 로고    scopus 로고
    • Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons
    • Rolls, M. M., Hall, D. H., Victor, M., Stelzer, E. H. and Rapoport, T. A. (2002). Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons. Mol. Biol. Cell 13, 1778-1791.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1778-1791
    • Rolls, M.M.1    Hall, D.H.2    Victor, M.3    Stelzer, E.H.4    Rapoport, T.A.5
  • 35
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schröder, M. and Kaufman, R. J. (2005). The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 36
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development
    • Shen, X., Ellis, R. E., Lee, K., Liu, C.-Y., Yang, K., Solomon, A., Yoshida, H., Morimoto, R., Kurnit, D. M., Mori, K. et al. (2001). Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107, 893-903.
    • (2001) Cell , vol.107 , pp. 893-903
    • Shen, X.1    Ellis, R.E.2    Lee, K.3    Liu, C.-Y.4    Yang, K.5    Solomon, A.6    Yoshida, H.7    Morimoto, R.8    Kurnit, D.M.9    Mori, K.10
  • 37
    • 77957368304 scopus 로고    scopus 로고
    • The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging
    • Shibata, H., Inuzuka, T., Yoshida, H., Sugiura, H., Wada, I. and Maki, M. (2010). The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging. Biosci. Biotechnol. Biochem. 74, 1819-1826.
    • (2010) Biosci. Biotechnol. Biochem , vol.74 , pp. 1819-1826
    • Shibata, H.1    Inuzuka, T.2    Yoshida, H.3    Sugiura, H.4    Wada, I.5    Maki, M.6
  • 38
    • 0037119988 scopus 로고    scopus 로고
    • Sec16p potentiates the action of COPII proteins to bud transport vesicles
    • Supek, F., Madden, D. T., Hamamoto, S., Orci, L. and Schekman, R. (2002). Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029-1038.
    • (2002) J. Cell Biol , vol.158 , pp. 1029-1038
    • Supek, F.1    Madden, D.T.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 39
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I. and Ron, D. (2011). Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 13, 184-190.
    • (2011) Nat. Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 40
    • 0029092245 scopus 로고
    • Effect of ATP depletion and DTT on the transport of membrane proteins from the endoplasmic reticulum and the intermediate compartment to the Golgi complex
    • Verde, C., Pascale, M. C., Martire, G., Lotti, L. V., Torrisi, M. R., Helenius, A. and Bonatti, S. (1995). Effect of ATP depletion and DTT on the transport of membrane proteins from the endoplasmic reticulum and the intermediate compartment to the Golgi complex. Eur. J. Cell Biol. 67, 267-274.
    • (1995) Eur. J. Cell Biol , vol.67 , pp. 267-274
    • Verde, C.1    Pascale, M.C.2    Martire, G.3    Lotti, L.V.4    Torrisi, M.R.5    Helenius, A.6    Bonatti, S.7
  • 41
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter, P. and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 42
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L., Longo-Guess, C., Harris, B. S., Lee, J.-W. and Ackerman, S. L. (2005). Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37, 974-979.
    • (2005) Nat. Genet , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.-W.4    Ackerman, S.L.5
  • 43
    • 0041355317 scopus 로고    scopus 로고
    • ATP uptake in the Golgi and extracellular release require Mcd4 protein and the vacuolar H+-ATPase
    • Zhong, X., Malhotra, R. and Guidotti, G. (2003). ATP uptake in the Golgi and extracellular release require Mcd4 protein and the vacuolar H+-ATPase. J. Biol. Chem. 278, 33436-33444.
    • (2003) J. Biol. Chem , vol.278 , pp. 33436-33444
    • Zhong, X.1    Malhotra, R.2    Guidotti, G.3


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