메뉴 건너뛰기




Volumn 292, Issue 27, 2017, Pages 11349-11360

Refined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; EFFICIENCY; GLYCOSYLATION; HYDROPHOBICITY; MEMBRANES; PROTEINS; YEAST;

EID: 85023620149     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M117.779421     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 79959961077 scopus 로고    scopus 로고
    • Stepwise insertion and inversion of a type ii signal anchor sequence in the ribosome-sec61 translocon complex
    • Devaraneni, P. K., Conti, B., Matsumura, Y., Yang, Z., Johnson, A. E., and Skach, W. R. (2011) Stepwise insertion and inversion of a type II signal anchor sequence in the ribosome-Sec61 translocon complex. Cell 146, 134 –147
    • (2011) Cell , vol.146 , pp. 134-147
    • Devaraneni, P.K.1    Conti, B.2    Matsumura, Y.3    Yang, Z.4    Johnson, A.E.5    Skach, W.R.6
  • 2
    • 84946032322 scopus 로고    scopus 로고
    • Marginally hydrophobic transmembrane -helices shaping membrane protein folding
    • De Marothy, M. T., and Elofsson, A. (2015) Marginally hydrophobic transmembrane -helices shaping membrane protein folding. Protein Sci. 24, 1057–1074
    • (2015) Protein Sci , vol.24 , pp. 1057-1074
    • De Marothy, M.T.1    Elofsson, A.2
  • 3
    • 61949084073 scopus 로고    scopus 로고
    • Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum sec61 translocon
    • Pitonzo, D., Yang, Z., Matsumura, Y., Johnson, A. E., and Skach, W. R. (2009) Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon. Mol. Biol. Cell 20, 685– 698
    • (2009) Mol. Biol. Cell , vol.20 , pp. 685-698
    • Pitonzo, D.1    Yang, Z.2    Matsumura, Y.3    Johnson, A.E.4    Skach, W.R.5
  • 4
    • 80053610657 scopus 로고    scopus 로고
    • Membrane protein integration into the endoplasmic reticulum
    • Martínez-Gil, L., Saurí, A., Marti-Renom, M. A., and Mingarro, I. (2011) Membrane protein integration into the endoplasmic reticulum. FEBS J. 278, 3846 –3858
    • (2011) FEBS J. , vol.278 , pp. 3846-3858
    • Martínez-Gil, L.1    Saurí, A.2    Marti-Renom, M.A.3    Mingarro, I.4
  • 5
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao, S., and Hegde, R. S. (2011) Membrane protein insertion at the endoplasmic reticulum. Annu. Rev. Cell Dev. Biol. 27, 25–56
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 6
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of sec61/secy-mediated protein translocation across membranes
    • Park, E., and Rapoport, T. A. (2012) Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu. Rev. Biophys. 41, 21– 40
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 7
    • 84864310033 scopus 로고    scopus 로고
    • Understanding integration of -helical membrane proteins: The next steps
    • Gilmore, R., and Mandon, E. C. (2012) Understanding integration of -helical membrane proteins: the next steps. Trends Biochem. Sci. 37, 303–308
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 303-308
    • Gilmore, R.1    Mandon, E.C.2
  • 8
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D. J., and Gilmore, R. (2006) An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16, 47R– 62R
    • (2006) Glycobiology , vol.16 , pp. 47R-62R
    • Kelleher, D.J.1    Gilmore, R.2
  • 9
    • 0038294237 scopus 로고    scopus 로고
    • Oligo-saccharyltransferase isoforms that contain different catalytic stt3 subunits have distinct enzymatic properties
    • Kelleher, D. J., Karaoglu, D., Mandon, E. C., and Gilmore, R. (2003) Oligo-saccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol. Cell 12, 101–111
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 11
    • 0028834273 scopus 로고
    • Stt3, a highly conserved protein required for yeast oligosaccharyltransferase activity in vivo
    • Zufferey, R., Knauer, R., Burda, P., Stagljar, I., te Heesen, S., Lehle, L., and Aebi, M. (1995) STT3, a highly conserved protein required for yeast oligosaccharyltransferase activity in vivo. EMBO J. 14, 4949 – 4960
    • (1995) EMBO J. , vol.14 , pp. 4949-4960
    • Zufferey, R.1    Knauer, R.2    Burda, P.3    Stagljar, I.4    Te Heesen, S.5    Lehle, L.6    Aebi, M.7
  • 12
    • 0026503855 scopus 로고
    • Characterization of a staurosporine- and temperature-sensitive mutant, stt1, of saccharomyces cerevisiae: Stt1 is allelic to pkc1
    • Yoshida, S., Ikeda, E., Uno, I., and Mitsuzawa, H. (1992) Characterization of a staurosporine- and temperature-sensitive mutant, stt1, of Saccharomyces cerevisiae: STT1 is allelic to PKC1. Mol. Gen. Genet. 231, 337–344
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 337-344
    • Yoshida, S.1    Ikeda, E.2    Uno, I.3    Mitsuzawa, H.4
  • 13
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak, C., Gerber, S., Numao, S., Aebi, M., and Locher, K. P. (2011) X-ray structure of a bacterial oligosaccharyltransferase. Nature 474, 350 –355
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 14
    • 79953892814 scopus 로고    scopus 로고
    • Selective control of oligosaccharide transfer efficiency for the n-glycosylation sequon by a point mutation in oligosaccharyltransferase
    • Igura, M., and Kohda, D. (2011) Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase. J. Biol. Chem. 286, 13255–13260
    • (2011) J. Biol. Chem. , vol.286 , pp. 13255-13260
    • Igura, M.1    Kohda, D.2
  • 15
    • 80052254267 scopus 로고    scopus 로고
    • Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound n-linked oligosac-charyltransferases
    • Jaffee, M. B., and Imperiali, B. (2011) Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosac-charyltransferases. Biochemistry 50, 7557–7567
    • (2011) Biochemistry , vol.50 , pp. 7557-7567
    • Jaffee, M.B.1    Imperiali, B.2
  • 17
    • 84962877719 scopus 로고    scopus 로고
    • N-linked glycosylation and homeostasis of the endoplasmic reticulum
    • Cherepanova, N., Shrimal, S., and Gilmore, R. (2016) N-linked glycosylation and homeostasis of the endoplasmic reticulum. Curr. Opin. Cell Biol. 41, 57– 65
    • (2016) Curr. Opin. Cell Biol. , vol.41 , pp. 57-65
    • Cherepanova, N.1    Shrimal, S.2    Gilmore, R.3
  • 18
    • 84959259856 scopus 로고    scopus 로고
    • Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine-linked glycosylation
    • Cherepanova, N. A., and Gilmore, R. (2016) Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine-linked glycosylation. Sci. Rep. 6, 20946
    • (2016) Sci. Rep. , vol.6 , pp. 20946
    • Cherepanova, N.A.1    Gilmore, R.2
  • 19
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of n-linked glycosylation
    • Burda, P., and Aebi, M. (1999) The Dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426, 239 –257
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 20
    • 20144378272 scopus 로고    scopus 로고
    • Membrane topology of the stt3 subunit of the oligosaccharyltransferase complex
    • Kim, H., von Heijne, G., and Nilsson, I. (2005) Membrane topology of the STT3 subunit of the oligosaccharyltransferase complex. J. Biol. Chem. 280, 20261–20267
    • (2005) J. Biol. Chem. , vol.280 , pp. 20261-20267
    • Kim, H.1    Von Heijne, G.2    Nilsson, I.3
  • 23
    • 57349168025 scopus 로고    scopus 로고
    • Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for n(in)-c(out) and n(out)-c(in) transmembrane helices
    • Lundin, C., Kim, H., Nilsson, I., White, S. H., and von Heijne, G. (2008) Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices. Proc. Natl. Acad. Sci. U.S.A. 105, 15702–15707
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15702-15707
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.H.4    Von Heijne, G.5
  • 24
    • 84857439394 scopus 로고    scopus 로고
    • Orien-tational preferences of neighboring helices can drive er insertion of a marginally hydrophobic transmembrane helix
    • Ojemalm, K., Halling, K. K., Nilsson, I., and von Heijne, G. (2012) Orien-tational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix. Mol. Cell 45, 529 –540
    • (2012) Mol. Cell , vol.45 , pp. 529-540
    • Ojemalm, K.1    Halling, K.K.2    Nilsson, I.3    Von Heijne, G.4
  • 25
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in escherichia coli than in mammalian microsomes
    • Johansson, M., Nilsson, I., and von Heijne, G. (1993) Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. 239, 251–256
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    Von Heijne, G.3
  • 26
    • 0037051897 scopus 로고    scopus 로고
    • Cleavage of a tail-anchored protein by signal peptidase
    • Nilsson, I., Johnson, A. E., and von Heijne, G. (2002) Cleavage of a tail-anchored protein by signal peptidase. FEBS Lett. 516, 106 –108
    • (2002) FEBS Lett. , vol.516 , pp. 106-108
    • Nilsson, I.1    Johnson, A.E.2    Von Heijne, G.3
  • 27
    • 0033950717 scopus 로고    scopus 로고
    • Characterization of the n-oligosaccharides attached to the atypical asn-x-cys sequence of recombinant human epidermal growth factor receptor
    • Sato, C., Kim, J. H., Abe, Y., Saito, K., Yokoyama, S., and Kohda, D. (2000) Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J. Biochem. 127, 65–72
    • (2000) J. Biochem. , vol.127 , pp. 65-72
    • Sato, C.1    Kim, J.H.2    Abe, Y.3    Saito, K.4    Yokoyama, S.5    Kohda, D.6
  • 29
    • 66249114347 scopus 로고    scopus 로고
    • N-glycosylation microheterogeneity and site occupancy of an asn-x-cys sequon in plasma-derived and recombinant protein C
    • Gil, G. C., Velander, W. H., and Van Cott, K. E. (2009) N-Glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Proteomics 9, 2555–2567
    • (2009) Proteomics , vol.9 , pp. 2555-2567
    • Gil, G.C.1    Velander, W.H.2    Van Cott, K.E.3
  • 30
    • 0025297484 scopus 로고
    • Beta protein c is not glycosylated at asparagine 329: The rate of translation may influence the frequency of usage at asparagine-x-cysteine sites
    • Miletich, J. P., and Broze, G. J., Jr. (1990) Beta protein C is not glycosylated at asparagine 329: the rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J. Biol. Chem. 265, 11397–11404
    • (1990) J. Biol. Chem. , vol.265 , pp. 11397-11404
    • Miletich, J.P.1    Broze, G.J.2
  • 31
    • 84933564227 scopus 로고    scopus 로고
    • The atypical n-glycosylation motif, asn-cys-cys, in human gpr109a is required for normal cell surface expression and intracellular signaling
    • Yasuda, D., Imura, Y., Ishii, S., Shimizu, T., and Nakamura, M. (2015) The atypical N-glycosylation motif, Asn-Cys-Cys, in human GPR109A is required for normal cell surface expression and intracellular signaling. FASEB J. 29, 2412–2422
    • (2015) FASEB J , vol.29 , pp. 2412-2422
    • Yasuda, D.1    Imura, Y.2    Ishii, S.3    Shimizu, T.4    Nakamura, M.5
  • 32
    • 60849083215 scopus 로고    scopus 로고
    • Analysis of transmembrane helix integration in the endoplasmic reticulum in s. Cerevisiae
    • Hessa, T., Reithinger, J. H., von Heijne, G., and Kim, H. (2009) Analysis of transmembrane helix integration in the endoplasmic reticulum in S. cerevisiae. J. Mol. Biol. 386, 1222–1228
    • (2009) J. Mol. Biol. , vol.386 , pp. 1222-1228
    • Hessa, T.1    Reithinger, J.H.2    Von Heijne, G.3    Kim, H.4
  • 33
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I. M., and von Heijne, G. (1993) Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268, 5798 –5801
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 36
    • 17744395499 scopus 로고    scopus 로고
    • Biogenesis of cftr and other poly-topic membrane proteins: New roles for the ribosome-translocon complex
    • Sadlish, H., and Skach, W. R. (2004) Biogenesis of CFTR and other poly-topic membrane proteins: new roles for the ribosome-translocon complex. J. Membr. Biol. 202, 115–126
    • (2004) J. Membr. Biol. , vol.202 , pp. 115-126
    • Sadlish, H.1    Skach, W.R.2
  • 37
    • 84959572680 scopus 로고    scopus 로고
    • Membrane insertion and topology of the amino-terminal domain tmd0 of multidrug-resistance associated protein 6 (mrp6)
    • Cuviello, F., Tellgren-Roth, Å., Lara, P., Ruud Selin, F., Monné, M., Bisaccia, F., Nilsson, I., and Ostuni, A. (2015) Membrane insertion and topology of the amino-terminal domain TMD0 of multidrug-resistance associated protein 6 (MRP6). FEBS Lett. 589, 3921–3928
    • (2015) FEBS Lett. , vol.589 , pp. 3921-3928
    • Cuviello, F.1    Tellgren-Roth, Å.2    Lara, P.3    Ruud Selin, F.4    Monné, M.5    Bisaccia, F.6    Nilsson, I.7    Ostuni, A.8
  • 38
    • 84899823053 scopus 로고    scopus 로고
    • Changed membrane integration and catalytic site conformation are two mechanisms behind the increased A42/a40 ratio by presenilin 1 familial alzheimer-linked mutations
    • Wanngren, J., Lara, P., Ojemalm, K., Maioli, S., Moradi, N., Chen, L., Tjernberg, L. O., Lundkvist, J., Nilsson, I., and Karlström, H. (2014) Changed membrane integration and catalytic site conformation are two mechanisms behind the increased A42/A40 ratio by presenilin 1 familial Alzheimer-linked mutations. FEBS Open Bio. 4, 393– 406
    • (2014) FEBS Open Bio , vol.4 , pp. 393-406
    • Wanngren, J.1    Lara, P.2    Ojemalm, K.3    Maioli, S.4    Moradi, N.5    Chen, L.6    Tjernberg, L.O.7    Lundkvist, J.8    Nilsson, I.9    Karlström, H.10
  • 40
    • 0036795563 scopus 로고    scopus 로고
    • Molecular mechanism of p-glycoprotein assembly into cellular membranes
    • Anthony, V., and Skach, W. R. (2002) Molecular mechanism of P-glycoprotein assembly into cellular membranes. Curr. Protein Pept. Sci. 3, 485–501
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 485-501
    • Anthony, V.1    Skach, W.R.2
  • 41
    • 33748602095 scopus 로고    scopus 로고
    • Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum sec61 translocon
    • Pitonzo, D., and Skach, W. R. (2006) Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum Sec61 translocon. Biochim. Biophys. Acta 1758, 976 –988
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 976-988
    • Pitonzo, D.1    Skach, W.R.2
  • 42
    • 0037039368 scopus 로고    scopus 로고
    • Integration of shaker-type k channel, kat1, into the endoplasmic reticulum membrane: Synergistic insertion of voltage-sensing segments, s3-s4, and independent insertion of pore-forming segments, s5-p-s6
    • Sato, Y., Sakaguchi, M., Goshima, S., Nakamura, T., and Uozumi, N. (2002) Integration of Shaker-type K channel, KAT1, into the endoplasmic reticulum membrane: synergistic insertion of voltage-sensing segments, S3-S4, and independent insertion of pore-forming segments, S5-P-S6. Proc. Natl. Acad. Sci. U.S.A. 99, 60 – 65
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 60-65
    • Sato, Y.1    Sakaguchi, M.2    Goshima, S.3    Nakamura, T.4    Uozumi, N.5
  • 43
    • 0030024638 scopus 로고    scopus 로고
    • Molecular cloning of a highly conserved mouse and human integral membrane protein (itm1) and genetic mapping to mouse chromosome 9
    • Hong, G., Deleersnijder, W., Kozak, C. A., Van Marck, E., Tylzanowski, P., and Merregaert, J. (1996) Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9. Genomics 31, 295–300
    • (1996) Genomics , vol.31 , pp. 295-300
    • Hong, G.1    Deleersnijder, W.2    Kozak, C.A.3    Van Marck, E.4    Tylzanowski, P.5    Merregaert, J.6
  • 44
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P., and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84 –93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 45
    • 0035463587 scopus 로고    scopus 로고
    • Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum
    • Wilkinson, B. M., Tyson, J. R., and Stirling, C. J. (2001) Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum. Dev. Cell 1, 401– 409
    • (2001) Dev. Cell , vol.1 , pp. 401-409
    • Wilkinson, B.M.1    Tyson, J.R.2    Stirling, C.J.3
  • 46
    • 84880071444 scopus 로고    scopus 로고
    • Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (er)
    • Reithinger, J. H., Kim, J. E., and Kim, H. (2013) Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER). J. Biol. Chem. 288, 18058–18067
    • (2013) J. Biol. Chem. , vol.288 , pp. 18058-18067
    • Reithinger, J.H.1    Kim, J.E.2    Kim, H.3
  • 48
    • 84874597747 scopus 로고    scopus 로고
    • Alignment of helical membrane protein sequences using alignme
    • Stamm, M., Staritzbichler, R., Khafizov, K., and Forrest, L. R. (2013) Alignment of helical membrane protein sequences using AlignMe. PLoS ONE 8, e57731
    • (2013) Plos ONE , vol.8
    • Stamm, M.1    Staritzbichler, R.2    Khafizov, K.3    Forrest, L.R.4
  • 49
    • 78650397484 scopus 로고    scopus 로고
    • A study of the evolution of inverted-topology repeats from leut-fold transporters using alignme
    • Khafizov, K., Staritzbichler, R., Stamm, M., and Forrest, L. R. (2010) A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe. Biochemistry 49, 10702–10713
    • (2010) Biochemistry , vol.49 , pp. 10702-10713
    • Khafizov, K.1    Staritzbichler, R.2    Stamm, M.3    Forrest, L.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.