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Research Article

Endoplasmic reticulum-associated degradation of a degron-containing polytopic membrane protein

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Pages 448-464 | Received 14 Jul 2009, Accepted 14 Sep 2009, Published online: 02 Nov 2009

References

  • Anelli T, Sitia R. 2008. Protein quality control in the early secretory pathway. EMBO J 27:315–327.
  • Hebert DN, Molinari M. 2007. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87:1377–1408.
  • Vembar SS, Brodsky JL. 2008. One step at a time: Endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9:944–957.
  • Lilley BN, Ploegh HL. 2005. Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 102:14296–14301.
  • Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA. 2005. Inaugural article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 102:14132–14138.
  • Scott DC, Schekman R. 2008. Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins. J Cell Biol 181:1095–1105.
  • Bonifacino JS, Cosson P, Shah N, Klausner RD. 1991. Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J 10:2783–2793.
  • Bonifacino JS, Suzuki CK, Klausner RD. 1990. A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science 247:79–82.
  • Fayadat L, Kopito RR. 2003. Recognition of a single transmembrane degron by sequential quality control checkpoints. Mol Biol Cell 14:1268–1278.
  • Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M. 2000. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739–745.
  • Adamus G, Zam ZS, Arendt A, Palczewski K, McDowell JH, Hargrave PA. 1991. Anti-rhodopsin monoclonal antibodies of defined specificity: Characterization and application. Vision Res 31:17–31.
  • Laird V, High S. 1997. Discrete cross-linking products identified during membrane protein biosynthesis. J Biol Chem 272:1983–1989.
  • Kikkert M, Doolman R, Dai M, Avner R, Hassink G, van Voorden S, Thanedar S, Roitelman J, Chau V, Wiertz E. 2004. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 279:3525–3534.
  • Cross BC, High S. 2009. Dissecting the physiological role of selective transmembrane-segment retention at the ER translocon. J Cell Sci 122:1768–1777.
  • Ismail N, Crawshaw SG, Cross BC, Haagsma AC, High S. 2008. Specific transmembrane segments are selectively delayed at the ER translocon during opsin biogenesis. Biochem J 411:495–506.
  • Wilson CM, Roebuck Q, High S. 2008. Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core. Proc Natl Acad Sci USA 105:9534–9539.
  • Fagioli C, Sitia R. 2001. Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits. J Biol Chem 276:12885–12892.
  • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP. 2008. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454:183–187.
  • Friedlander M, Blobel G. 1985. Bovine opsin has more than one signal sequence. Nature 318:338–343.
  • Kanner EM, Klein IK, Friedlander M, Simon SM. 2002. The amino terminus of opsin translocates ‘posttranslationally’ as efficiently as cotranslationally. Biochemistry 41:7707–7715.
  • Pool MR. 2005. Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol Membr Biol 22:3–15.
  • Hessa T, Meindl-Beinker NM, Bernsel A, Kim H, Sato Y, Lerch-Bader M, Nilsson I, White SH, von Heijne G. 2007. Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450:1026–1030.
  • Lundin C, Kim H, Nilsson I, White SH, 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 USA 105:15702–15707.
  • Abell BM, Pool MR, Schlenker O, Sinning I, High S. 2004. Signal recognition particle mediates post-translational targeting in eukaryotes. EMBO J 23:2755–2764.
  • Cross BC, Sinning I, Luirink J, High S. 2009. Delivering proteins for export from the cytosol. Nat Rev Mol Cell Biol 10:255–264.
  • Audigier Y, Friedlander M, Blobel G. 1987. Multiple topogenic sequences in bovine opsin. Proc Natl Acad Sci USA 84:5783–5787.
  • Lakkaraju AK, Mary C, Scherrer A, Johnson AE, Strub K. 2008. SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell 133:440–451.
  • Hessa T, Kim H, Bihlmaier K, Lundin C, Boekel J, Andersson H, Nilsson I, White SH, von Heijne G. 2005. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433:377–381.
  • Ismail N, Crawshaw SG, High S. 2006. Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon. J Cell Sci 119:2826–2836.
  • Kaushal S, Khorana HG. 1994. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33:6121–6128.
  • Kaushal S, Ridge KD, Khorana HG. 1994. Structure and function in rhodopsin: The role of asparagine-linked glycosylation. Proc Natl Acad Sci USA 91:4024–4028.
  • Saliba RS, Munro PM, Luthert PJ, Cheetham ME. 2002. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J Cell Sci 115:2907–2918.
  • Nagahama M, Suzuki M, Hamada Y, Hatsuzawa K, Tani K, Yamamoto A, Tagaya M. 2003. SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation. Mol Biol Cell 14:262–273.
  • Zuber C, Fan JY, Guhl B, Parodi A, Fessler JH, Parker C, Roth J. 2001. Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc Natl Acad Sci USA 98:10710–10715.
  • Appenzeller-Herzog C, Hauri HP. 2006. The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function. J Cell Sci 119:2173–2183.
  • Kornfeld R, Kornfeld S. 1985. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631–664.
  • Kota P, Reeves PJ, Rajbhandary UL, Khorana HG. 2006. Opsin is present as dimers in COS1 cells: Identification of amino acids at the dimeric interface. Proc Natl Acad Sci USA 103:3054–3059.
  • Lanctot PM, Leclerc PC, Escher E, Guillemette G, Leduc R. 2006. Role of N-glycan-dependent quality control in the cell-surface expression of the AT1 receptor. Biochem Biophys Res Commun 340:395–402.
  • Sato BK, Schulz D, Do PH, Hampton RY. 2009. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell 34:212–222.
  • Lass A, Kujawa M, McConnell E, Paton AW, Paton JC, Wojcik C. 2008. Decreased ER-associated degradation of alpha-TCR induced by Grp78 depletion with the SubAB cytotoxin. Int J Biochem Cell Biol 40:2865–2879.

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