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Eric Rubenstein describes for SIIC the most significant aspects of his article describe para SIIC los aspectos relevantes de su artículo Role of the Hrd1 ubiquitin ligase in Endoplasmic Reticulum-Associated Degradation of translocon-associated proteins QUALITY CONTROL AT THE ENDOPLASMIC RETICULUM TRANSLOCON The essential Sec61 translocon brings proteins into and across the endoplasmic reticulum membrane. Little was known about how proteins blocking this channel are removed. New data reveal that the Hrd1 ubiquitin ligase degrades proteins that persistently and abnormally engage Sec61. This quality control pathway may also regulate low-density lipoprotein particle synthesis. The article was published by El artículo fue publicado por
Principal institution where the research took place Institución principal de la investigación Yale University, New Haven, Connecticut, United States  Authors' Report Crónica del Autor Bibliographic references Referencias bibliográficas Carvalho P, Goder V, Rapoport TA. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126(2):361-73, 2006. Hampton RY, Sommer T. Finding the will and the way of ERAD substrate retrotranslocation. Curr Opin Cell Biol 24(4):460-6, 2012. Hochstrasser M, Varshavsky A. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell 61(4):697-708, 1990. Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, Brodsky JL. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). J Biol Chem 282(45):32665-75, 2007. Johnson PR, Swanson R, Rakhilina L, Hochstrasser M. Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 94(2):217-27, 1998. Olzmann JA, Kopito RR, Christianson JC. The Mammalian Endoplasmic Reticulum-Associated Degradation System. Cold Spring Harbor perspectives in biology 2012 Dec 10. PubMed PMID: 23232094. Pariyarath R, Wang H, Aitchison JD, Ginsberg HN, Welch WJ, Johnson AE, et al. Co-translational interactions of apoprotein B with the ribosome and translocon during lipoprotein assembly or targeting to the proteasome. J Biol Chem 276(1):541-50, 2001. Ravid T, Kreft SG, Hochstrasser M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. Embo J 25(3):533-43, 2006. Rubenstein EM, Kreft SG, Greenblatt W, Swanson R, Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J Cell Biol 197(6):761-73, 2012. Zimmermann R, Eyrisch S, Ahmad M, Helms V. Protein translocation across the ER membrane. Biochim Biophys Acta 1808(3):912-24, 2011. Schafer A, Wolf DH. Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J 28(19):2874-84, 2009. Shao S, Hegde RS. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol 27:25-56, 2011. Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 15(20):2660-74, 2001. Thibault G, Ng DT. The endoplasmic reticulum-associated degradation pathways of budding yeast. Cold Spring Harbor perspectives in biology 4(12), 2012. Other articles written by the author Eric Rubenstein Otros artículos de Eric Rubenstein 1. Rubenstein EM, Kreft SG, Greenblatt W, Swanson R, Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J Cell Biol. 2012 Jun 11;197(6):761-73. PubMed PMID: 22689655. Pubmed Central PMCID: 3373407. Epub 2012/06/13. eng. 2. Rubenstein LD, Siegle D, Gubbins EJ, Bruce-Davis MN, J. G, Richardson SM, et al. Empowering underachieving high potential students for academic success Annual Meeting of the American Educational Research Association Vancouver, BC, CA2012. 3. Rubenstein EM, Hochstrasser M. Redundancy and variation in the ubiquitin-mediated proteolytic targeting of a transcription factor. Cell Cycle. 2010 Nov 1;9(21):4282-5. PubMed PMID: 20980825. Pubmed Central PMCID: PMC3055181. Epub 2010/10/29. eng. 4. Rubenstein EM, Schmidt MC. The glucose signal and metabolic p[H+]lux. EMBO J. 2010 Aug 4;29(15):2473-4. PubMed PMID: 20683466. Pubmed Central PMCID: 2928691. 5. Xie Y, Rubenstein EM, Matt T, Hochstrasser M. SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor. Genes Dev. 2010 Apr 13. PubMed PMID: 20388728. Epub 2010/04/15. Eng. 6. Rubenstein EM, McCartney RR, Zhang C, Shokat KM, Shirra MK, Arndt KM, et al. Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase. J Biol Chem. 2008 Jan 4;283(1):222-30. PubMed PMID: 17991748. 7. Rubenstein EM, Schmidt MC. Mechanisms regulating the protein kinases of Saccharomyces cerevisiae. Eukaryot Cell. 2007 Apr;6(4):571-83. PubMed PMID: 17337635. Pubmed Central PMCID: 1865659. 8. Elbing K, Rubenstein EM, McCartney RR, Schmidt MC. Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity. J Biol Chem. 2006 Sep 8;281(36):26170-80. PubMed PMID: 16847059. 9. Rubenstein EM, McCartney RR, Schmidt MC. Regulatory domains of Snf1-activating kinases determine pathway specificity. Eukaryot Cell. 2006 Apr;5(4):620-7. PubMed PMID: 16607009. Pubmed Central PMCID: 1459672. 10. McCartney RR, Rubenstein EM, Schmidt MC. Snf1 kinase complexes with different beta subunits display stress-dependent preferences for the three Snf1-activating kinases. Curr Genet. 2005 Jun;47(6):335-44. PubMed PMID: 15824893. SIIC System of Assisted Editing (SSEA) / Sistema SIIC de Edición Asistida (SSEA)
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Information about the full text Acerca del trabajo completo Aberrant Substrate Engagement of the ER Translocon Triggers Degradation by the Hrd1 Ubiquitin Ligase Author / Autor Eric Rubenstein1 1, Yale University, New Haven, EE.UU. Access to the original source The Journal of Cell Biology Article URL: / URL del artículo: http://www.jcb.org/ URL of Abstract: / URL del abstract: http://jcb.rupress.org/content/197/6/761 URL of Abstract page in Medline: / URL del abstract en Medline: http://www.ncbi.nlm.nih.gov/pubmed/22689655 siic DB: / siic DB: http://www.siicsalud.com/main/distriprinrel.php |
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