How viruses hijack the ERAD tuning machinery

Journal of Virology

Volumn 88, Issue 18, 2014, Pages 10272-10275

  Noack, Julia ^a   Bernasconi, Riccardo ^a   Molinari, Maurizio ^a,b  

^a INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Switzerland)

^b EPFL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN LC3; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

ARTICLE; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; MEMBRANE VESICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; QUALITY CONTROL; RNA STRUCTURE; VIRUS GENOME; VIRUS INFECTION; VIRUS MORPHOLOGY; VIRUS REPLICATION; ANIMAL; ENDOPLASMIC RETICULUM; GENETICS; HUMAN; METABOLISM; VIRAL PHENOMENA AND FUNCTIONS; VIROLOGY; VIRUS;

ANIMALS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; HUMANS; VIRUS DISEASES; VIRUS PHYSIOLOGICAL PHENOMENA; VIRUS REPLICATION; VIRUSES;

EID: 84906342535     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00801-14     Document Type: Article

References (20)

1. Brodsky JL. 2012. Cleaning up: ER-associated degradation to the rescue. Cell 151:1163-1167. http://dx.doi.org/10.1016/j.cell.2012.11.012.
2. Chambers JE, Petrova K, Tomba G, Vendruscolo M, Ron D. 2012. ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. J. Cell Biol. 198:371-385. http://dx.doi.org/10 .1083/jcb.201202005.
3. Bernasconi R, Galli C, Noack J, Bianchi S, de Haan CA, Reggiori F, Molinari M. 2012. Role of the SEL1L:LC3-I complex as an ERAD tuning receptor in the mammalian ER. Mol. Cell 46:809-819. http://dx.doi.org /10.1016/j.molcel.2012.04.017.
4. Bernasconi R, Galli C, Kokame K, Molinari M. 2013. Autoadaptive ER-associated degradation defines a preemptive unfolded protein response pathway. Mol. Cell 52:783-793. http://dx.doi.org/10.1016/j.molcel .2013.10.016.
5. Li GW, Burkhardt D, Gross C, Weissman JS. 2014. Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157:624-635. http://dx.doi.org/10.1016/j.cell.2014.02.033.
6. Cambridge SB, Gnad F, Nguyen C, Bermejo JL, Kruger M, Mann M. 2011. Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover. J. Proteome Res. 10:5275-5284. http: //dx.doi.org/10.1021/pr101183k.
7. Bernasconi R, Molinari M. 2011. ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr. Opin. Cell Biol. 23:176-183. http://dx.doi.org/10.1016/j.ceb.2010.10.002.
8. Horn SC, Hanna J, Hirsch C, Volkwein C, Schutz A, Heinemann U, Sommer T, Jarosch E. 2009. Usa1 functions as a scaffold of the HRDubiquitin ligase. Mol. Cell 36:782-793. http://dx.doi.org/10.1016/j.molcel .2009.10.015.
9. Hori O, Ichinoda F, Yamaguchi A, Tamatani T, Taniguchi M, Koyama Y, Katayama T, Tohyama M, Stern DM, Ozawa K, Kitao Y, Ogawa S. 2004. Role of Herp in the endoplasmic reticulum stress response. Genes Cells 9:457-469. http://dx.doi.org/10.1111/j.1356-9597.2004.00735.x.
10. Mizushima N. 2007. Autophagy: process and function. Genes Dev. 21: 2861-2873. http://dx.doi.org/10.1101/gad.1599207.
11. Cali T, Galli C, Olivari S, Molinari M. 2008. Segregation and rapid turnover ofEDEM1by an autophagy-like mechanism modulates standard ERAD and folding activities. Biochem. Biophys. Res. Commun. 371:405-410. http://dx.doi.org/10.1016/j.bbrc.2008.04.098.
12. Noack J, Bernasconi R, Molinari M. 2014. Non-lipidated LC3 is essential for mouse hepatitis virus infection, p 129-136. In Hayat MA (ed), Autophagy: cancer, other pathologies, inflammation, immunity, infection and aging, vol 2. Academic Press, Amsterdam, Netherlands.
13. Angelini MM, Neuman BW, Buchmeier MJ. 2014. Untangling membrane rearrangement in the nidovirales. DNA Cell Biol. 33:122-127. http: //dx.doi.org/10.1089/dna.2013.2304.
14. Reggiori F, Monastyrska I, Verheije MH, Cali T, Ulasli M, Bianchi S, Bernasconi R, de Haan CA, Molinari M. 2010. Coronaviruses hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication. Cell Host Microbe 7:500-508. http://dx .doi.org/10.1016/j.chom.2010.05.013.
15. Monastyrska I, Ulasli M, Rottier PJ, Guan JL, Reggiori F, de Haan CA. 2013. An autophagy-independent role for LC3 in equine arteritis virus replication. Autophagy 9:164-174. http://dx.doi.org/10.4161/auto.22743.
16. Sharma M, Bhattacharyya S, Nain M, Kaur M, Sood V, Gupta V, Khasa R, Abdin M, Vrati S, Kalia M. 2014. Japanese encephalitis virus replication is negatively regulated by autophagy and occurs on LC3-I- and EDEM1-containing membranes. Autophagy 10(9):53-54.
17. Hagemeijer MC, Monastyrska I, Griffith J, van der Sluijs P, Voortman J, van Bergen En Henegouwen PM, Vonk AM, Rottier PJM, Reggiori F, de Haan CA. 2014. Membrane rearrangements mediated by coronavirus nonstructural proteins 3 and 4. Virology 458-459:125-135. http://dx.doi .org/10.1016/j.virol.2014.04.027.
18. Aebi M, Bernasconi R, Clerc S, Molinari M. 2010. N-Glycan structures: recognition and processing in the ER. Trends Biochem. Sci. 35:74-82. http://dx.doi.org/10.1016/j.tibs.2009.10.001.
19. de Haan CA, Molinari M, Reggiori F. 2010. Autophagy-independent LC3 function in vesicular traffic. Autophagy 6:994-996. http://dx.doi.org /10.4161/auto.6.7.13309.
20. Lundin A, Dijkman R, Bergstrom T, Kann N, Adamiak B, Hannoun C, Kindler E, Jonsdottir HR, Muth D, Kint J, Forlenza M, Muller MA, Drosten C, Thiel V, Trybala E. 2014. Targeting membrane-bound viral RNA synthesis reveals potent inhibition of diverse coronaviruses including the middle East respiratory syndrome virus. PLoS Pathog. 10: e1004166. http://dx.doi.org/10.1371/journal.ppat.1004166.