During Muscle Atrophy, Thick, but not Thin, Filament Components are Degraded by MuRF1-Dependent Ubiquitylation

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During Muscle Atrophy, Thick, but not Thin, Filament Components are Degraded by MuRF1-Dependent Ubiquitylation

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dc.contributor.author Brault, Jeffrey J.
dc.contributor.author Valenzuela, David M.
dc.contributor.author Gartner, Carlos
dc.contributor.author Latres, Esther
dc.contributor.author Cohen, Shenhav Orit
dc.contributor.author Gygi, Steven P.
dc.contributor.author Glass, David Jonathan
dc.contributor.author Goldberg, Alfred L.
dc.date.accessioned 2011-02-05T14:00:39Z
dc.date.issued 2009
dc.identifier.citation Cohen, Shenhav O., Jeffrey J. Brault, Steven P. Gygi, David J. Glass, David M. Valenzuela, Carlos Gartner, Esther Latres, and Alfred L. Goldberg. 2009. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. Journal of Cell Biology 185(6): 1083-1095. en_US
dc.identifier.issn 0021-9525 en_US
dc.identifier.uri http://nrs.harvard.edu/urn-3:HUL.InstRepos:4706108
dc.description.abstract Loss of myofibrillar proteins is a hallmark of atrophying muscle. Expression of muscle RING-finger 1 (MuRF1), a ubiquitin ligase, is markedly induced during atrophy, and MuRF1 deletion attenuates muscle wasting. We generated mice expressing a Ring-deletion mutant MuRF1, which binds but cannot ubiquitylate substrates. Mass spectrometry of the bound proteins in denervated muscle identified many myofibrillar components. Upon denervation or fasting, atrophying muscles show a loss of myosin-binding protein C (MyBP-C) and myosin light chains 1 and 2 (MyLC1 and MyLC2) from the myofibril, before any measurable decrease in myosin heavy chain (MyHC). Their selective loss requires MuRF1. MyHC is protected from ubiquitylation in myofibrils by associated proteins, but eventually undergoes MuRF1-dependent degradation. In contrast, MuRF1 ubiquitylates MyBP-C, MyLC1, and MyLC2, even in myofibrils. Because these proteins stabilize the thick filament, their selective ubiquitylation may facilitate thick filament disassembly. However, the thin filament components decreased by a mechanism not requiring MuRF1. en_US
dc.language.iso en_US en_US
dc.publisher Rockefeller University Press en_US
dc.relation.isversionof doi:10.1083/jcb.200901052 en_US
dc.relation.hasversion http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2711608/pdf/ en_US
dash.license LAA
dc.title During Muscle Atrophy, Thick, but not Thin, Filament Components are Degraded by MuRF1-Dependent Ubiquitylation en_US
dc.type Journal Article en_US
dc.description.version Version of Record en_US
dc.relation.journal Journal of Cell Biology en_US
dash.depositing.author Goldberg, Alfred L.
dc.date.available 2011-02-05T14:00:39Z
dash.affiliation.other HMS^Cell Biology en_US
dash.affiliation.other HMS^Cell Biology en_US

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