Show simple item record

dc.contributor.author Lee, JY
dc.contributor.author Yao, TP
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:21:59Z
dc.date.issued 2010-05
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20404488
dc.identifier 11812
dc.identifier.citation Autophagy, 2010, 6 (4), pp. 555 - 557
dc.identifier.uri http://hdl.handle.net/10161/3964
dc.description.abstract Autophagy has been predominantly studied as a nonselective self-digestion process that recycles macromolecules and produces energy in response to starvation. However, autophagy independent of nutrient status has long been known to exist. Recent evidence suggests that this form of autophagy enforces intracellular quality control by selectively disposing of aberrant protein aggregates and damaged organelles--common denominators in various forms of neurodegenerative diseases. By definition, this form of autophagy, termed quality-control (QC) autophagy, must be different from nutrient-regulated autophagy in substrate selectivity, regulation and function. We have recently identified the ubiquitin-binding deacetylase, HDAC6, as a key component that establishes QC. HDAC6 is not required for autophagy activation per se; rather, it is recruited to ubiquitinated autophagic substrates where it stimulates autophagosome-lysosome fusion by promoting F-actin remodeling in a cortactin-dependent manner. Remarkably, HDAC6 and cortactin are dispensable for starvation-induced autophagy. These findings reveal that autophagosomes associated with QC are molecularly and biochemically distinct from those associated with starvation autophagy, thereby providing a new molecular framework to understand the emerging complexity of autophagy and therapeutic potential of this unique machinery.
dc.format.extent 555 - 557
dc.language eng
dc.language.iso en_US en_US
dc.relation.ispartof Autophagy
dc.relation.isversionof 10.4161/auto.6.4.11812
dc.subject Actin Cytoskeleton
dc.subject Animals
dc.subject Autophagy
dc.subject Disease Models, Animal
dc.subject Histone Deacetylases
dc.subject Humans
dc.subject Lysosomes
dc.subject Mice
dc.subject Models, Biological
dc.subject Neuroprotective Agents
dc.subject Phagosomes
dc.subject Ubiquitin
dc.title Quality control autophagy: a joint effort of ubiquitin, protein deacetylase and actin cytoskeleton.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-5-16 en_US
duke.description.endpage 557 en_US
duke.description.issue 4 en_US
duke.description.startpage 555 en_US
duke.description.volume 6 en_US
dc.relation.journal Autophagy en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20404488
pubs.issue 4
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Pharmacology & Cancer Biology
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Radiation Oncology
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.publication-status Published
pubs.volume 6
dc.identifier.eissn 1554-8635

Files in this item

This item appears in the following Collection(s)

Show simple item record