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dc.contributor.authorShaw, Leslie M.
dc.date2022-08-11T08:10:06.000
dc.date.accessioned2022-08-23T16:55:26Z
dc.date.available2022-08-23T16:55:26Z
dc.date.issued2021-09-24
dc.date.submitted2022-06-02
dc.identifier.citation<p>Shaw LM. TBK1 has a new Akt. J Biol Chem. 2021 Oct;297(4):101244. doi: 10.1016/j.jbc.2021.101244. Epub 2021 Sep 24. PMID: 34563542; PMCID: PMC8498460. <a href="https://doi.org/10.1016/j.jbc.2021.101244">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9258 (Linking)
dc.identifier.doi10.1016/j.jbc.2021.101244
dc.identifier.pmid34563542
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42712
dc.description.abstractTANK-binding kinase 1 (TBK1) is a noncanonical IkappaB kinase that plays an essential role in the innate immune response to foreign pathogens. Recent studies have highlighted additional roles for TBK1 in the regulation of metabolism, although the mechanisms of this regulation have not been well characterized. In a recent issue, Tooley et al. demonstrated that TBK1-dependent activation of downstream kinase Akt is mediated via mechanistic target of rapamycin complex 2. This novel action of TBK1 reveals a key role for this kinase in the regulation of cellular metabolism and growth by diverse environmental inputs.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=34563542&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 2021 The Author. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.titleTBK1 has a new Akt
dc.typeResponse or Comment
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume297
dc.source.issue4
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=5991&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/4956
dc.identifier.contextkey29511289
refterms.dateFOA2022-08-23T16:55:26Z
html.description.abstract<p>TANK-binding kinase 1 (TBK1) is a noncanonical IkappaB kinase that plays an essential role in the innate immune response to foreign pathogens. Recent studies have highlighted additional roles for TBK1 in the regulation of metabolism, although the mechanisms of this regulation have not been well characterized. In a recent issue, Tooley et al. demonstrated that TBK1-dependent activation of downstream kinase Akt is mediated via mechanistic target of rapamycin complex 2. This novel action of TBK1 reveals a key role for this kinase in the regulation of cellular metabolism and growth by diverse environmental inputs.</p>
dc.identifier.submissionpathoapubs/4956
dc.contributor.departmentDepartment of Molecular, Cell and Cancer Biology
dc.source.pages101244


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Copyright © 2021 The Author. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's license is described as Copyright © 2021 The Author. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).