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000289494 1001_ $$0P:(DE-He78)2514ea6c79ba09982b07649cbda6645b$$aLorenzo, Jose Paulo$$b0$$eFirst author$$udkfz
000289494 245__ $$aAPOBEC2 safeguards skeletal muscle cell fate through binding chromatin and regulating transcription of non-muscle genes during myoblast differentiation.
000289494 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2024
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000289494 520__ $$aThe apolipoprotein B messenger RNA editing enzyme, catalytic polypeptide (APOBEC) family is composed of nucleic acid editors with roles ranging from antibody diversification to RNA editing. APOBEC2, a member of this family with an evolutionarily conserved nucleic acid-binding cytidine deaminase domain, has neither an established substrate nor function. Using a cellular model of muscle differentiation where APOBEC2 is inducibly expressed, we confirmed that APOBEC2 does not have the attributed molecular functions of the APOBEC family, such as RNA editing, DNA demethylation, and DNA mutation. Instead, we found that during muscle differentiation APOBEC2 occupied a specific motif within promoter regions; its removal from those regions resulted in transcriptional changes. Mechanistically, these changes reflect the direct interaction of APOBEC2 with histone deacetylase (HDAC) transcriptional corepressor complexes. We also found that APOBEC2 could bind DNA directly, in a sequence-specific fashion, suggesting that it functions as a recruiter of HDAC to specific genes whose promoters it occupies. These genes are normally suppressed during muscle cell differentiation, and their suppression may contribute to the safeguarding of muscle cell fate. Altogether, our results reveal a unique role for APOBEC2 within the APOBEC family.
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000289494 650_7 $$2Other$$aAPOBEC family
000289494 650_7 $$2Other$$aDNA binding
000289494 650_7 $$2Other$$amuscle differentiation
000289494 650_7 $$2Other$$asafeguard factor
000289494 650_7 $$2Other$$atranscriptional regulator
000289494 650_7 $$2NLM Chemicals$$aChromatin
000289494 650_7 $$2NLM Chemicals$$aMuscle Proteins
000289494 650_7 $$0EC 3.5.4.5$$2NLM Chemicals$$aAPOBEC Deaminases
000289494 650_7 $$0EC 3.5.4.5$$2NLM Chemicals$$aCytidine Deaminase
000289494 650_7 $$2NLM Chemicals$$aRNA, Messenger
000289494 650_7 $$09007-49-2$$2NLM Chemicals$$aDNA
000289494 650_7 $$0EC 3.5.4.36$$2NLM Chemicals$$aAPOBEC-1 Deaminase
000289494 650_2 $$2MeSH$$aChromatin: genetics
000289494 650_2 $$2MeSH$$aMuscle Proteins: metabolism
000289494 650_2 $$2MeSH$$aAPOBEC Deaminases: genetics
000289494 650_2 $$2MeSH$$aCytidine Deaminase: metabolism
000289494 650_2 $$2MeSH$$aMuscle Fibers, Skeletal: metabolism
000289494 650_2 $$2MeSH$$aCell Differentiation: genetics
000289494 650_2 $$2MeSH$$aRNA, Messenger: genetics
000289494 650_2 $$2MeSH$$aMyoblasts: metabolism
000289494 650_2 $$2MeSH$$aDNA
000289494 650_2 $$2MeSH$$aAPOBEC-1 Deaminase: genetics
000289494 7001_ $$aMolla, Linda$$b1
000289494 7001_ $$0P:(DE-He78)1bbd2b961460d6dad83b63ac2004fd3b$$aAmro, Elias M. E.$$b2$$eFirst author$$udkfz
000289494 7001_ $$aIbarra, Ignacio L$$b3
000289494 7001_ $$0P:(DE-He78)987a16a93296d4a043a1b2337d224b53$$aRuf, Sandra$$b4$$udkfz
000289494 7001_ $$0P:(DE-He78)2a4b1dc59dce9461adf2a4e237efef7c$$aNeber, Cedrik$$b5$$udkfz
000289494 7001_ $$00009-0009-1640-3457$$aGkougkousis, Christos$$b6
000289494 7001_ $$aRidani, Jana$$b7
000289494 7001_ $$aSubramani, Poorani Ganesh$$b8
000289494 7001_ $$aBoulais, Jonathan$$b9
000289494 7001_ $$aHarjanto, Dewi$$b10
000289494 7001_ $$00000-0001-8044-9569$$aVonica, Alin$$b11
000289494 7001_ $$00000-0003-2896-0321$$aDi Noia, Javier M$$b12
000289494 7001_ $$00000-0001-9468-6311$$aDieterich, Christoph$$b13
000289494 7001_ $$aZaugg, Judith B$$b14
000289494 7001_ $$0P:(DE-He78)79dbda58d51b613a0a421f579d2dfed3$$aPapavasiliou, Fotini$$b15$$eLast author$$udkfz
000289494 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.2312330121$$gVol. 121, no. 17, p. e2312330121$$n17$$pe2312330121$$tProceedings of the National Academy of Sciences of the United States of America$$v121$$x0027-8424$$y2024
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