<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(1)</volume><submitter>Szabo A</submitter><pubmed_abstract>The microtubule network exerts multifarious functions controlled by its decoration with various proteins and post-translational modifications. The disordered microtubule associated Tubulin Polymerization Promoting Protein (TPPP/p25) and the NAD&lt;sup>+&lt;/sup>-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte differentiation by acting as dominant factors in the organization of myelin proteome. Herein, we show that SIRT2 impedes the TPPP/p25-promoted microtubule assembly independently of NAD&lt;sup>+&lt;/sup>; however, the TPPP/p25-assembled tubulin ultrastructures were resistant against SIRT2 activity. TPPP/p25 counteracts the SIRT2-derived tubulin deacetylation producing enhanced microtubule acetylation. The inhibition of the SIRT2 deacetylase activity by TPPP/p25 is</pubmed_abstract><journal>Scientific reports</journal><pagination>17070</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5719079</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Modulation Of Microtubule Acetylation By The Interplay Of TPPP/p25, SIRT2 And New Anticancer Agents With Anti-SIRT2 Potency.</pubmed_title><pmcid>PMC5719079</pmcid><pubmed_authors>Olah J</pubmed_authors><pubmed_authors>Szunyogh S</pubmed_authors><pubmed_authors>Csaplar M</pubmed_authors><pubmed_authors>Szabo A</pubmed_authors><pubmed_authors>Lehotzky A</pubmed_authors><pubmed_authors>Low P</pubmed_authors><pubmed_authors>Ovadi J</pubmed_authors><pubmed_authors>Jung M</pubmed_authors><pubmed_authors>Szenasi T</pubmed_authors><pubmed_authors>Schiedel M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Modulation Of Microtubule Acetylation By The Interplay Of TPPP/p25, SIRT2 And New Anticancer Agents With Anti-SIRT2 Potency.</name><description>The microtubule network exerts multifarious functions controlled by its decoration with various proteins and post-translational modifications. The disordered microtubule associated Tubulin Polymerization Promoting Protein (TPPP/p25) and the NAD&lt;sup>+&lt;/sup>-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte differentiation by acting as dominant factors in the organization of myelin proteome. Herein, we show that SIRT2 impedes the TPPP/p25-promoted microtubule assembly independently of NAD&lt;sup>+&lt;/sup>; however, the TPPP/p25-assembled tubulin ultrastructures were resistant against SIRT2 activity. TPPP/p25 counteracts the SIRT2-derived tubulin deacetylation producing enhanced microtubule acetylation. The inhibition of the SIRT2 deacetylase activity by TPPP/p25 is</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Dec</publication><modification>2025-04-22T14:59:46.107Z</modification><creation>2019-03-27T03:04:06Z</creation></dates><accession>S-EPMC5719079</accession><cross_references><pubmed>29213065</pubmed><doi>10.1038/s41598-017-17381-3</doi></cross_references></HashMap>