01822nas a2200193   4500008004100000022001400041245006400055210006400119260000900183300001400192490000700206520118600213100002801399700003401427700001601461700002601477700003601503856008901539       2020                        eng d  a0006-296000aHDAC6 ZnF UBP as the modifier of tau structure and function0 aHDAC6 ZnF UBP as the modifier of tau structure and function  cDEC   a4546-45620 v593 a<p>Histone deacetylase 6 is a class H histone deacetylase primarily present in the cytoplasm and involved in the regulation of various cellular functions. It consists of two catalytic deacetylase domains and a unique zinc finger ubiquitin binding protein domain, which sets it apart from other HDACs. HDAC6 is known to regulate cellular activities by modifying the function of microtubules, HSP90, and cortactin through deacetylation. Apart from the catalytic activity of HDAC6, it interacts with other proteins through either the SE14 domain or the ZnF UBP domain to modulate their functions. Here, we have studied the role of the HDAC6 ZnF UBP domain as a modifier of Tau aggregation by its direct interaction with the polyproline region/repeat region of Tau. Interaction of HDAC6 ZnF UBP with Tau was found to reduce the propensity of Tau to self-aggregate and to disaggregate preformed aggregates in a concentration-dependent manner and also bring about the conformational changes in Tau protein. The interaction of HDAC6 ZnF UBP with Tau results in its degradation, suggesting either proteolytic activity of HDAC6 ZnF UBP or its role in enhancing autoproteolysis of Tau.</p>
1 aBalmik, Abhishek, Ankur1 aChidambaram, Hariharakrishnan1 aDangi, Abha1 aMarelli, Udaya, Kiran1 aChinnathambi, Subashchandrabose  uhttps://library.ncl.res.in/content/hdac6-znf-ubp-modifier-tau-structure-and-function