p(INTERPRO:"Heat shock protein Hsp90 family")

Entity

Name

Heat shock protein Hsp90 family

Namespace

interpro

Namespace Version

20181021

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/interpro-names.belns

Ganetespib treatment had a strong effect on most Hsp90- client interactions. Of the 630 unique proteins that we detected by LUMIER assay, 46% significantly decreased their interaction with Hsp90beta (change in LUMIER score > 1.5, adjusted p value <0.05; Figure 4A) PubMed:25036637

NUDC proteins have been found to associate with the Hsp90 complex, but the biological roles of these cochaperones are largely unknown (Zheng et al., 2011) PubMed:25036637

This study aimed to investigate the protective effects and mechanism of the novel HDAC6 inhibitor, MPT0G211, using an AD model. Our results indicated that MPT0G211 significantly reduced tau phosphorylation and aggregation, the processes highly correlated with the formation of NFTs. This HDAC6 inhibitory activity resulted in an increase in acetylated Hsp90, which decreased Hsp90 and HDAC6 binding, causing ubiquitination of phosphorylated tau proteins. In addition, a significant increase of phospho-glycogen synthase kinase-3β (phospho-GSK3β) on Ser9 (the inactive form) through Akt phosphorylation was associated with the inhibition of phospho-tau Ser396 in response to MPT0G211 treatment. PubMed:29844403

NUDC proteins have been found to associate with the Hsp90 complex, but the biological roles of these cochaperones are largely unknown (Zheng et al., 2011) PubMed:25036637

This study aimed to investigate the protective effects and mechanism of the novel HDAC6 inhibitor, MPT0G211, using an AD model. Our results indicated that MPT0G211 significantly reduced tau phosphorylation and aggregation, the processes highly correlated with the formation of NFTs. This HDAC6 inhibitory activity resulted in an increase in acetylated Hsp90, which decreased Hsp90 and HDAC6 binding, causing ubiquitination of phosphorylated tau proteins. In addition, a significant increase of phospho-glycogen synthase kinase-3β (phospho-GSK3β) on Ser9 (the inactive form) through Akt phosphorylation was associated with the inhibition of phospho-tau Ser396 in response to MPT0G211 treatment. PubMed:29844403