Inhibition of HDAC6 activity through interaction with RanBPM and its associated CTLH complex.

ABSTRACT:

Background

Histone deacetylase 6 (HDAC6) is a microtubule-associated deacetylase that promotes many cellular processes that lead to cell transformation and tumour development. We previously documented an interaction between Ran-Binding Protein M (RanBPM) and HDAC6 and found that RanBPM expression inhibits HDAC6 activity. RanBPM is part of a putative E3 ubiquitin ligase complex, termed the C-terminal to LisH (CTLH) complex. Here, we investigated the involvement of the CTLH complex on HDAC6 inhibition and assessed the outcome of this regulation on the cellular motility induced by HDAC6.

Methods

Cell lines (Hela, HEK293 and immortalized mouse embryonic fibroblasts) stably or transiently downregulated for several components of the CTLH complex were employed for the assays used i

SUBMITTER: Salemi LM 

PROVIDER: S-EPMC5494137 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature