SIRT2 reduces actin polymerization and cell migration through deacetylation and degradation of HSP90

Publication date: September 2018Source: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1865, Issue 9Author(s): Jung Sun Min, Jin Chul Kim, Ji Ae Kim, Inho Kang, Jeong Keun AhnAbstractSIRT2, a member of the class III histone deacetylase family, has been identified as a tumor suppressor, which is associated with various cellular processes including metabolism and proliferation. However, the effects of SIRT2 on cancer cell migration caused by cytoskeletal rearrangement remain uncertain. Here we show that SIRT2 inhibits cell motility by suppressing actin polymerization. SIRT2 regulates actin dynamics through HSP90 destabilization and subsequent repression of LIM kinase (LIMK) 1/cofilin pathway. SIRT2 directly interacts with HSP90 and regulates its acetylation and ubiquitination. In addition, the deacetylase activity of SIRT2 is required for the regulation of actin polymerization and the ubiquitin-mediated proteasomal degradation of HSP90 induced by SIRT2.
Source: Biochimica et Biophysica Acta (BBA) Molecular Cell Research - Category: Molecular Biology Source Type: research