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• W1998023930 abstract "The intermediate filament protein synemin is present in astrocyte progenitors and glioblastoma cells but not in mature astrocytes. Here we demonstrate a role for synemin in enhancing glioblastoma cell proliferation and clonogenic survival, as synemin RNA interference decreased both behaviors by inducing G1 arrest along with Rb hypophosphorylation and increased protein levels of the G1/S inhibitors p21 Cip1 and p27 Kip1 . Akt involvement was demonstrated by decreased phosphorylation of its substrate, p21 Cip1 , and reduced Akt catalytic activity and phosphorylation at essential activation sites. Synemin silencing, however, did not affect the activities of PDPK1 and mTOR complex 2, which directly phosphorylate Akt activation sites, but instead enhanced the activity of the major regulator of Akt dephosphorylation, protein phosphatase type 2A (PP2A). This was accompanied by changes in PP2A subcellular distribution resulting in increased physical interactions between PP2A and Akt, as shown by proximity ligation assays (PLAs). PLAs and immunoprecipitation experiments further revealed that synemin and PP2A form a protein complex. In addition, treatment of synemin-silenced cells with the PP2A inhibitor cantharidic acid resulted in proliferation and pAkt and pRb levels similar to those of controls. Collectively these results indicate that synemin positively regulates glioblastoma cell proliferation by helping sequester PP2A away from Akt, thereby favoring Akt activation." @default.
• W1998023930 created "2016-06-24" @default.
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• W1998023930 date "2012-04-01" @default.
• W1998023930 modified "2023-10-16" @default.
• W1998023930 title "Synemin promotes AKT-dependent glioblastoma cell proliferation by antagonizing PP2A" @default.
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• W1998023930 doi "https://doi.org/10.1091/mbc.e11-08-0685" @default.
• W1998023930 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3315805" @default.
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