Abstract:
:Transactive response DNA-binding protein of 43 kDa (TDP-43) regulates RNA processing, including alternative splicing of tau exon 10. Pathological TDP-43 is hyperphosphorylated. However, how do the protein phosphatase(s) (PP) regulate TDP-43 phosphorylation is unclear. Here, we found that both PP1 and PP2A were coimmunoprecipitated with TDP-43. Treatment with calyculin A, but not with okadaic acid, increased TDP-43 phosphorylation at Ser379, Ser403/404, and Ser409/410 in cultured cells. PP1α, PP1β, and PP1γ interacted with TDP-43. Overexpression of PP1α and PP1γ, but not PP1β, suppressed TDP-43 phosphorylation at Ser403/404 and Ser409/410 and TDP-43-induced tau exon 10 inclusion. These findings suggest that PP1α and PP1γ regulate TDP-43 phosphorylation and its function in tau exon 10 inclusion mainly through its phosphorylation at Ser403/404 and Ser409/410.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gu J,Wang W,Miao S,Chen F,Wu F,Hu W,Iqbal K,Gong CX,Liu Fdoi
10.1002/1873-3468.12976subject
Has Abstractpub_date
2018-02-01 00:00:00pages
402-410issue
3eissn
0014-5793issn
1873-3468journal_volume
592pub_type
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