O-GlcNAcylation and phosphorylation of β-actin Ser¹⁹⁹ in diabetic nephropathy.

ABSTRACT: The function of actin is regulated by various posttranslational modifications. We have previously shown that in the kidneys of nonobese type 2 diabetes model Goto-Kakizaki rats, increased O-GlcNAcylation of β-actin protein is observed. It has also been reported that both O-GlcNAcylation and phosphorylation occur on Ser¹⁹⁹ of β-actin. However, their roles are not known. To elucidate their roles in diabetic nephropathy, we examined the rat kidney for changes in O-GlcNAcylation of Ser¹⁹⁹ (gS199)-actin and in the phosphorylation of Ser¹⁹⁹ (pS199)-actin. Both gS199- and pS199-actin molecules had an apparent molecular weight of 40 kDa and were localized as nonfilamentous actin in both the cytoplasm and nucleus. Compared with the normal kidney

SUBMITTER: Akimoto Y 

PROVIDER: S-EPMC6879942 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature