The activity of glyoxylase 1 is regulated by glucose-responsive phosphorylation on Tyr136.

ABSTRACT:

Objective

Methylglyoxal (MG) is a highly reactive α-oxoaldehyde that glycates proteins. MG has been linked to the development of diabetic complications: MG is the major precursor of advanced glycation end products (AGEs), a risk marker for diabetic complications in humans. Furthermore, flies and fish with elevated MG develop insulin resistance, obesity, and hyperglycemia. MG is detoxified in large part through the glyoxalase system, whose rate-limiting enzyme is glyoxalase I (Glo1). Hence, we aimed to study how Glo1 activity is regulated.

Methods

We studied the regulation and effect of post-translational modifications of Glo1 in tissue culture and in mouse models of diabetes.

Results

We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multipl

SUBMITTER: Cortizo FG 

PROVIDER: S-EPMC8715127 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature