Mutational analysis of two residues in the DYRK homology box of the protein kinase DYRK1A.

ABSTRACT:

Objective

Dual specificity tyrosine phosphorylation-regulated kinases (DYRK) contain a characteristic sequence motif (DYRK homology box, DH box) that is located N-terminal of the catalytic domain and supports the autophosphorylation of a conserved tyrosine during maturation of the catalytic domain. Two missense mutations in the DH box of human DYRK1B were recently identified as causative of a rare familiar form of metabolic syndrome. We have recently shown that these amino acid exchanges impair maturation of the kinase domain. Here we report the characterization of DYRK1A point mutants (D138P, K150C) that correspond to the pathogenic DYRK1B variants (H90P, R102C).

Results

When expressed in HeLa cells, DYRK1A-D138P and K150C showed no significant difference from wild type DYR

SUBMITTER: Widowati EW 

PROVIDER: S-EPMC5952693 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature