High impact information on WDR68

• In the present study, we purified the 3a-kinase from rabbit skeletal muscle and identified one constituent polypeptide as HAN11, a WD40 domain protein with unknown function [1].
• We showed that HAN11 binds the FH2 actin binding domain of mDia1 and confirmed that HAN11 also interacts with DYRK1A [2].
• We performed in situ hybridisation to compare expression of HAN11 with GLI1 and patched in mouse embryos [2].
• HAN11 is the human homologue of AN11, which controls flavonoid synthesis in plants [2].
• Wdr68 homologs appear to exist in all eukaryotic genomes [3].

Biological context of WDR68

• Notably, we found that the Drosophila wdr68 homolog CG14614 could substitute for the vertebrate wdr68 gene even though insects lack the NC cell lineage [3].

Anatomical context of WDR68

• AN11 was highly expressed in E10.5 mouse embryo limb buds, in an overlapping pattern with Ptc and GLI1 [2].
• Wdr68 interacts with two minibrain-related kinases, Dyrk1a and Dyrk1b, required for embryonic growth and myotube differentiation, respectively [3].
• We show that a GFP-Wdr68 fusion protein localizes to the nucleus with Dyrk1a in contrast to an engineered loss of function mutation Wdr68-T284F that no longer accumulated in the cell nucleus and failed to rescue wdr68 mutant animals [3].

Other interactions of WDR68

• GLI1-dependent transcription is positively regulated by DYRK1A, which is reported to bind HAN11 [2].

Analytical, diagnostic and therapeutic context of WDR68

• Cell fractionation experiments show that the bulk of the AN11 protein is localized in the cytoplasm [4].
• We used immunofluorescence microscopy to examine the subcellular distribution of HAN11, mDia1 and GLI1 [2].

References