High impact information on PRKD3

• Kinase-inactive forms of PKD1, PKD2 and PKD3 localize to the TGN in polarized and non-polarized cells [1].
• The nuclear import of protein kinase D3 requires its catalytic activity [2].
• We also found that activation loop phosphorylation of PKD3 did not require its nuclear localization, and it was not sufficient to promote the nuclear import of PKD3 [2].
• Real time imaging of a photoactivatable green fluorescent protein fused to PKD3 revealed that point mutations that render PKD3 catalytically inactive completely prevented its nuclear import despite its interaction with importin alpha and beta [2].
• We found that the C-terminal region of PKD3, which contains its catalytic domain, is necessary but not sufficient for its nuclear localization [2].

Biological context of PRKD3

• Most prominently, adenoviral gene expression of a dominant-negative PKD isoform, PKD3, primarily inhibits basal glucose uptake and, to a lesser extent, insulin-stimulated glucose uptake, whereas overexpression of wild-type PKD3 significantly enhances basal glucose uptake [3].

Anatomical context of PRKD3

• Cell stimulation with the GPCR agonist neurotensin induced a rapid and reversible plasma membrane translocation of PKD3 that is PKC-dependent [4].
• Protein kinase C-independent effects of protein kinase D3 in glucose transport in L6 myotubes [3].
• Taken together, our results indicate that PKD, specifically PKD3, directly contributes to insulin-independent basal glucose uptake in L6 skeletal muscle cells [3].

Associations of PRKD3 with chemical compounds

• Moreover, expression of a PKD3-targeted siRNA significantly inhibits basal glucose uptake [3].

Other interactions of PRKD3

• Protein kinase C nu/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G protein-coupled receptor agonists [4].

References