IndraLab

Statements

DYRK2 phosphorylates USP28. 6 / 6
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"Since DYRK2 can regulate the accumulation of one of its substrates through both its kinase and scaffolding function [ xref ], we could not rule out USP28 phosphorylation by DYRK2."
40858801
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"DYRK2 phosphorylates USP28, promoting its ubiquitination and proteasomal degradation."
40858801
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"We demonstrate that DYRK2 phosphorylates USP28, promoting its ubiquitination and proteasomal degradation in a kinase activity-independent manner, thereby contributing to the maintenance of oncogenic protein homeostasis."
40858801
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"In summary, DYRK2 phosphorylates USP28 at several residues increasing its interaction affinity but promotes its degradation via a kinase activity-independent mechanism."
40858801
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"Our findings demonstrate that DYRK2 phosphorylates USP28, leading to its ubiquitination and proteasomal degradation, while USP28 acts stabilizing DYRK2 protein levels and kinase activity by its deubiquitination."
40858801
sparser
"DYRK2 phosphorylates USP28 promoting its degradation through a kinase activity-independent mechanism."
40858801