Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase.

Abstract:

:Protein kinases have central functions in various cellular signal transduction pathways through their substrate phosphorylation. Here we show that a protein kinase, DYRK2, has unexpected role as a scaffold for an E3 ubiquitin ligase complex. DYRK2 associates with an E3 ligase complex containing EDD, DDB1 and VPRBP proteins (EDVP complex). Strikingly, DYRK2 serves as a scaffold for the EDVP complex, because small-interfering-RNA-mediated depletion of DYRK2 disrupts the formation of the EDD-DDB1-VPRBP complex. Although the kinase activity of DYRK2 is dispensable for its ability to mediate EDVP complex formation, it is required for the phosphorylation and subsequent degradation of its downstream substrate, katanin p60. Collectively, our results reveal a new type of E3-ubiquitin ligase complex in humans that depends on a protein kinase for complex formation as well as for the subsequent phosphorylation, ubiquitylation and degradation of their substrates.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Maddika S,Chen J

doi

10.1038/ncb1848

subject

Has Abstract

pub_date

2009-04-01 00:00:00

pages

409-19

issue

4

eissn

1465-7392

issn

1476-4679

pii

ncb1848

journal_volume

11

pub_type

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