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Multisite phosphorylation of intrinsically disordered region of Dishevelled

ABSTRACT: When WNT binds to its receptor Frizzled (FZD) to activate the signaling, Dishevelled (DVL), the central component of Wnt signaling, is phosphorylated by redundant Casein kinase 1 (CK1) isoforms ε or δ, to transduce the signal downstream. Although the basic principles of Wnt signal transduction are known, the mechanistic aspects of DVL phosphorylation remain elusive. Here we identify Wnt-dependent multisite phosphorylation of a large and conserved serine/threonine (S/T) cluster within intrinsically disordered region (IDR), located between the PDZ and DEP domains. The detailed analysis of the phosphorylation and its effect on the flanking domains was performed with the construct containing both domains PDZ and DEP flanking the IDR (hDVL3 PDZ-DEP, aa 243-496).

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Escherichia Coli

TISSUE(S): Cell Suspension Culture

SUBMITTER: Functional Proteomics Platform FPP

LAB HEAD: Cherine Bechara

PROVIDER: PXD063470 | Pride | 2026-04-07

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	211208_HDX_sample.zip	Other
	220210_PDZ.zip	Other
	Ion-Outputs.zip	Other
	PDZ-DEP.fasta	Fasta
	checksum.txt	Txt

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Multisite phosphorylation of intrinsically disordered region of DVL

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