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Interactome analysis of DVL3 S/T cluster mutants using proximity labeling

ABSTRACT: When WNT binds to its receptor Frizzled (FZD) to activate the signalling, Dishevelled (DVL), the central component of Wnt signalling, is phosphorylated by redundant Casein kinase 1 (CK1) isoforms ε or δ, to transduce the signal downstream. Here, we mutated key serine/threonine residues in the intrinsically disordered region (IDR) between the PDZ and DEP domains. Either to alanine to prevent phosphorylation, or to glutamic acid to mimic phosphorylation, or we deleted these residues altogether. We investigated the impact of these mutations on DVL’s interactome using proximity labeling with TurboID-tagged fusion proteins at N-terminus of DVL.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Katerina Hanakova

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD067002 | Pride | 2026-04-07

REPOSITORIES: Pride

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Multisite phosphorylation of intrinsically disordered region of DVL

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