Proteomics

Dataset Information

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Nuclear F-actin Assembly on Damaged Chromatin is Regulated By DYRK1A and Spir1 Phosphorylation


ABSTRACT: The uploaded data are described within "DYRK1A promotes nuclear F-actin assembly to effect DSB repair metabolism". Peptides from RPE1 epithelial cells with either, over expression of DYRK1A, normal expression of DYRK1A, or knockout of DYRK1A were labeled with TMTpro-16 reagents and phosphopeptides enriched by TiO2 and Fe-NTA resins.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Retinal Pigment Epithelium Cell Line, Epithelial Cell

SUBMITTER: Kirk West  

LAB HEAD: Justin Wai

PROVIDER: PXD031714 | Pride | 2024-07-19

REPOSITORIES: Pride

Dataset's files

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Publications

Nuclear F-actin assembly on damaged chromatin is regulated by DYRK1A and Spir1 phosphorylation.

Li Junshi J   Xiong Nan N   West Kirk L KL   Leung Manton M   Ching Yick Pang YP   Huang Jun J   Yuan Jian J   Yu Cheng-Han CH   Leung Justin J   Huen Michael M  

Nucleic acids research 20240801 15


Nuclear actin-based movements support DNA double-strand break (DSB) repair. However, molecular determinants that promote filamentous actin (F-actin) formation on the damaged chromatin remain undefined. Here we describe the DYRK1A kinase as a nuclear activity that promotes local F-actin assembly to support DSB mobility and repair, accomplished in part by its targeting of actin nucleator spire homolog 1 (Spir1). Indeed, perturbing DYRK1A-dependent phosphorylation of S482 mis-regulated Spir1 accumu  ...[more]

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