Dataset Information

Identifying dynamic protein and RNA proximity interaction networks of actinin reveals RNA-binding and metabolic regulatory mechanisms

ABSTRACT: We deployed proximity-dependent biotinylation to identify actinin proximity proteins and RNA transcripts in human cardiomyocytes to reveal new functions of the actin cytoskeleton. We identified 285 proximity protein partners including unexpected effectors of RNA-binding and metabolism, and interrogated dynamic partners using a sarcomere assembly model.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Feria Ladha

LAB HEAD: J. Travis Hinson

PROVIDER: PXD018040 | Pride | 2022-02-15

REPOSITORIES: Pride

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Publications

Actinin BioID reveals sarcomere crosstalk with oxidative metabolism through interactions with IGF2BP2.

Ladha Feria A FA Thakar Ketan K Pettinato Anthony M AM Legere Nicholas N Ghahremani Shahnaz S Cohn Rachel R Romano Robert R Meredith Emily E Chen Yu-Sheng YS Hinson J Travis JT

Cell reports 20210801 6

Actinins are strain-sensing actin cross-linkers that are ubiquitously expressed and harbor mutations in human diseases. We utilize CRISPR, pluripotent stem cells, and BioID to study actinin interactomes in human cardiomyocytes. We identify 324 actinin proximity partners, including those that are dependent on sarcomere assembly. We confirm 19 known interactors and identify a network of RNA-binding proteins, including those with RNA localization functions. In vivo and biochemical interaction studi ...[more]

PMID: 34380038

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