Proteomics

Dataset Information

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Detection of IGF2BP1 phosphorylation in vitro and in vivo via Pro-Alanase treatment


ABSTRACT: In this project we aim to identify phosphorylation sites of IGF2BP1 that have not been discovered yet in mass spec experiments due to insufficient coverage. To this end we used Pro-Alanase treatment that produced detectable peptides in regions that are not covered by commonly used approaches. IGF2BP1 phosphorylation was investigated in vitro by treating purified IGF2BP1 with Src and in vivo by comparing immunoprecipitated IGF2BP1 from unstressed and stressed (1.5 h thapsigargin or 2 h or arsenite) HEK293T cells expressing GFP-labeled IGF2BP1.

INSTRUMENT(S): Orbitrap Exploris 480

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

TISSUE(S): Cell Culture

SUBMITTER: Markus Hartl  

LAB HEAD: Elif Karagöz

PROVIDER: PXD056497 | Pride | 2024-11-13

REPOSITORIES: pride

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Publications

IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism.

Hornegger Harald H   Anisimova Aleksandra S AS   Muratovic Adnan A   Bourgeois Benjamin B   Spinetti Elena E   Niedermoser Isabell I   Covino Roberto R   Madl Tobias T   Karagöz G Elif GE  

Nature communications 20241020 1


The insulin-like growth factor 2 mRNA binding protein 1 (IGF2BP1) is a conserved RNA-binding protein that regulates RNA stability, localization and translation. IGF2BP1 is part of various ribonucleoprotein (RNP) condensates. However, the mechanism that regulates its assembly into condensates remains unknown. By using proteomics, we demonstrate that phosphorylation of IGF2BP1 at S181 in a disordered linker is regulated in a stress-dependent manner. Phosphomimetic mutations in two disordered linke  ...[more]

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