Proteomics

Dataset Information

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The interactome of the clathrin adaptor AP2 is modulated by the phosphorylation status of its µ2 subunit.


ABSTRACT: The clathrin adaptor AP2 is phosphorylated at a single site (Thr156) of its µ2 subunit. To gain insight how phosphorylation influences the interactome of AP2, we used human RPE cells which that were treated with LP-935509, an inhibitor of the adaptor-associated kinase AAK1. Kinase inhibition and loss of µ2 phosphorylation was verified with phospho-specific antibodies in westernblots of total cell extracts. We then used SILAC labelled cells and immune-isolated AP-2 and subjected bound proteins to mass spectrometry to identify all bound proteins and to determine phosphorylation-dependent changes in the interactome.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Retinal Pigment Epithelial Cell

SUBMITTER: Stefan Hoening  

LAB HEAD: Stefan Höning

PROVIDER: PXD013468 | Pride | 2019-11-12

REPOSITORIES: Pride

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Publications


Clathrin-mediated endocytosis (CME) is key to maintaining the transmembrane protein composition of cells' limiting membranes. During mammalian CME, a reversible phosphorylation event occurs on Thr156 of the μ2 subunit of the main endocytic clathrin adaptor, AP2. We show that this phosphorylation event starts during clathrin-coated pit (CCP) initiation and increases throughout CCP lifetime. μ2Thr156 phosphorylation favors a new, cargo-bound conformation of AP2 and simultaneously creates a binding  ...[more]

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