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Identification of human PKD2 interaction partners from Golgi-enriched protein fractions of HeLa cells by affinity enrichment cross-linking/MS

ABSTRACT: We investigated the interaction network of human PKD2 in the cytosol as well as in Golgi-enriched subcellular protein fractions, using an affinity enrichment strategy combined with chemical cross-linking/mass spectrometry (MS). Analysis of the subproteomes revealed the presence of distinct proteins in the cytosolic and Golgi fractions. The covalent fixation of transient or weak interactors by chemical cross-linking allowed capturing interaction partners that might otherwise vanish during conventional pull-down experiments. In total, 31 interaction partners were identified for PKD2.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Cervix Carcinoma

SUBMITTER: Björn Häupl

LAB HEAD: Andrea Sinz

PROVIDER: PXD003913 | Pride | 2016-09-27

REPOSITORIES: Pride

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Protein Interaction Network of Human Protein Kinase D2 Revealed by Chemical Cross-Linking/Mass Spectrometry.

Häupl Björn B Ihling Christian H CH Sinz Andrea A

Journal of proteome research 20160902 10

We investigated the interaction network of human PKD2 in the cytosol and in Golgi-enriched subcellular protein fractions by an affinity enrichment strategy combined with chemical cross-linking/mass spectrometry (MS). Analysis of the subproteomes revealed the presence of distinct proteins in the cytosolic and Golgi fractions. The covalent fixation of transient or weak interactors by chemical cross-linking allowed capturing interaction partners that might otherwise disappear during conventional pu ...[more]

PMID: 27559607

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Identification of human PKD2 interaction partners from cytosolic protein fractions of HeLa cells by affinity enrichment cross-linking/MS

Project description:We investigated the interaction network of human PKD2 in the cytosol as well as in Golgi-enriched subcellular protein fractions, using an affinity enrichment strategy combined with chemical cross-linking/mass spectrometry (MS). Analysis of the subproteomes revealed the presence of distinct proteins in the cytosolic and Golgi fractions. The covalent fixation of transient or weak interactors by chemical cross-linking allowed capturing interaction partners that might otherwise vanish during conventional pull-down experiments. In total, 31 interaction partners were identified for PKD2.

2016-09-27 | PXD003909 | Pride

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2023-03-10 | PXD036896 | Pride

Molecular characterization of a complex of Apoptosis Inducing Factor 1 (AIFM1) with cytochrome c oxidase of the mitochondrial respiratory chain

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2019-09-11 | PXD004596 | Pride

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2022-06-16 | PXD023817 | Pride

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2019-09-25 | GSE137945 | GEO

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