Proteomics

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SILAC APMS analysis of Pih1D2 interactome

ABSTRACT: To get insights into the function of Pih1D2 protein, we characterized its partners by performing a proteomic analysis in human cells. We fused this domain to GFP and stably expressed it in HeLa cells using site-specific integration with the Flp-In system. Following differential labeling of GFP-Pih1D2 and control cells with isotopically labelled amino-acids (SILAC), whole cell extracts were immuno-precipitated (IP) with anti-GFP antibodies and immunoprecipitates were subjected to quantitative mass-spectrometry analysis. SILAC labels: K0R0 control Hela H9 vs K4R6 x-FLAG- GFP- Pih1D2

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Franck Vandermoere  

LAB HEAD: Edouard Bertrand

PROVIDER: PXD009520 | Pride | 2018-06-10

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
CPS_human_SPTr_canonical_150114.fasta Fasta
PHAXRNASE_170301_1_E130314_B01.raw Raw
PHAXRNASE_170301_1_E130314_B02.raw Raw
PHAXRNASE_170301_1_E130314_B03.raw Raw
PHAXRNASE_170301_1_E130314_B04.raw Raw
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Publications

R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like  ...[more]

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