Proteomics

Dataset Information

0

Proteomic analysis of peroxisome-associated PEX5 mutants in Xenopus egg extract.


ABSTRACT: This project sought to identify the features in PEX5 required for interaction with the peroxisomal PEX2-PEX10-PEX12 ubiquitin ligase complex. Peroxisomes equilibrated with different PEX5 mutants (i.e., C11A, AH1, AH2) were purified from Xenopus egg extract, solubilized in digitonin, and PEX5-associated material was immunoprecipitated via a C-terminal FLAG tag. PEX5 without a FLAG tag was used as a negative control. PEX5-interacting peroxins were identified by LC-MS/MS at the Taplin Mass Spectrometry Facility at Harvard Medical School.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Xenopus Laevis (african Clawed Frog)

TISSUE(S): Egg

SUBMITTER: Michael Leszek Skowyra  

LAB HEAD: Tom Abraham Rapoport

PROVIDER: PXD035105 | Pride | 2022-08-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
94922.mzXML Mzxml
94923.mzXML Mzxml
94924.mzXML Mzxml
95370.mzXML Mzxml
95371.mzXML Mzxml
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Publications

PEX5 translocation into and out of peroxisomes drives matrix protein import.

Skowyra Michael L ML   Rapoport Tom A TA  

Molecular cell 20220804 17


Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases. Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which interacts with a docking complex in the peroxisomal membrane and then returns to the cytosol after monoubiquitination by a membrane-embedded ubiquitin ligase. The mechanism by which PEX5 shuttles between cytosol and peroxisomes and releases cargo inside the lumen is unclear. Here, we use Xenopus egg extract to demonstrate that PEX  ...[more]

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