Proteomics

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Pulldown of P180/RRBP1 interacting protein

ABSTRACT: P180/RRBP1 is an integral ER-resident protein known to be involved in mRNA binding and translation at the ER. We found that P180/RBBP1 is enriched in neuronal axons. To acquire more knowledge about its interactome and confirmation that P180/RRBP1 is interacting with ribosomes, we performed an unbiased screen of P180 interacting proteins by performing streptavidin pulldowns with GFP-biotin (GFPbio/AviTag)-tagged P180 and subsequent mass spectrometry analysis using HEK293T lysates and adult rat brain extracts. Co-transfection with a BirA construct ensures biotinylation ofP180 and allows subsequent streptavidin pulldown. A GFP-biotin/AviTag only construct was used as control conditionfor specificity.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human)

TISSUE(S): Brain, Cell Culture

SUBMITTER: Max Koppers  

LAB HEAD: Ginny G. Farias

PROVIDER: PXD050948 | Pride | 2024-10-14

REPOSITORIES: Pride

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20191022_OR14_Ag2_Stucc001_SA_Max_GFP.raw Raw
20191022_OR14_Ag2_Stucc001_SA_Max_GFP_brains.raw Raw
20191022_OR14_Ag2_Stucc001_SA_Max_P180.raw Raw
20191022_OR14_Ag2_Stucc001_SA_Max_P180_brains.raw Raw
Koppersetal_DataTable1.xlsx Xlsx
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Publications

Local mRNA translation in axons is critical for the spatiotemporal regulation of the axonal proteome. A wide variety of mRNAs are localized and translated in axons; however, how protein synthesis is regulated at specific subcellular sites in axons remains unclear. Here, we establish that the axonal endoplasmic reticulum (ER) supports axonal translation in developing rat hippocampal cultured neurons. Axonal ER tubule disruption impairs local translation and ribosome distribution. Using nanoscale  ...[more]

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