Biotinylation-based proximity labelling proteomics: basics, applications and technical considerations.

Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Internet ISSN: 1756-2651 (Electronic) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE

Publication: : Abingdon, UK : Oxford University Press
Original Publication: Tokyo : Japanese Biochemical Society

Proteome/*metabolism ; Proteomics/*methods; Animals ; Biotinylation ; Humans ; Mass Spectrometry/methods ; Organelles/metabolism ; Protein Binding ; Protein Interaction Maps ; Proteome/analysis ; Secretome

Recent advances in biotinylation-based proximity labelling (PL) have opened up new avenues for mapping the protein composition of cellular compartments and protein complexes in living cells at high spatiotemporal resolution. In particular, PL combined with mass spectrometry-based proteomics has been successfully applied to defining protein-protein interactions, protein-nucleic acid interactions, (membraneless) organelle proteomes and secretomes in various systems ranging from cultured cells to whole animals. In this review, we first summarize the basics and recent biological applications of PL proteomics and then highlight recent developments in enrichment techniques for biotinylated proteins and peptides, focusing on the advantages of PL and technical considerations.
(© The Author(s) 2021. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.)

Takeda Science Foundation; 18070870 JST Strategic Basic Research Program CREST; JST ERATO; JPMJPR18H2 JST PRESTO; 21J15068 JSPS Grants-in-Aid for Scientific Research

Keywords: affinity purification; biotinylation protein; interaction; proteomics; proximity labelling

0 (Proteome)

Date Created: 20211109 Date Completed: 20220324 Latest Revision: 20220324

20221213

10.1093/jb/mvab123

34752609