Format

Send to

Choose Destination
See comment in PubMed Commons below
J Proteome Res. 2009 Jan;8(1):104-12. doi: 10.1021/pr800641v.

Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC.

Author information

1
School of Biomedical Sciences, University of Liverpool, Crown Street, Liverpool L69 3BX, UK.

Abstract

The proteome of any system is a dynamic entity, such that the intracellular concentration of a protein is dictated by the relative rates of synthesis and degradation. In this work, we have analyzed time-dependent changes in the incorporation of a stable amino acid resolved precursor, a protocol we refer to as "dynamic SILAC", using 1-D gel separation followed by in-gel digestion and LC-MS/MS analyses to profile the intracellular stability of almost 600 proteins from human A549 adenocarcinoma cells, requiring multiple measures of the extent of labeling with stable isotope labeled amino acids in a classic label-chase experiment. As turnover rates are acquired, a profile can be built up that allows exploration of the 'dynamic proteome' and of putative features that predispose a protein to a high or a low rate of turnover. Moreover, measurement of the turnover rate of individual components of supramolecular complexes provides a unique insight in processes of protein complex assembly and turnover.

PMID:
18954100
DOI:
10.1021/pr800641v
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center