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

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.

journal_name

J Proteome Res

journal_title

Journal of proteome research

authors

Doherty MK,Hammond DE,Clague MJ,Gaskell SJ,Beynon RJ

doi

10.1021/pr800641v

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

104-12

issue

1

eissn

1535-3893

issn

1535-3907

journal_volume

8

pub_type

杂志文章

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