Profiling of ubiquitin-like modifications reveals features of mitotic control

Yifat Merbl, Phillipe Refour, Hevan Patel, Michael Springer, Marc W. Kirschner

Research output: Contribution to journalArticlepeer-review

Abstract

Ubiquitin and ubiquitin-like (Ubl) protein modifications affect protein stability, activity, and localization, but we still lack broad understanding of the functions of Ubl modifications. We have profiled the protein targets of ubiquitin and six additional Ubls in mitosis using a functional assay that utilizes active mammalian cell extracts and protein microarrays and identified 1,500 potential substrates; 80-200 protein targets were exclusive to each Ubl. The network structure is nonrandom, with most targets mapping to a single Ubl. There are distinct molecular functions for each Ubl, suggesting divergent biological roles. Analysis of differential profiles between mitosis and G1 highlighted a previously underappreciated role for the Ubl, FAT10, in mitotic regulation. In addition to its role as a resource for Ubl modifications, our study provides a systematic approach to analyze changes in posttranslational modifications at various cellular states.

Original languageEnglish
Pages (from-to)1160-1172
Number of pages13
JournalCell
Volume152
Issue number5
DOIs
StatePublished - 28 Feb 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Biochemistry,Genetics and Molecular Biology

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