Work

Deciphering Tissue-Specific Ubiquitylation by Mass Spectrometry

Year: 2012

Type: book-chapter

Abstract: Protein ubiquitylation is a highly conserved, central mechanism to regulate cellular events in all eukaryotes, such as proteasomal degradation, protein trafficking, DNA repair, synaptic plasticity, and immune response. The consequence of protein ubiquitylation is modulated by the structure of ubiquitin (Ub) moiety attached on the substrates, including ubiquitin monomer and diverse polyubiquitin chains with different linkages (N-terminus, K6, K11, K27, K29, K33, K48, and K63). The development of ubiquitin-enrichment strategies coupled with sensitive mass spectrometry enables direct analysis of ubiquitylated proteins in cells, providing an invaluable tool for ubiquitin research. In this chapter, we describe recent technology updates for analyzing tissue-specific ubiquitin conjugates in transgenic models, as well as targeted proteomics methods for quantifying different polyubiquitin chain linkages in any type of -samples, including human tissues.

Source: Methods in molecular biology

DOI: 10.1007/978-1-61779-474-2_3

Authors: Ugo Mayor, Junmin Peng

Institutions: Ikerbasque, St. Jude Children's Research Hospital

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Center for Research Resources

Awards: G2654164304, Analysis of Ubiquitinated Proteome