title: Proteomic insights into ubiquitin and ubiquitin-like proteins.
abstract: The dynamic and specific modification of cellular proteins by members of the ubiquitin protein family is a vital regulatory mechanism that lies at the heart of almost all biological processes. Because of both their pervasive and complex nature, these regulatory pathways have been the target of many recent proteomic studies. Such works have provided numerous insights. Through the use of various mass spectrometry techniques, affinity purification methods, and/or chemical probes, large lists have begun to be compiled for the multitude of substrates, interacting partners, and enzymatic components of these regulatory circuits. Furthermore, similar tools have provided many insights into functional aspects such as their mechanisms of substrate specificity and enzymatic activity. This review provides a summary of these recent proteomic works, along with comments on future directions of the field.
authors.affiliation: Department of Cell Biology, 240 Longwood Avenue, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Carilee
authors.initials: C
authors.lastname: Denison
authors.forename: Donald S
authors.initials: DS
authors.lastname: Kirkpatrick
authors.forename: Steven P
authors.initials: SP
authors.lastname: Gygi
mesh_terms: D006801:Humans; D040901:Proteomics; D025801:Ubiquitin / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism*; D015003:Yeasts / Q000378:metabolism
chemical_list: D025801:Ubiquitin; D014452:Ubiquitins