Open AccessTRIM proteins in blood cancers
Author(s) -
Crawford Lisa J.,
Johnston Cliona K.,
Irvine Alexandra E.
Publication year - 2018
Publication title -
journal of cell communication and signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 44
eISSN - 1873-961X
pISSN - 1873-9601
DOI - 10.1007/s12079-017-0423-5
Subject(s) - ubiquitin , trim , ubiquitin protein ligases , ubiquitin ligase , biology , bioinformatics , microbiology and biotechnology , computational biology , medicine , genetics , gene , computer science , operating system
Post‐translational modification of proteins with ubiquitin plays a central role in regulating numerous cellular processes. E3 ligases determine the specificity of ubiquitination by mediating the transfer of ubiquitin to substrate proteins. The family of tripartite motif (TRIM) proteins make up one of the largest subfamilies of E3 ligases. Accumulating evidence suggests that dysregulation of TRIM proteins is associated with a variety of diseases. In this review we focus on the involvement of TRIM proteins in blood cancers.