Signaling through monoubiquitination.

by: S Sigismund, S Polo, PP Di Fiore

Curr Top Microbiol Immunol, Vol. 286 (2004), pp. 149-185.

View FullText article

Pubmed, Hubmed

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

kieran101, ecattell

Find related articles with these CiteULike tags

monoub, review, ubiquitin

Abstract

Ubiquitination is a post-translational modification in which a small conserved peptide, ubiquitin, is appended to target proteins in the cell, through a series of complex enzymatic reactions. Recently, a particular form of ubiquitination, monoubiquitination, has emerged as a nonproteolytic reversible modification that controls protein function. In this review, we highlight recent findings on monoubiquitination as a signaling-induced modification, controlled, among others, by pathways originating from active receptor tyrosine kinases. Furthermore, we review the major cellular processes controlled by ubiquitin modification, including membrane trafficking, histone function, transcription regulation, DNA repair, and DNA replication.

@article{citeulike:1342967, abstract = {Ubiquitination is a post-translational modification in which a small conserved peptide, ubiquitin, is appended to target proteins in the cell, through a series of complex enzymatic reactions. Recently, a particular form of ubiquitination, monoubiquitination, has emerged as a nonproteolytic reversible modification that controls protein function. In this review, we highlight recent findings on monoubiquitination as a signaling-induced modification, controlled, among others, by pathways originating from active receptor tyrosine kinases. Furthermore, we review the major cellular processes controlled by ubiquitin modification, including membrane trafficking, histone function, transcription regulation, DNA repair, and DNA replication.}, address = {IFOM, The FIRC Institute for Molecular Oncology, Via Adamello 16, 20139 Milan, Italy.}, author = {Sigismund, S. and Polo, S. and Di Fiore, P. P. }, citeulike-article-id = {1342967}, issn = {0070-217X}, journal = {Curr Top Microbiol Immunol}, keywords = {ubiquitin}, pages = {149--185}, posted-at = {2008-05-15 18:06:36}, priority = {2}, title = {Signaling through monoubiquitination.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/15645713}, volume = {286}, year = {2004} }

RIS record

TY - JOUR ID - citeulike:1342967 L3 - citeulike-article-id:1342967 TI - Signaling through monoubiquitination. JF - Curr Top Microbiol Immunol VL - 286 SP - 149 EP - 185 AD - IFOM, The FIRC Institute for Molecular Oncology, Via Adamello 16, 20139 Milan, Italy. SN - 0070-217X N2 - Ubiquitination is a post-translational modification in which a small conserved peptide, ubiquitin, is appended to target proteins in the cell, through a series of complex enzymatic reactions. Recently, a particular form of ubiquitination, monoubiquitination, has emerged as a nonproteolytic reversible modification that controls protein function. In this review, we highlight recent findings on monoubiquitination as a signaling-induced modification, controlled, among others, by pathways originating from active receptor tyrosine kinases. Furthermore, we review the major cellular processes controlled by ubiquitin modification, including membrane trafficking, histone function, transcription regulation, DNA repair, and DNA replication. KW - ubiquitin AU - Sigismund, S AU - Polo, S AU - Di Fiore, PP PY - 2004/// UR - http://view.ncbi.nlm.nih.gov/pubmed/15645713 ER -

RIS BibTeX