When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling

Hdl Handle:
http://hdl.handle.net/10147/299874
Title:
When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling
Authors:
Nguyen, Lan K; Kolch, Walter; Kholodenko, Boris N
Citation:
Cell Communication and Signaling. 2013 Jul 31;11(1):52
Issue Date:
31-Jul-2013
URI:
http://dx.doi.org/10.1186/1478-811X-11-52; http://hdl.handle.net/10147/299874
Abstract:
Abstract Ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as a ubiquitous post-translational modification (PTM) whose function extends far beyond its original role as a tag for protein degradation identified three decades ago. Although sharing parallel properties with phosphorylation, ubiquitination distinguishes itself in important ways. Nevertheless, the interplay and crosstalk between ubiquitination and phosphorylation events have become a recurrent theme in cell signalling regulation. Understanding how these two major PTMs intersect to regulate signal transduction is an important research question. In this review, we first discuss the involvement of ubiquitination in the regulation of the EGF-mediated ERK signalling pathway via the EGF receptor, highlighting the interplay between ubiquitination and phosphorylation in this cancer-implicated system and addressing open questions. The roles of ubiquitination in pathways crosstalking to EGFR/MAPK signalling will then be discussed. In the final part of the review, we demonstrate the rich and versatile dynamics of crosstalk between ubiquitination and phosphorylation by using quantitative modelling and analysis of network motifs commonly observed in cellular processes. We argue that given the overwhelming complexity arising from inter-connected PTMs, a quantitative framework based on systems biology and mathematical modelling is needed to efficiently understand their roles in cell signalling.
Item Type:
Article
Language:
en
Keywords:
GENETICS
Local subject classification:
CELL BIOLOGY; SYSTEMS BIOLOGY

Full metadata record

DC FieldValue Language
dc.contributor.authorNguyen, Lan Ken_GB
dc.contributor.authorKolch, Walteren_GB
dc.contributor.authorKholodenko, Boris Nen_GB
dc.date.accessioned2013-08-26T16:40:18Z-
dc.date.available2013-08-26T16:40:18Z-
dc.date.issued2013-07-31-
dc.identifier.citationCell Communication and Signaling. 2013 Jul 31;11(1):52en_GB
dc.identifier.urihttp://dx.doi.org/10.1186/1478-811X-11-52-
dc.identifier.urihttp://hdl.handle.net/10147/299874-
dc.description.abstractAbstract Ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as a ubiquitous post-translational modification (PTM) whose function extends far beyond its original role as a tag for protein degradation identified three decades ago. Although sharing parallel properties with phosphorylation, ubiquitination distinguishes itself in important ways. Nevertheless, the interplay and crosstalk between ubiquitination and phosphorylation events have become a recurrent theme in cell signalling regulation. Understanding how these two major PTMs intersect to regulate signal transduction is an important research question. In this review, we first discuss the involvement of ubiquitination in the regulation of the EGF-mediated ERK signalling pathway via the EGF receptor, highlighting the interplay between ubiquitination and phosphorylation in this cancer-implicated system and addressing open questions. The roles of ubiquitination in pathways crosstalking to EGFR/MAPK signalling will then be discussed. In the final part of the review, we demonstrate the rich and versatile dynamics of crosstalk between ubiquitination and phosphorylation by using quantitative modelling and analysis of network motifs commonly observed in cellular processes. We argue that given the overwhelming complexity arising from inter-connected PTMs, a quantitative framework based on systems biology and mathematical modelling is needed to efficiently understand their roles in cell signalling.-
dc.language.isoenen
dc.subjectGENETICSen_GB
dc.subject.otherCELL BIOLOGYen_GB
dc.subject.otherSYSTEMS BIOLOGYen_GB
dc.titleWhen ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signallingen_GB
dc.typeArticleen
dc.language.rfc3066en-
dc.rights.holderLan K Nguyen et al.; licensee BioMed Central Ltd.-
dc.description.statusPeer Reviewed-
dc.date.updated2013-08-05T15:08:58Z-
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