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Comparative analysis of interactions of RASSF1-10

Chan, JJ; Flatters, D; Rodrigues-Lima, F; Yan, J; Thalassinos, K; Katan, M; (2013) Comparative analysis of interactions of RASSF1-10. Advances in Biological Regulation , 53 (2) 190 - 201. 10.1016/j.jbior.2012.12.001. Green open access

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Abstract

Members of the RASSF family (RASSF1-10) have been identified as candidate tumour suppressors that are frequently downregulated by promoter hypermethylation in cancers. These proteins carry a common Ras-association (RA) and SARAH domain (RASSF1-6) that can potentially bind Ras oncoproteins and mediate protein-protein interactions with other SARAH domain proteins. However, there is a notable lack of comparative characterisation of the RASSF family, as well as molecular and structural information that facilitate their tumour suppressive functions. As part of our comparative analysis, we modelled the RA and SARAH domains of the RASSF members based on existing structures and predicted their potential interactions. These in silico predictions were compared to in vitro interaction studies with Ras and MST kinase (a SARAH domain-containing protein). Our data shows a diversity of interaction within the RASSF family RA domain, whereas the SARAH domain-mediated interactions for RASSF1-6 are consistent with the predictions. This suggests that different members, despite shared general architecture, could have distinct functional properties. Additionally, we identify a new interacting partner for MST kinase in the form of RASSF7. Current data supports an interaction model where RASSF serves as an adaptor for the assembly of multiple protein complexes and further functional interactions, involving MST kinases and other SARAH domain proteins, which could be regulated by Ras.

Type: Article
Title: Comparative analysis of interactions of RASSF1-10
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/j.jbior.2012.12.001
Publisher version: http://dx.doi.org/10.1016/j.jbior.2012.12.001
Language: English
Additional information: This is the author’s version of a work that was accepted for publication in Advances in Biological Regulation. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Advances in Biological Regulation, Volume 53, Issue 2, May 2013 http://dx.doi.org/10.1016/j.jbior.2012.12.001
Keywords: Amino Acid Sequence, Models, Molecular, Monomeric GTP-Binding Proteins, Protein Multimerization, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Sequence Alignment, Transcription Factors, Tumor Suppressor Proteins, ras Proteins
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1385511
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