RAP55: Insights into an evolutionarily conserved protein family

Marnef, A., Sommerville, J. and Ladomery, M. (2009) RAP55: Insights into an evolutionarily conserved protein family. The International Journal of Biochemistry & Cell Biology, 41 (5). pp. 977-981. ISSN 1357-2725 Available from: http://eprints.uwe.ac.uk/7142

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Publisher's URL: http://dx.doi.org/10.1016/j.biocel.2008.06.015


The RAP55 protein family is evolutionarily conserved in eukaryotes. Two highly conserved paralogues, RAP55A and RAP55B, exist in vertebrates; their functional properties and expression patterns remain to be compared. RAP55 proteins share multiple domains: the LSm14 domain, a serine/threonine rich region, an FDF (phenylalanine–aspartate–phenylalanine) motif, an FFD-TFG box and RGG (arginine–glycine–glycine) repeats. Together these domains are responsible for RAP55 proteins participating in translational repression, incorporation into mRNP particles, protein–protein interactions, P-body formation and stress granule localisation. All RAP55A proteins localise to P-body-like complexes either in the germline or in somatic cells. Xenopus laevis RAP55B has been shown to be part of translationally repressed mRNP complexes in early oocytes. Together these findings suggest that this protein family has evolved a common and fundamental role in the control of mRNA translation. Furthermore human RAP55A is an autoantigen detected in the serum of patients with primary biliary cirrhosis (PBC). The link between RAP55A, P-bodies and PBC remains to be elucidated.

Item Type:Article
Uncontrolled Keywords:RAP55, MRNP particles, P-bodies, stress granules, translational repression
Faculty/Department:Faculty of Health and Applied Sciences > Department of Applied Sciences
ID Code:7142
Deposited By: H. Hammond
Deposited On:15 Jul 2010 07:36
Last Modified:15 Nov 2016 23:26

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