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Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico

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Volume 3, Issue 4


Pat1 proteins: regulating mRNAs from birth to death?

Nancy Standart
  • Corresponding author
  • Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK
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/ Aline Marnef
Published Online: 2012-06-20 | DOI: https://doi.org/10.1515/bmc-2012-0005


The Pat1 protein family has been the subject of several recent extensive investigations of diverse model systems ranging from yeast, flies and worms to man, using a variety of experimental approaches. Although some contradictions remain, the emerging consensus view is that these RNA-binding proteins act in mRNA decay by physically linking deadenylation with decapping and by regulating gene expression as translational repressors. These multiple functions are present in the single invertebrate Pat1 proteins, whereas, in vertebrates, one Pat1 variant represses translation in early development, while a somatic version synthesised in embrogenesis and in adults acts in mRNA decay. At steady state, Pat1 proteins are found enriched in cytoplasmic P(rocessing)-bodies, and related mRNP complexes and granules. Evidence recently obtained from mammalian tissue culture cells shows that Pat1 shuttles in and out of the nucleus, where it localises to nuclear speckles, PML bodies and nucleolar caps, which suggests RNA-related nuclear functions. Less well understood, Pat1 proteins may play additional roles in miRNA silencing and/or biogenesis, as well in the regulation of viral gene expression. Due to the relatively low level of sequence conservation between Pat1 proteins from different species and lacking any discernable motifs, determining their functional domains has proved difficult, as is obtaining a simple unified view of the location of the binding sites of their interacting proteins in all examined species. Questions that remain to be addressed include the following: 1) What are their roles in the nucleus? 2) What is the link, if one exists, between their cytoplasmic and nuclear roles? 3) Do they have specific mRNA targets? 4) Which signalling pathways regulate their P-body localisation in mammalian cells, which may affect quiescent cell survival?

Keywords: 4E-T; HeLa cells; Pat1b; rck/p54/Dhh1; Xenopus oocytes

About the article

Nancy Standart

Nancy Standart, an American born in Prague, undertook her undergraduate and graduate studies in the UK, and did post-doctoral work with Klaus Scherrer in Paris, Joan Ruderman in Cambridge, USA and Tim Hunt in Cambridge, UK. Her early research interests focused on control of translation (and mRNA localization) in early development by specific RNA-binding proteins, first in marine invertebrates and then in Xenopus. Currently, the lab studies the role of P-body components in gene expression regulation.

Aline Marnef

Aline Marnef is from Belgium and did her undergraduate studies in Applied Genetics at U.W.E. in Bristol. During her studies she gained experiences in bacterial genetics, developmental biology, proteomics and mRNP complexes. AM did her PhD degree in Nancy Standart’s lab in the Biochemistry Department at the University of Cambridge, where she investigated the roles of Pat1 proteins and P-bodies in the control of gene expression, in particular at the post-transcriptional level. In 2012, she joined Dr Tamas Kiss’ group in Toulouse (France) and now works on nuclear non-coding RNAs.

Corresponding author

Received: 2012-02-16

Accepted: 2012-05-14

Published Online: 2012-06-20

Published in Print: 2012-08-01

Citation Information: BioMolecular Concepts, Volume 3, Issue 4, Pages 295–306, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/bmc-2012-0005.

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©2012 by Walter de Gruyter Berlin Boston.Get Permission

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