Pat1 proteins are conserved across eukaryotes. Vertebrates have evolved two Pat1 proteins paralogues, whereas invertebrates and yeast only possess one such protein. Despite their lack of known domains or motifs, Pat1 proteins are involved in several key post-transcriptional mechanisms of gene expression control. In yeast, Pat1p interacts with translating mRNPs (messenger ribonucleoproteins), and is responsible for translational repression and decapping activation, ultimately leading to mRNP degradation. Drosophila HPat and human Pat1b (PatL1) proteins also have conserved roles in the 5′→3′ mRNA decay pathway. Consistent with their functions in silencing gene expression, Pat1 proteins localize to P-bodies (processing bodies) in yeast, Drosophila, Caenorhabditis elegans and human cells. Altogether, Pat1 proteins may act as scaffold proteins allowing the sequential binding of repression and decay factors on mRNPs, eventually leading to their degradation. In the present mini-review, we present the current knowledge on Pat1 proteins in the context of their multiple functions in post-transcriptional control.
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Conference Article|
November 24 2010
Pat1 proteins: a life in translation, translation repression and mRNA decay
Aline Marnef;
Aline Marnef
1Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, U.K.
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Nancy Standart
Nancy Standart
1
1Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, U.K.
1To whom correspondence should be addressed (email nms@mole.bio.cam.ac.uk).
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Publisher: Portland Press Ltd
Received:
June 30 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem Soc Trans (2010) 38 (6): 1602–1607.
Article history
Received:
June 30 2010
Citation
Aline Marnef, Nancy Standart; Pat1 proteins: a life in translation, translation repression and mRNA decay. Biochem Soc Trans 1 December 2010; 38 (6): 1602–1607. doi: https://doi.org/10.1042/BST0381602
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