1. Academic Validation
  2. Identification of PatL1, a human homolog to yeast P body component Pat1

Identification of PatL1, a human homolog to yeast P body component Pat1

  • Biochim Biophys Acta. 2007 Dec;1773(12):1786-92. doi: 10.1016/j.bbamcr.2007.08.009.
Nicoletta Scheller 1 Patricia Resa-Infante Susana de la Luna Rui Pedro Galao Mario Albrecht Lars Kaestner Peter Lipp Thomas Lengauer Andreas Meyerhans Juana Díez
Affiliations

Affiliation

  • 1 Institute of Virology, Saarland University, 66421 Homburg, Germany.
Abstract

In yeast, the activators of mRNA decapping, Pat1, Lsm1 and Dhh1, accumulate in processing bodies (P bodies) together with Other proteins of the 5'-3'-deadenylation-dependent mRNA decay pathway. The Pat1 protein is of particular interest because it functions in the opposing processes of mRNA translation and mRNA degradation, thus suggesting an important regulatory role. In contrast to Other components of this mRNA decay pathway, the human homolog of the yeast Pat1 protein was unknown. Here we describe the identification of two human PAT1 genes and show that one of them, PATL1, codes for an ORF with similar features as the yeast PAT1. As expected for a protein with a fundamental role in translation control, PATL1 mRNA was ubiquitously expressed in all human tissues as were the mRNAs of LSM1 and RCK, the human homologs of yeast LSM1 and DHH1, respectively. Furthermore, fluorescence-tagged PatL1 protein accumulated in distinct foci that correspond to P bodies, as they co-localized with the P body components Lsm1, Rck/p54 and the decapping Enzyme Dcp1. In addition, as for its yeast counterpart, PatL1 expression was required for P body formation. Taken together, these data emphasize the conservation of important P body components from yeast to human cells.

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