title: Identification of PatL1, a human homolog to yeast P body component Pat1.
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.
authors.affiliation: Institute of Virology, Saarland University, 66421 Homburg, Germany.
authors.forename: Nicoletta
authors.initials: N
authors.lastname: Scheller
authors.forename: Patricia
authors.initials: P
authors.lastname: Resa-Infante
authors.forename: Susana
authors.initials: S
authors.lastname: de la Luna
authors.forename: Rui Pedro
authors.initials: RP
authors.lastname: Galao
authors.forename: Mario
authors.initials: M
authors.lastname: Albrecht
authors.forename: Lars
authors.initials: L
authors.lastname: Kaestner
authors.forename: Peter
authors.initials: P
authors.lastname: Lipp
authors.forename: Thomas
authors.initials: T
authors.lastname: Lengauer
authors.forename: Andreas
authors.initials: A
authors.lastname: Meyerhans
authors.forename: Juana
authors.initials: J
authors.lastname: Díez
mesh_terms: D022083:Cytoplasmic Structures / Q000378:metabolism*; D053487:DEAD-box RNA Helicases / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D020869:Gene Expression Profiling; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D021381:Protein Transport; D011518:Proto-Oncogene Proteins / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D017385:Sequence Homology
chemical_list: D004268:DNA-Binding Proteins; C464824:LSM1 protein, human; C103266:PAT1 protein, S cerevisiae; C526510:PATL1 protein, human; D011518:Proto-Oncogene Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C094683:DDX6 protein, human; D053487:DEAD-box RNA Helicases