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

Scheller, Nicoletta; Resa-Infante, Patricia; Luna, Susana de la; Galão, Rui Pedro; Albrecht, Mario; Kaestner, Lars; Lipp, Peter; Lengauer, Thomas; Meyerhans, Andreas; Díez, Juana

doi:10.1016/j.bbamcr.2007.08.009

Cited by 57 publications

(61 citation statements)

References 40 publications

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“…2), it is also clear that during most of oogenesis Pat1a functions alone, while in embryos (Fig. 2) and adult tissues (Scheller et al 2007), Pat1b predominates, suggesting that they may have different functions. We therefore asked whether in stage VI oocytes endogenous xPat1a and xPat1b interacted with CPEB, by gel filtration and coimmunoprecipitation assays.…”

Section: Flag-tagged Xpat1a and Xpat1b Interact With Cpeb Rnp Componementioning

confidence: 99%

“…Using different antibodies to xPat1 proteins, Nakamura et al (2010) show a similar pattern of expression and phosphorylation in oocytes and eggs. Overall, based on our and others' data (Rother et al 1992;Scheller et al 2007), we conclude that maternal Pat1a is replaced by Pat1b in embryos and adults. xPat1 protein expression switch in meiosis results from xPat1a degradation and cytoplasmic polyadenylation of xPat1b mRNA…”

Section: Vertebrates Possess Two Proteins Related To Yeast Pat1mentioning

confidence: 99%

“…Human Pat1a is not expressed in HeLa cells, according to qPCR and Northern blot data (data not shown; Scheller et al 2007). Hence, to compare Pat1a and Pat1b localization, we transfected cells with GFP fusion proteins encoding mammalian Pat1 proteins.…”

Section: Pat1a Proteins Disperse P-bodies In a Dominant-negative Mannermentioning

confidence: 99%

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Distinct functions of maternal and somatic Pat1 protein paralogs

Marnef¹,

Maldonado²,

Bugaut³

et al. 2010

RNA

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We previously identified Xenopus Pat1a (P100) as a member of the maternal CPEB RNP complex, whose components resemble those of P-(rocessing) bodies, and which is implicated in translational control in Xenopus oocytes. Database searches have identified Pat1a proteins in other vertebrates, as well as paralogous Pat1b proteins. Here we characterize Pat1 proteins, which have no readily discernable sequence features, in Xenopus oocytes, eggs, and early embryos and in human tissue culture cells. xPat1a and 1b have essentially mutually exclusive expression patterns in oogenesis and embryogenesis. xPat1a is degraded during meiotic maturation, via PEST-like regions, while xPat1b mRNA is translationally activated at GVBD by cytoplasmic polyadenylation. Pat1 proteins bind RNA in vitro, via a central domain, with a preference for G-rich sequences, including the NRAS 59 UTR G-quadruplex-forming sequence. When tethered to reporter mRNA, both Pat proteins repress translation in oocytes. Indeed, both epitope-tagged proteins interact with the same components of the CPEB RNP complex, including CPEB, Xp54, eIF4E1b, Rap55B, and ePAB. However, examining endogenous protein interactions, we find that in oocytes only xPat1a is a bona fide component of the CPEB RNP, and that xPat1b resides in a separate large complex. In tissue culture cells, hPat1b localizes to P-bodies, while mPat1a-GFP is either found weakly in P-bodies or disperses P-bodies in a dominant-negative fashion. Altogether we conclude that Pat1a and Pat1b proteins have distinct functions, mediated in separate complexes. Pat1a is a translational repressor in oocytes in a CPEB-containing complex, and Pat1b is a component of P-bodies in somatic cells.

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Section: Flag-tagged Xpat1a and Xpat1b Interact With Cpeb Rnp Componementioning

confidence: 99%

Section: Vertebrates Possess Two Proteins Related To Yeast Pat1mentioning

confidence: 99%

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Distinct functions of maternal and somatic Pat1 protein paralogs

Marnef¹,

Maldonado²,

Bugaut³

et al. 2010

RNA

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“…They do not have any readily recognizable motifs (Scheller et al 2007;Ozgur et al 2010). The region close to the N terminus of Pat1 proteins is sufficient for interaction with Dhh1 orthologs in yeast, Drosophila, and humans Haas et al 2010;Ozgur et al 2010;.…”

Section: Introductionmentioning

confidence: 99%

“…Like the Lsm1 through Lsm7 proteins, Pat1 is also well conserved in all eukaryotes. While a single Pat1 protein is present in yeast and invertebrates (Bonnerot et al 2000;Bouveret et al 2000;Tharun et al 2000;Eulalio et al 2007;Gallo et al 2008), vertebrates have two paralogs, Pat1a and Pat1b (Rother et al 1992;Scheller et al 2007;. Pat1 has been implicated in several functions, and not all of them are related to its association with the Lsm1-7 complex.…”

Section: Introductionmentioning

confidence: 99%

Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex

Chowdhury

Kalurupalle

Tharun

2014

RNA

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A major mRNA decay pathway in eukaryotes is initiated by deadenylation followed by decapping of the oligoadenylated mRNAs and subsequent 5 ′ -to-3 ′ exonucleolytic degradation of the capless mRNA. In this pathway, decapping is a rate-limiting step that requires the hetero-octameric Lsm1-7-Pat1 complex to occur at normal rates in vivo. This complex is made up of the seven Sm-like proteins, Lsm1 through Lsm7, and the Pat1 protein. It binds RNA and has a unique binding preference for oligoadenylated RNAs over polyadenylated RNAs. Such binding ability is crucial for its mRNA decay function in vivo. In order to determine the contribution of Pat1 to the function of the Lsm1-7-Pat1 complex, we compared the RNA binding properties of the Lsm1-7 complex purified from pat1Δ cells and purified Pat1 fragments with that of the wild-type Lsm1-7-Pat1 complex. Our studies revealed that both the Lsm1-7 complex and purified Pat1 fragments have very low RNA binding activity and are impaired in the ability to recognize the oligo(A) tail on the RNA. However, reconstitution of the Lsm1-7-Pat1 complex from these components restored these abilities. We also observed that Pat1 directly contacts RNA in the context of the Lsm1-7-Pat1 complex. These studies suggest that the unique RNA binding properties and the mRNA decay function of the Lsm1-7-Pat1 complex involve cooperation of residues from both Pat1 and the Lsm1-7 ring. Finally our studies also revealed that the middle domain of Pat1 is essential for the interaction of Pat1 with the Lsm1-7 complex in vivo.

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Molecular cloning and characterization of oocyte-specific Pat1a inRana rugosafrogs

et al. 2015

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The Pat1 gene is expressed in the immature oocytes of Xenopus, and is reportedly involved in regulating the translation of maternal mRNAs required for oocyte-maturation. However, it is still unknown when Pat1a first appears in the differentiating ovary of amphibians. To address this issue, we isolated the full-length Pat1a cDNA from the frog Rana rugosa and examined its expression in the differentiating ovary of this frog. Among eight different tissues examined, the Pat1a mRNA was detectable in only the ovary. When frozen sections from the ovaries of tadpoles at various stages of development were immunostained for Vasa-a germ cell-specific protein-and Pat1a, Vasa-immunopositive signals were observed in all of the germ cells, whereas Pat1a signals were confined to the growing oocytes (50-200 μm in diameter), and absent from small germ cells (<50 μm in diameter). Forty days after testosterone injection into tadpoles to induce female-to-male sex-reversal, Pat1a-immunoreactive oocytes had disappeared completely from the sex-reversed gonad, but Vasa-positive small germ cells persisted. Thus, Pat1a would be a good marker for identifying the sexual status of the sex-reversing gonad in amphibians. In addition, fluorescence in situ hybridization analysis showed Pat1a to have an autosomal locus, suggesting that Pat1a transcription is probably regulated by a tissue-specific transcription factor in R. rugosa.

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

Cited by 57 publications

References 40 publications

Distinct functions of maternal and somatic Pat1 protein paralogs

Distinct functions of maternal and somatic Pat1 protein paralogs

Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex

Molecular cloning and characterization of oocyte-specific Pat1a inRana rugosafrogs

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