2009
DOI: 10.1083/jcb.200904111
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Yvh1 is required for a late maturation step in the 60S biogenesis pathway

Abstract: The step by step assembly process from preribosome in the nucleus to translation-competent 60S ribosome subunit in the cytoplasm is revealed (also see Lo et al. in this issue).

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Cited by 102 publications
(151 citation statements)
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“…The predominant phenotype associated with Yvh1 malfunction or other conditions affecting Mrt4-P-stalk exchange is re-localization of the Mrt4 protein from the nucleus/nucleolus into the cytoplasm. 28,38,39 We saw no signs of such abnormal Mrt4 behavior, which was found in the nuclear compartment in the wild type and in both mutants analyzed, namely the DuL11AB and DEfl1 strains (Fig. 4B).…”
Section: Ribosomal Biogenesismentioning
confidence: 95%
“…The predominant phenotype associated with Yvh1 malfunction or other conditions affecting Mrt4-P-stalk exchange is re-localization of the Mrt4 protein from the nucleus/nucleolus into the cytoplasm. 28,38,39 We saw no signs of such abnormal Mrt4 behavior, which was found in the nuclear compartment in the wild type and in both mutants analyzed, namely the DuL11AB and DEfl1 strains (Fig. 4B).…”
Section: Ribosomal Biogenesismentioning
confidence: 95%
“…This finding is reminiscent of studies in yeast where the phosphatase activity seems dispensable for complementing various cell growth defects including sporulation and ribosome biogenesis, when the yvh1 gene is deleted while the zinc-binding domain is required. 4,8,12,13 While the precise function of this domain remains unknown, we predict that it serves as an interaction module and are currently performing mass spectrometry-based experiments aimed at identifying biomolecules (proteins and/or nucleic acids) that associate with this domain in a cell cycle-dependent manner.…”
Section: Discussionmentioning
confidence: 99%
“…In yeast, the C-terminal zinc-binding domain is able to complement the slow-growth phenotype of a yvh1 deletion, 8,16 rescue the 60S export defect 12,13,16 and is necessary for glycogen accumulation, growth and spore maturation. 8 In humans, this domain can function as a redox sensor and is necessary for the cytoprotective function of hYVH1.…”
Section: O N O T D I S T R I B U T Ementioning
confidence: 99%
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“…Insights into DUSP12's cellular function(s) can be obtained by investigating the budding yeast DUSP12 ortholog, Yvh1p. YVH1 transcription is up-regulated by nitrogen starvation and low temperatures and yvh1Δ yeast strains exhibit a severe growth phenotype, display defects in sporulation, glycogen accumulation, and ribosome biogenesis [74][75][76][77][78]. Expression of the Yvh1p CRD domain in isolation was able to suppress all the mutant phenotypes of yvh1Δ strains, suggesting that neither phosphatase activity nor the N-terminal phosphatase domain is required for its cellular function in yeast [76].…”
Section: Dusp12mentioning
confidence: 99%