Evidence map›Paper›PMID 23175604›Full record

ArticleNucleic acids research2013

Las1 interacts with Grc3 polynucleotide kinase and is required for ribosome synthesis in Saccharomyces cerevisiae.

Christopher D Castle, Richa Sardana, Varada Dandekar, Victoria Borgianini, Arlen W Johnson, Catherine Denicourt

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
0.4field-weighted citation impact, top 37% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Many paths to destruction: Family-specific turnover and stress responses for tRNA introns.Proceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Christopher D CastleDepartment of Integrative Biology and Pharmacology, Graduate School of Biomedical Sciences, The University of Texas Health Science Center, Houston, TX 77030, USA.
Richa Sardana
Varada Dandekar
Victoria Borgianini
Arlen W Johnson
Catherine Denicourt
The University of Texas Health Science Center at Houston · US

Funding

MRNA DEGRADATION AND TRANSLATION CONTROL IN YEASTR01GM053655 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSON, ARLEN W · 1995 to 2017
$5.1M
NIGMS NIH HHS GM53655NIGMS NIH HHS R01 GM053655
6 · The paper itself

Abstract

Ribosome biogenesis is a multi-step process that couples cell growth with cell proliferation. Although several large-scale analysis of pre-ribosomal particles have identified numerous trans-acting factors involved in this process, many proteins involved in pre-rRNA processing and ribosomal subunit maturation have yet to be identified. Las1 was originally identified in Saccharomyces cerevisiae as a protein involved in cell morphogenesis. We previously demonstrated that the human homolog, Las1L, is required for efficient ITS2 rRNA processing and synthesis of the 60S ribosomal subunit. Here, we report that the functions of Las1 in ribosome biogenesis are also conserved in S. cerevisiae. Depletion of Las1 led to the accumulation of both the 27S and 7S rRNA intermediates and impaired the synthesis of the 60S subunit. We show that Las1 co-precipitates mainly with the 27S rRNA and associates with an Nsa1 and Rix1-containing pre-60S particle. We further identify Grc3 as a major Las1-interacting protein. We demonstrate that the kinase activity of Grc3 is required for efficient pre-rRNA processing and that depletion of Grc3 leads to rRNA processing defects similar to the ones observed in Las1-depleted cells. We propose that Las1 and Grc3 function together in a conserved mechanism to modulate rRNA processing and eukaryotic ribosome biogenesis.

Indexed as

RNA Processing, Post-TranscriptionalCell CycleNuclear ProteinsPolynucleotide 5'-Hydroxyl-KinaseRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLAS1 protein, S cerevisiaeNsa1 protein, S cerevisiaeNuclear ProteinsPolynucleotide 5'-Hydroxyl-KinaseRibosomal ProteinsRix1 protein, S cerevisiaeRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID23175604
PMCPMC3553937
OpenAlexW2157475454

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.