Evidence map›Paper›PMID 20837994›Full record

ArticleGenetics2010

Telomerase recruitment in Saccharomyces cerevisiae is not dependent on Tel1-mediated phosphorylation of Cdc13.

Hua Gao, Tasha B Toro, Margherita Paschini, Bari Braunstein-Ballew, Rachel B Cervantes, Victoria Lundblad

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 52 citations in OpenAlex.

  1. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 3 institutions in 1 country.

Hua GaoSalk Institute for Biological Studies, La Jolla, California 92093-0130, USA.
Tasha B Toro
Margherita Paschini
Bari Braunstein-Ballew
Rachel B Cervantes
Victoria Lundblad
Salk Institute for Biological Studies · USBaylor College of Medicine · USUniversity of California, San Diego · US

Funding

DUAL ROLE FOR CDC13 IN YEAST TELOMERE FUNCTIONR01GM055867 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LUNDBLAD, VICTORIA · 1997 to 2004
$1.4M
NIGMS NIH HHS GM55867NIGMS NIH HHS R01 GM055867
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, association between the Est1 telomerase subunit and the telomere-binding protein Cdc13 is essential for telomerase to be recruited to its site of action. A current model proposes that Tel1 binding to telomeres marks them for elongation, as the result of phosphorylation of a proposed S/TQ cluster in the telomerase recruitment domain of Cdc13. However, three observations presented here argue against one key aspect of this model. First, the pattern of Cdc13 phosphatase-sensitive isoforms is not altered by loss of Tel1 function or by mutations introduced into two conserved serines (S249 and S255) in the Cdc13 recruitment domain. Second, an interaction between Cdc13 and Est1, as monitored by a two-hybrid assay, is dependent on S255 but Tel1-independent. Finally, a derivative of Cdc13, cdc13-(S/TQ)11→(S/TA)11, in which every potential consensus phosphorylation site for Tel1 has been eliminated, confers nearly wild-type telomere length. These results are inconsistent with a model in which the Cdc13-Est1 interaction is regulated by Tel1-mediated phosphorylation of the Cdc13 telomerase recruitment domain. We propose an alternative model for the role of Tel1 in telomere homeostasis, which is based on the assumption that Tel1 performs the same molecular task at double-strand breaks (DSBs) and chromosome termini.

Indexed as

HemostasisIntracellular Signaling Peptides and ProteinsPhosphorylationProtein BindingProtein IsoformsProtein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomeraseTelomereTelomere-Binding ProteinsCdc13 protein, S cerevisiaeEST1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsProtein IsoformsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTEL1 protein, S cerevisiaeTelomeraseTelomere-Binding Proteins

Identifiers

PMID20837994
PMCPMC2998300
OpenAlexW2002934655

What OpenQuestion holds

Textmetadata
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.