Evidence map›Paper›PMID 33526451›Full record

ArticleMolecular and cellular biology2021

SUMOylation- and GAR1-Dependent Regulation of Dyskerin Nuclear and Subnuclear Localization.

D E MacNeil, P Lambert-Lanteigne, J Qin, F P McManus, E Bonneil, P Thibault, C Autexier

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Advances in understanding telomerase assembly.Biochemical Society transactions · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
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

7 authors at 2 institutions in 1 country.

D E MacNeilLady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montréal, Quebec, Canada.
P Lambert-Lanteigne *Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montréal, Quebec, Canada.
J Qin *Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montréal, Quebec, Canada.
F P McManusUniversité de Montréal, Montréal, Quebec, Canada.
E BonneilUniversité de Montréal, Montréal, Quebec, Canada.
P ThibaultUniversité de Montréal, Montréal, Quebec, Canada.
C AutexierLady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montréal, Quebec, Canada chantal.autexier@mcgill.ca.ORCID 0000-0002-7201-0975
Jewish General Hospital · CAUniversité de Montréal · CA

Funding

CIHR PJT-166130
6 · The paper itself

Abstract

The nuclear and subnuclear compartmentalization of the telomerase-associated protein and H/ACA ribonucleoprotein component dyskerin is an important although incompletely understood aspect of H/ACA ribonucleoprotein function. Four SUMOylation sites were previously identified in the C-terminal nuclear/nucleolar localization signal (N/NoLS) of dyskerin. We found that a cytoplasmic localized C-terminal truncation variant of dyskerin lacking most of the C-terminal N/NoLS represents an under-SUMOylated variant of dyskerin compared to wild-type dyskerin. We demonstrate that mimicking constitutive SUMOylation of dyskerin using a SUMO3 fusion construct can drive nuclear accumulation of this variant and that the SUMO site K467 in this N/NoLS is particularly important for the subnuclear localization of dyskerin to the nucleolus in a mature H/ACA complex assembly- and SUMO-dependent manner. We also characterize a novel SUMO-interacting motif in the mature H/ACA complex component GAR1 that mediates the interaction between dyskerin and GAR1. Mislocalization of dyskerin, either in the cytoplasm or excluded from the nucleolus, disrupts dyskerin function and leads to reduced interaction of dyskerin with the telomerase RNA. These data indicate a role for dyskerin C-terminal N/NoLS SUMOylation in regulating the nuclear and subnuclear localization of dyskerin, which is essential for dyskerin function as both a telomerase-associated protein and as an H/ACA ribonucleoprotein.

Indexed as

Cell Cycle ProteinsCell NucleusCytoplasmDyskeratosis CongenitaHumansNuclear Localization SignalsNuclear ProteinsRibonucleoproteins, Small NucleolarRNARNA-Binding ProteinsSumoylationTelomeraseCell Cycle ProteinsGAR1 protein, humanNuclear Localization SignalsNuclear ProteinsRibonucleoproteins, Small NucleolarRNARNA-Binding ProteinsTelomerasetelomerase RNAdyskerinGAR1nuclear localizationsubnuclear localizationSUMOylationtelomerase

Identifiers

PMID33526451
PMCPMC8088130
OpenAlexW3128977685

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.