Evidence map›Paper›PMID 16782883›Full record

ArticleMolecular and cellular biology2006

Distinct functional domains of Ubc9 dictate cell survival and resistance to genotoxic stress.

Robert C A M van Waardenburg, David M Duda, Cynthia S Lancaster, Brenda A Schulman, Mary-Ann Bjornsti

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Robert C A M van WaardenburgDept. of Molecular Pharmacology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105, USA.
David M Duda
Cynthia S Lancaster
Brenda A Schulman
Mary-Ann Bjornsti
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
XENOGRAFT STUDIESP01CA023099 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HOUGHTON, PETER J · 1985 to 2011
$22.4M
Ubiquitin-like Protein Transfer CascadesR01GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2013
$3.4M
E3-mediated Ubiquitin-like Protein LigationR37GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2014 to 2018
$2.0M
SUMOylation and Cell Sensitivity to Top1 PoisonsR01CA111542 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BJORNSTI, MARY-ANN · 2005 to 2009
$1.4M
NCI NIH HHS CA111542NCI NIH HHS CA21765NCI NIH HHS CA23099NCI NIH HHS P01 CA023099NCI NIH HHS P30 CA021765NCI NIH HHS R01 CA111542NIGMS NIH HHS GM069530NIGMS NIH HHS R01 GM069530NIGMS NIH HHS R37 GM069530
6 · The paper itself

Abstract

Covalent modification with SUMO alters protein function, intracellular localization, or protein-protein interactions. Target recognition is determined, in part, by the SUMO E2 enzyme, Ubc9, while Siz/Pias E3 ligases may facilitate select interactions by acting as substrate adaptors. A yeast conditional Ubc9P(123)L mutant was viable at 36 degrees C yet exhibited enhanced sensitivity to DNA damage. To define functional domains in Ubc9 that dictate cellular responses to genotoxic stress versus those necessary for cell viability, a 1.75-A structure of yeast Ubc9 that demonstrated considerable conservation of backbone architecture with human Ubc9 was solved. Nevertheless, differences in side chain geometry/charge guided the design of human/yeast chimeras, where swapping domains implicated in (i) binding residues within substrates that flank canonical SUMOylation sites, (ii) interactions with the RanBP2 E3 ligase, and (iii) binding of the heterodimeric E1 and SUMO had distinct effects on cell growth and resistance to DNA-damaging agents. Our findings establish a functional interaction between N-terminal and substrate-binding domains of Ubc9 and distinguish the activities of E3 ligases Siz1 and Siz2 in regulating cellular responses to genotoxic stress.

Indexed as

DNA DamageAmino Acid SequenceHumansMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein LigasesX-Ray DiffractionRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSiz1 protein, S cerevisiaeSiz2 protein, S cerevisiaeUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligases

Identifiers

PMID16782883
PMCPMC1489148
OpenAlexW1985483685

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.