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Molecular basis of Pirh2-mediated p53 ubiquitylation

Overview of attention for article published in Nature Structural & Molecular Biology, November 2008
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Title
Molecular basis of Pirh2-mediated p53 ubiquitylation
Published in
Nature Structural & Molecular Biology, November 2008
DOI 10.1038/nsmb.1521
Pubmed ID
Authors

Yi Sheng, Rob C Laister, Alexander Lemak, Bin Wu, Elizabeth Tai, Shili Duan, Jonathan Lukin, Maria Sunnerhagen, Sampath Srisailam, Murthy Karra, Sam Benchimol, Cheryl H Arrowsmith

Abstract

Pirh2 (p53-induced RING-H2 domain protein; also known as Rchy1) is an E3 ubiquitin ligase involved in a negative-feedback loop with p53. Using NMR spectroscopy, we show that Pirh2 is a unique cysteine-rich protein comprising three modular domains. The protein binds nine zinc ions using a variety of zinc coordination schemes, including a RING domain and a left-handed beta-spiral in which three zinc ions align three consecutive small beta-sheets in an interleaved fashion. We show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. As a result, Pirh2 preferentially ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting that Pirh2 regulates protein turnover of the transcriptionally active form of p53.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 58 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Switzerland 1 2%
France 1 2%
India 1 2%
Canada 1 2%
Singapore 1 2%
Unknown 53 91%

Demographic breakdown

Readers by professional status Count As %
Researcher 12 21%
Student > Ph. D. Student 9 16%
Student > Bachelor 6 10%
Student > Master 5 9%
Professor > Associate Professor 4 7%
Other 7 12%
Unknown 15 26%
Readers by discipline Count As %
Agricultural and Biological Sciences 26 45%
Biochemistry, Genetics and Molecular Biology 11 19%
Medicine and Dentistry 3 5%
Pharmacology, Toxicology and Pharmaceutical Science 2 3%
Chemistry 1 2%
Other 0 0%
Unknown 15 26%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 July 2009.
All research outputs
#8,534,528
of 25,373,627 outputs
Outputs from Nature Structural & Molecular Biology
#2,602
of 4,186 outputs
Outputs of similar age
#51,400
of 179,190 outputs
Outputs of similar age from Nature Structural & Molecular Biology
#13
of 29 outputs
Altmetric has tracked 25,373,627 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 4,186 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 15.5. This one is in the 20th percentile – i.e., 20% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 179,190 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 18th percentile – i.e., 18% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 29 others from the same source and published within six weeks on either side of this one. This one is in the 24th percentile – i.e., 24% of its contemporaries scored the same or lower than it.