Evidence map›Paper›PMID 20969846›Full record

ArticleDevelopmental biology2011

Prolyl hydroxylation- and glycosylation-dependent functions of Skp1 in O2-regulated development of Dictyostelium.

Zhuo A Wang, Divyendu Singh, Hanke van der Wel, Christopher M West

Abstract read
In one paragraph

Article in Developmental biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

24 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Nucleocytoplasmic O-glycosylation in protists.Current opinion in structural biology · 2019
    Review
  10. Regulation of SCFRedox biology · 2018
    Article
  11. Article
  12. Article
  13. Oxygen sensing by protozoans: how they catch their breath.Current opinion in microbiology · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
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

4 authors at 1 institution in 1 country.

Zhuo A WangDepartment of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Divyendu Singh
Hanke van der Wel
Christopher M West
University of Oklahoma Health Sciences Center · US

Funding

Transfer of 5R01GM037539 - 22 CYTOSOLIC PROLINE HYDROXYLATION AND GLYCOSYLATIONR01GM037539 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI WEST, CHRISTOPHER M. · 1986 to 2016
$4.4M
Glycoregulation of Skp1 in the cytoplasm and nucleusR01GM084383 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI BLADER, IRA J, WEST, CHRISTOPHER M. · 2009 to 2018
$2.9M
NIGMS NIH HHS GM-37539NIGMS NIH HHS GM-84383NIGMS NIH HHS R01 GM037539NIGMS NIH HHS R01 GM084383
6 · The paper itself

Abstract

O(2) regulates multicellular development of the social amoeba Dictyostelium, suggesting it may serve as an important cue in its native soil environment. Dictyostelium expresses an HIFα-type prolyl 4-hydroxylase (P4H1) whose levels affect the O(2)-threshold for culmination implicating it as a direct O(2)-sensor, as in animals. But Dictyostelium lacks HIFα, a mediator of animal prolyl 4-hydroxylase signaling, and P4H1 can hydroxylate Pro143 of Skp1, a subunit of E3(SCF)ubiquitin-ligases. Skp1 hydroxyproline then becomes the target of five sequential glycosyltransferase reactions that modulate the O(2)-signal. Here we show that genetically induced changes in Skp1 levels also affect the O(2)-threshold, in opposite direction to that of the modification enzymes suggesting that the latter reduce Skp1 activity. Consistent with this, overexpressed Skp1 is poorly hydroxylated and Skp1 is the only P4H1 substrate detectable in extracts. Effects of Pro143 mutations, and of combinations of Skp1 and enzyme level perturbations, are consistent with pathway modulation of Skp1 activity. However, some effects were not mirrored by changes in modification of the bulk Skp1 pool, implicating a Skp1 subpopulation and possibly additional unknown factors. Altered Skp1 levels also affected other developmental transitions in a modification-dependent fashion. Whereas hydroxylation of animal HIFα results in its polyubiquitination and proteasomal degradation, Dictyostelium Skp1 levels were little affected by its modification status. These data indicate that Skp1 and possibly E3(SCF)ubiquitin-ligase activity modulate O(2)-dependent culmination and other developmental processes, and at least partially mediate the action of the hydroxylation/glycosylation pathway in O(2)-sensing.

Indexed as

Blotting, WesternDictyosteliumGene Expression Regulation, DevelopmentalGlycosylationHydroxylationLuminescent ProteinsMass SpectrometryMutationOxygenProcollagen-Proline DioxygenaseProlineS-Phase Kinase-Associated ProteinsUbiquitin-Protein LigasesLuminescent ProteinsOxygenProcollagen-Proline DioxygenaseProlineS-Phase Kinase-Associated ProteinsUbiquitin-Protein Ligases

Identifiers

PMID20969846
PMCPMC3095822
OpenAlexW2037963845

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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.