Evidence map›Paper›PMID 10781063›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination.

V N Podust, J E Brownell, T B Gladysheva, R S Luo, C Wang, M B Coggins, J W Pierce, E S Lightcap, V Chau

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

102 citing papers in PubMed, 243 citations in OpenAlex.

  1. Review
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  5. Quantitative analyses for effects of neddylation on CRL2Protein science : a publication of the Protein Society · 2021
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  18. Inhibition of atherogenesis by the COP9 signalosome subunit 5 in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  20. Article

42 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 1 country.

V N PodustDepartment of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
J E Brownell
T B Gladysheva
R S Luo
C Wang
M B Coggins
J W Pierce
E S Lightcap
V Chau
KalVista Pharmaceuticals (United States) · USPenn State Milton S. Hershey Medical Center · USPennsylvania State University · US

Funding

STRUCTURE/FUNCTION OF UBIQUITIN CONJUGATING ENZYMESR01GM053136 · NIGMS · WAYNE STATE UNIVERSITY · PI CHAU, VINCENT · 1996 to 1999
–
NIGMS NIH HHS GM53136
6 · The paper itself

Abstract

Temporal control of p27(Kip1) (p27) degradation imposes periodicity in its activity during cell cycle progression and its accumulation during cell cycle exit. Degradation of p27 is initiated by phosphorylation of p27 at Thr-187, which marks the protein for ubiquitination by SCF(Skp2) and subsequent proteolysis by the 26S proteasome. Here we show that the p27 ubiquitination activity in cell extracts depends on the presence of the ubiquitin-like protein Nedd8 and enzymes that catalyze Nedd8 conjugation to proteins. Moreover, we show that reconstitution of the p27 ubiquitination activity of recombinant SCF(Skp2) also requires Nedd8 conjugation pathway components. Inactivation of the Nedd8 conjugation pathway by a dominant negative mutant of the Nedd8-conjugating enzyme Nce1/Ubc12 blocks the ubiquitination and degradation of p27 in cell extracts. Consistent with a role in cell-cycle progression, Nedd8 is expressed in proliferating cells and is itself down-regulated upon cellular differentiation. These results suggest that the Nedd8 conjugation pathway may regulate the turnover of p27(Kip1), independently of p27 phosphorylation, and further establishes the identity of protein components involved in p27 ubiquitination. Finally, these findings provide a direct demonstration of a function for Nedd8 in a biological process.

Indexed as

CDC2-CDC28 KinasesCell Cycle ProteinsTumor Suppressor ProteinsUbiquitin-Protein Ligase ComplexesAmino Acid SubstitutionAnaphase-Promoting Complex-CyclosomeBinding SitesCatalytic DomainCyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p27Cyclin-Dependent KinasesCyclin ECysteineEnzyme InhibitorsEscherichia coliHeLa CellsAnaphase-Promoting Complex-CyclosomeCDC2-CDC28 KinasesCDK2 protein, humanCell Cycle ProteinsCyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p27Cyclin-Dependent KinasesCyclin ECysteineEnzyme InhibitorsLigasesMicrotubule-Associated ProteinsNEDD8 ProteinNEDD8 protein, humanProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSerineTumor Suppressor ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID10781063
PMCPMC18275
OpenAlexW1994755995

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.