Evidence map›Paper›PMID 11259599›Full record

ArticleMolecular and cellular biology2001

F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat.

Y G Hsiung, H C Chang, J L Pellequer, R La Valle, S Lanker, C Wittenberg

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein Phosphatases in G1 Regulation.International journal of molecular sciences · 2020
    Review
  6. COmBio · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. PP2A(Cdc55) regulates G1 cyclin stability.Cell cycle (Georgetown, Tex.) · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 2 institutions in 1 country.

Y G HsiungDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
H C Chang
J L Pellequer
R La Valle
S Lanker
C Wittenberg
Scripps Research Institute · USOregon Health & Science University · US

Funding

ROLE OF CYCLINS IN CONTROL OF THE YEAST CELL CYCLER01GM043487 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WITTENBERG, CURT · 1990 to 2005
$2.0M
YEAST G1 CYCLIN DEGRADATION BY THE SCF UBIQUITIN LIGASER01GM059759 · NIGMS · OREGON HEALTH AND SCIENCE UNIVERSITY · PI MOSES, ROBB E · 1999 to 2003
$1.1M
NIGMS NIH HHS GM43487NIGMS NIH HHS GM59759NIGMS NIH HHS R01 GM043487NIGMS NIH HHS R01 GM059759
6 · The paper itself

Abstract

The flexibility and specificity of ubiquitin-dependent proteolysis are mediated, in part, by the E3 ubiquitin ligases. One class of E3 enzymes, SKp1/cullin/F-box protein (SCF), derives its specificity from F-box proteins, a heterogeneous family of adapters for target protein recognition. Grr1, the F-box component of SCF(Grr1), mediates the interaction with phosphorylated forms of the G(1) cyclins Cln1 and Cln2. We show that binding of Cln2 by SCF(Grr1) was dependent upon its leucine-rich repeat (LRR) domain and its carboxy terminus. Our structural model for the Grr1 LRR predicted a high density of positive charge on the concave surface of the characteristic horseshoe structure. We hypothesized that specific basic residues on the predicted concave surface are important for recognition of phosphorylated Cln2. We show that point mutations that converted the basic residues on the concave surface but not those on the convex surface to neutral or acidic residues interfered with the capacity of Grr1 to bind to Cln2. The same mutations resulted in the stabilization of Cln2 and Gic2 and also in a spectrum of phenotypes characteristic of inactivation of GRR1, including hyperpolarization and enhancement of pseudohyphal growth. It was surprising that the same residues were not important for the role of Grr1 in nutrient-regulated transcription of HXT1 or AGP1. We concluded that the cationic nature of the concave surface of the Grr1 LRR is critical for the recognition of phosphorylated targets of SCF(Grr1) but that other properties of Grr1 are required for its other functions.

Indexed as

Carrier ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesAmino Acid SequenceBinding SitesCyclinsF-Box ProteinsFungal ProteinsLeucine-Rich Repeat ProteinsMolecular Sequence DataPhosphorylationProtein BindingProteinsSaccharomyces cerevisiaeCarrier ProteinsCLN1 protein, S cerevisiaeCLN2 protein, S cerevisiaeCyclinsF-Box ProteinsFungal ProteinsGRR1 protein, S cerevisiaeLeucine-Rich Repeat ProteinsProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID11259599
PMCPMC86883
OpenAlexW2108599821

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.