Evidence map›Paper›PMID 24989075›Full record

ArticleMolecular microbiology2014

ClpXP and ClpAP proteolytic activity on divisome substrates is differentially regulated following the Caulobacter asymmetric cell division.

Brandon Williams, Nowsheen Bhat, Peter Chien, Lucy Shapiro

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  7. Review
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  13. The Protein Quality Control Network inFrontiers in molecular biosciences · 2021
    Review
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  18. Article
  19. Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018
    Review
  20. Reduction in adaptor amounts establishes degradation hierarchy among protease substrates.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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 2 institutions in 1 country.

Brandon WilliamsDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Nowsheen Bhat
Peter Chien
Lucy Shapiro
Stanford University · USUniversity of Massachusetts Amherst · US

Funding

GENETICS TRAINING PROGRAM FOR PHD CANDIDATEST32GM007790 · NIGMS · STANFORD UNIVERSITY · PI BRUNET, ANNE, KINGSLEY, DAVID M · 1985 to 2020
$12.8M
REGULATION OF DIFFERENTIATION IN CAULOBACTERR01GM032506 · NIGMS · YESHIVA UNIVERSITY · PI SHAPIRO, LUCILLE · 1985 to 2014
$7.1M
Specificity, Regulation and Proteomic Profiling of an Essential AAA+ ProteaseR00GM084157 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHIEN, PETER · 2010 to 2012
$742k
NIGMS NIH HHS GM 07790NIGMS NIH HHS R00 GM084157NIGMS NIH HHS R00GM084157NIGMS NIH HHS R01 GM032506NIGMS NIH HHS R01GM 32506NIGMS NIH HHS T32 GM007790
6 · The paper itself

Abstract

Proteolytic control of Caulobacter cell cycle proteins is primarily executed by ClpXP, a dynamically localized protease implicated in turnover of several factors critical for faithful cell cycle progression. Here, we show that the transient midcell localization of ClpXP that precedes cytokinesis requires the FtsZ component of the divisome. Although ClpAP does not exhibit subcellular localization, FtsZ is a substrate of both ClpXP and ClpAP in vivo and in vitro. A peptide containing the C-terminal portion of the FtsA divisome protein is a substrate of both ClpXP and ClpAP in vitro but is primarily degraded by ClpAP in vivo. Caulobacter carries out an asymmetric division in which FtsZ and FtsA are stable in stalked cells but degraded in the non-replicative swarmer cell where ClpAP alone degrades FtsA and both ClpAP and ClpXP degrade FtsZ. While asymmetric division in Caulobacter normally yields larger stalked and smaller swarmer daughters, we observe a loss of asymmetric size distribution among daughter cells when clpA is depleted from a strain in which FtsZ is constitutively produced. Taken together, these results suggest that the activity of both ClpXP and ClpAP on divisome substrates is differentially regulated in daughter cells.

Indexed as

Asymmetric Cell DivisionBacterial ProteinsCaulobacterCytoskeletal ProteinsEndopeptidase ClpProteolysisSubstrate SpecificityBacterial ProteinsCytoskeletal ProteinsEndopeptidase ClpFtsZ protein, Bacteria

Identifiers

PMID24989075
PMCPMC4285227
OpenAlexW1874595510

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.