Evidence map›Paper›PMID 18946044›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade.

Antonio A Iniesta, Lucy Shapiro

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. A localized adaptor protein performs distinct functions at theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016
    Review
  16. In-phase oscillation of global regulons is orchestrated by a pole-specific organizer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Dynamic translation regulation in Caulobacter cell cycle control.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  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

2 authors at 1 institution in 1 country.

Antonio A IniestaDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Lucy Shapiro
Stanford University · US

Funding

REGULATION OF DIFFERENTIATION IN CAULOBACTERR01GM032506 · NIGMS · YESHIVA UNIVERSITY · PI SHAPIRO, LUCILLE · 1985 to 2014
$7.1M
REGULATION OF DIFFERENTIATION IN CAULOBACTERR37GM032506 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 1993 to 2002
$1.4M
NIGMS NIH HHS GM32506NIGMS NIH HHS R01 GM032506NIGMS NIH HHS R37 GM032506
6 · The paper itself

Abstract

Dynamic protein localization is an integral component of the regulatory circuit that drives the Caulobacter cell cycle. The ClpXP protease is localized to the Caulobacter cell pole, where it catalyzes the degradation of the CtrA master regulator at specific times in the cell cycle. Clearance of active CtrA at the G1/S transition allows the initiation of DNA replication and cell-cycle progression. The polar localization of ClpXP is dependent on the polar positioning of the CpdR single-domain response regulator. Only the unphosphorylated form of CpdR localizes and activates ClpXP. We demonstrate that another single domain response regulator, DivK, promotes the polar accumulation of unphosphorylated CpdR and that CpdR is subsequently degraded at the cell pole by the localized ClpXP protease. Thus, CpdR function is regulated by a feedback loop that incorporates its differential phosphorylation, the transient polar localization and activity of the ClpXP protease, and the clearance of the CpdR by polar ClpXP that, in turn, releases ClpXP from the pole relieving the degradation of CtrA. CtrA approximately P then accumulates and activates the transcription of cpdR, completing the regulatory loop, establishing an integrated network that controls a robust cell-cycle transition.

Indexed as

Cell CycleSignal TransductionBacterial ProteinsCaulobacterEndopeptidase ClpPhosphorylationSystems BiologyBacterial ProteinsDivK protein, Caulobacter crescentusEndopeptidase Clp

Identifiers

PMID18946044
PMCPMC2575466
OpenAlexW2019650206

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.