Evidence map›Paper›PMID 12198158›Full record

ArticleThe EMBO journal2002

A novel cGMP signalling pathway mediating myosin phosphorylation and chemotaxis in Dictyostelium.

Leonard Bosgraaf, Henk Russcher, Janet L Smith, Deborah Wessels, David R Soll, Peter J M Van Haastert

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.7field-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

65 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
  2. Spontaneous signal generation by an excitable system for cell migration.Frontiers in cell and developmental biology · 2024
    Review
  3. Analysis of cGMP Signaling in Dictyostelium.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Review
  6. Forty-five years of cGMP research inMolecular biology of the cell · 2021
    Review
  7. Frontiers in cellular neuroscience · 2021
    Review
  8. Article
  9. Article
  10. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  11. Roco Proteins and the Parkinson's Disease-Associated LRRK2.International journal of molecular sciences · 2018
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

5 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

6 authors at 1 institution in 1 country.

Leonard BosgraafDepartment of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Henk Russcher
Janet L Smith
Deborah Wessels
David R Soll
Peter J M Van Haastert
University of Groningen · NL

Funding

VIDEO LABORATORY FOR ANALYSIS OF CELL BEHAVIORP01HD018577 · NICHD · UNIVERSITY OF IOWA · PI VOSS, EDWARD R · 1985 to 2006
$5.1M
NICHD NIH HHS HD-18577NICHD NIH HHS P01 HD018577
6 · The paper itself

Abstract

Chemotactic stimulation of Dictyostelium cells results in a transient increase in cGMP levels, and transient phosphorylation of myosin II heavy and regulatory light chains. In Dictyostelium, two guanylyl cyclases and four candidate cGMP-binding proteins (GbpA- GbpD) are implicated in cGMP signalling. GbpA and GbpB are homologous proteins with a Zn2+-hydrolase domain. A double gbpA/gbpB gene disruption leads to a reduction of cGMP-phosphodiesterase activity and a 10-fold increase of basal and stimulated cGMP levels. Chemotaxis in gbpA(-)B(-) cells is associated with increased myosin II phosphorylation compared with wild-type cells; formation of lateral pseudopodia is suppressed resulting in enhanced chemotaxis. GbpC is homologous to GbpD, and contains Ras, MAPKKK and Ras-GEF domains. Inactivation of the gbp genes indicates that only GbpC harbours high affinity cGMP-binding activity. Myosin phosphorylation, assembly of myosin in the cytoskeleton as well as chemotaxis are severely impaired in mutants lacking GbpC and GbpD, or mutants lacking both guanylyl cyclases. Thus, a novel cGMP signalling cascade is critical for chemotaxis in Dictyostelium, and plays a major role in myosin II regulation during this process.

Indexed as

Intracellular Signaling Peptides and Proteins3',5'-Cyclic-AMP PhosphodiesterasesAnimalsCarrier ProteinsChemotaxisCyclic GMPCytoskeletonDictyosteliumGuanylate CyclaseMyosin Type IIPhosphorylationProtein Processing, Post-TranslationalProtozoan ProteinsSecond Messenger Systems3',5'-Cyclic-AMP PhosphodiesterasesCarrier ProteinsCyclic GMPcyclic GMP-binding proteinGuanylate CyclaseIntracellular Signaling Peptides and ProteinsMyosin Type IIProtozoan Proteins

Identifiers

PMID12198158
PMCPMC126179
OpenAlexW2046508710

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.