Evidence map›Paper›PMID 9008711›Full record

ArticleThe Journal of cell biology1997

Regulation of flagellar dynein by phosphorylation of a 138-kD inner arm dynein intermediate chain.

G Habermacher, W S Sale

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.6field-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

72 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.Nature structural & molecular biology · 2025
    Article
  3. Article
  4. Article
  5. Defective I1 dynein inmicroPublication biology · 2025
    Article
  6. The cAMP signaling module regulates sperm motility in the liverwortProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Single Cell in a Gravity Field.Life (Basel, Switzerland) · 2022
    Review
  10. Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  18. Review
  19. Review
  20. Article

12 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

2 authors at 1 institution in 1 country.

G HabermacherDepartment of Anatomy and Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
W S Sale
Emory University · US

Funding

Functional Substructure of Flagellar DyneinR37GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 2002 to 2011
$4.0M
FUNCTIONAL SUBSTRUCTURE OF FLAGELLAR DYNEINR01GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 1994 to 2020
$3.6M
NIGMS NIH HHS GM51173NIGMS NIH HHS R01 GM051173NIGMS NIH HHS R37 GM051173
6 · The paper itself

Abstract

One of the challenges in understanding ciliary and flagellar motility is determining the mechanisms that locally regulate dynein-driven microtubule sliding. Our recent studies demonstrated that microtubule sliding, in Chlamydomonas flagella, is regulated by phosphorylation. However, the regulatory proteins remain unknown. Here we identify the 138-kD intermediate chain of inner arm dynein I1 as the critical phosphoprotein required for regulation of motility. This conclusion is founded on the results of three different experimental approaches. First, genetic analysis and functional assays revealed that regulation of microtubule sliding, by phosphorylation, requires inner arm dynein I1. Second, in vitro phosphorylation indicated the 138-kD intermediate chain of I1 is the only phosphorylated subunit. Third, in vitro reconstitution demonstrated that phosphorylation and dephosphorylation of the 138-kD intermediate chain inhibits and restores wild-type microtubule sliding, respectively. We conclude that change in phosphorylation of the 138-kD intermediate chain of I1 regulates dynein-driven microtubule sliding. Moreover, based on these and other data, we predict that regulation of I1 activity is involved in modulation of flagellar waveform.

Indexed as

Intracellular Signaling Peptides and ProteinsAmino Acid SequenceAnimalsCarrier ProteinsChlamydomonas reinhardtiiDyneinsEnzyme InhibitorsFlagellaMarine ToxinsMicrocystinsMicrotubulesMolecular Sequence DataPeptide FragmentsPeptides, CyclicPhosphoprotein PhosphatasesPhosphoproteinsCarrier Proteinscyanoginosin LRDyneinsEnzyme InhibitorsIntracellular Signaling Peptides and ProteinsMarine ToxinsMicrocystinsPeptide FragmentsPeptides, CyclicPhosphoprotein PhosphatasesPhosphoproteinsprotein kinase inhibitor (6-22)-amideProtein Kinase Inhibitors

Identifiers

PMID9008711
PMCPMC2132463
OpenAlexW2155783111

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.