Evidence map›Paper›PMID 19696030›Full record

ArticleThe Journal of biological chemistry2009

Novel LC8 mutations have disparate effects on the assembly and stability of flagellar complexes.

Pinfen Yang, Chun Yang, Maureen Wirschell, Stephanie Davis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Sequential assembly of flagellar radial spokes.Cytoskeleton (Hoboken, N.J.) · 2011
    Article
  10. Article
  11. 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.

Pinfen YangDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53233, USA. pinfen.yang@marquette.edu
Chun Yang
Maureen Wirschell
Stephanie Davis
Marquette University · USEmory University · US

Funding

REGULATION OF DYNEIN-DRIVEN FLAGELLAR MOTILITYR01GM068101 · NIGMS · MARQUETTE UNIVERSITY · PI YANG, PINFEN · 2003 to 2009
$1.3M
Targeted and regulation of flagellar dyneinF32GM075446 · NIGMS · EMORY UNIVERSITY · PI WIRSCHELL, MAUREEN E · 2005 to 2007
$143k
NIGMS NIH HHS F32 GM075446NIGMS NIH HHS GM068101NIGMS NIH HHS GM075446NIGMS NIH HHS R01 GM068101
6 · The paper itself

Abstract

LC8 functions as a dimer crucial for a variety of molecular motors and non-motor complexes. Emerging models, founded on structural studies, suggest that the LC8 dimer promotes the stability and refolding of dimeric target proteins in molecular complexes, and its interactions with selective target proteins, including dynein subunits, is regulated by LC8 phosphorylation, which is proposed to prevent LC8 dimerization. To test these hypotheses in vivo, we determine the impacts of two new LC8 mutations on the assembly and stability of defined LC8-containing complexes in Chlamydomonas flagella. The three types of dyneins and the radial spoke are disparately affected by dimeric LC8 with a C-terminal extension. The defects include the absence of specific subunits, complex instability, and reduced incorporation into the axonemal super complex. Surprisingly, a phosphomimetic LC8 mutation, which is largely monomeric in vitro, is still dimeric in vivo and does not significantly change flagellar generation and motility. The differential defects in these flagellar complexes support the structural model and indicate that modulation of target proteins by LC8 leads to the proper assembly of complexes and ultimately higher level complexes. Furthermore, the ability of flagellar complexes to incorporate the phosphomimetic LC8 protein and the modest defects observed in the phosphomimetic LC8 mutant suggest that LC8 phosphorylation is not an effective mechanism for regulating molecular complexes.

Indexed as

MutationAlgal ProteinsChlamydomonasDimerizationFlagellaMolecular Motor ProteinsProtein StabilityAlgal ProteinsMolecular Motor Proteins

Identifiers

PMID19696030
PMCPMC2781537
OpenAlexW2083651192

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.