Evidence map›Paper›PMID 8522584›Full record

ArticleThe Journal of cell biology1995

Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis.

K D Novak, M D Peterson, M C Reedy, M A Titus

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025
    Article
  3. Procedures to Measure Dictyostelium Phagocytosis and Macropinocytosis.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Shaping the intestinal brush border.The Journal of cell biology · 2014
    Review
  18. Article
  19. Article
  20. Article

17 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

4 authors at 3 institutions in 1 country.

K D NovakDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
M D Peterson
M C Reedy
M A Titus
Duke University Hospital · USDuke Medical Center · USDuke University · US

Funding

Myofibrillar Structure of Striated MuscleR37AR014317 · NIAMS · DUKE UNIVERSITY · PI REEDY, MICHAEL KAY · 2001 to 2010
$5.0M
MYOFIBRILLAR STRUCTURE OF STRIATED MUSCLER01AR014317 · NIAMS · DUKE UNIVERSITY · PI EDWARDS, ROBERT JON · 1986 to 2016
$2.1M
NIAMS NIH HHS AR14317-22
6 · The paper itself

Abstract

The functional relationship between three Dictyostelium myosin Is, myoA, myoB, and myoC, has been examined through the creation of double mutants. Two double mutants, myoA-/B- and myoB-/C-, exhibit similar conditional defects in fluid-phase pinocytosis. Double mutants grown in suspension culture are significantly impaired in their ability to take in nutrients from the medium, whereas they are almost indistinguishable from wild-type and single mutant strains when grown on a surface. The double mutants are also found to internalize gp126, a 116-kD membrane protein, at a slower rate than either the wild-type or single mutant cells. Ultrastructural analysis reveals that both double mutants possess numerous small vesicles, in contrast to the wild-type or myosin I single mutants that exhibit several large, clear vacuoles. The alterations in fluid and membrane internalization in the suspension-grown double mutants, coupled with the altered vesicular profile, suggest that these cells may be compromised during the early stages of pinocytosis, a process that has been proposed to occur via actin-based cytoskeletal rearrangements. Scanning electron microscopy and rhodamine-phalloidin staining indicates that the myosin I double mutants appear to extend a larger number of actin-filled structures, such as filopodia and crowns, than wild-type cells. Rhodamine-phalloidin staining of the F-actin cytoskeleton of these suspension-grown cells also reveals that the double mutant cells are delayed in the rearrangement of cortical actin-rich structures upon adhesion to a substrate. We propose that myoA, myoB, and myoC play roles in controlling F-actin filled membrane projections that are required for pinosome internalization in suspension.

Indexed as

Myosin Type IActinsAnimalsDictyosteliumFungal ProteinsMutagenesisMyosinsPinocytosisProtozoan ProteinsVacuolesActinsFungal ProteinsMyoA protein, Aspergillus nidulansMyosinsMyosin Type IProtozoan Proteins

Identifiers

PMID8522584
PMCPMC2120646
OpenAlexW2127601291

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.