Evidence map›Paper›PMID 11553713›Full record

ArticleMolecular biology of the cell2001

Myosin Va bound to phagosomes binds to F-actin and delays microtubule-dependent motility.

A Al-Haddad, M A Shonn, B Redlich, A Blocker, J K Burkhardt, H Yu, J A Hammer, D G Weiss, W Steffen, G Griffiths and 1 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

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  18. Force measurements on cargoes in living cells reveal collective dynamics of microtubule motors.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Autonomous phagosomal degradation and antigen presentation in dendritic cells.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  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

11 authors.

A Al-HaddadInstitut für Zellbiologie und Biosystemtechnik, FB Biowissenschaften, Universität Rostock, D-18051 Rostock, Germany.
M A Shonn
B Redlich
A Blocker
J K Burkhardt
H Yu
J A Hammer
D G Weiss
W Steffen
G Griffiths
S A Kuznetsov

Funding

Structure And Function Of Unconventional Myosins and CARMIL ProteinsZIAHL000514 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI HAMMER, JOHN A · 2009 to 2018
$9.6M
THE STRUCTURE AND SEQUENCE OF NON-MUSCLE MYOSIN GENESZ01HL000514 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI HAMMER, JOHN A · 1985 to 2008
$4.7M
6 · The paper itself

Abstract

We established a light microscopy-based assay that reconstitutes the binding of phagosomes purified from mouse macrophages to preassembled F-actin in vitro. Both endogenous myosin Va from mouse macrophages and exogenous myosin Va from chicken brain stimulated the phagosome-F-actin interaction. Myosin Va association with phagosomes correlated with their ability to bind F-actin in an ATP-regulated manner and antibodies to myosin Va specifically blocked the ATP-sensitive phagosome binding to F-actin. The uptake and retrograde transport of phagosomes from the periphery to the center of cells in bone marrow macrophages was observed in both normal mice and mice homozygous for the dilute-lethal spontaneous mutation (myosin Va null). However, in dilute-lethal macrophages the accumulation of phagosomes in the perinuclear region occurred twofold faster than in normal macrophages. Motion analysis revealed saltatory phagosome movement with temporarily reversed direction in normal macrophages, whereas almost no reversals in direction were observed in dilute-lethal macrophages. These observations demonstrate that myosin Va mediates phagosome binding to F-actin, resulting in a delay in microtubule-dependent retrograde phagosome movement toward the cell center. We propose an "antagonistic/cooperative mechanism" to explain the saltatory phagosome movement toward the cell center in normal macrophages.

Indexed as

ActinsAdenosine TriphosphateAnimalsBrainCells, CulturedCell SizeChickensCytosolGene DeletionMacrophagesMiceMice, Mutant StrainsMicrofilament ProteinsMicroscopy, FluorescenceMicrospheresMicrotubulesActinsAdenosine TriphosphateMicrofilament ProteinsMyo5a protein, mouseMyosin Heavy ChainsMyosin Type V

Identifiers

PMID11553713
PMCPMC59709

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.