Evidence map›Paper›PMID 28143933›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Filopodia formation and endosome clustering induced by mutant plus-end-directed myosin VI.

Thomas A Masters, Folma Buss

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  3. The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025
    Article
  4. Variants inGenetics in medicine open · 2025
    Article
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  7. The twoFrontiers in physiology · 2024
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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.

Thomas A MastersCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom fb207@cam.ac.uk tam55@cam.ac.uk.
Folma BussCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom fb207@cam.ac.uk tam55@cam.ac.uk.
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K001981/1Wellcome TrustWellcome Trust 093026Wellcome Trust 100140
6 · The paper itself

Abstract

Myosin VI (MYO6) is the only myosin known to move toward the minus end of actin filaments. It has roles in numerous cellular processes, including maintenance of stereocilia structure, endocytosis, and autophagosome maturation. However, the functional necessity of minus-end-directed movement along actin is unclear as the underlying architecture of the local actin network is often unknown. To address this question, we engineered a mutant of MYO6, MYO6+, which undergoes plus-end-directed movement while retaining physiological cargo interactions in the tail. Expression of this mutant motor in HeLa cells led to a dramatic reorganization of cortical actin filaments and the formation of actin-rich filopodia. MYO6 is present on peripheral adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (APPL1) signaling endosomes and MYO6+ expression causes a dramatic relocalization and clustering of this endocytic compartment in the cell cortex. MYO6+ and its adaptor GAIP interacting protein, C terminus (GIPC) accumulate at the tips of these filopodia, while APPL1 endosomes accumulate at the base. A combination of MYO6+ mutagenesis and siRNA-mediated depletion of MYO6 binding partners demonstrates that motor activity and binding to endosomal membranes mediated by GIPC and PI(4,5)P

Indexed as

Actin CytoskeletonActinsAdaptor Proteins, Signal TransducingCell MembraneEndocytosisEndosomesHeLa CellsHumansMicroscopy, ConfocalMutationMyosin Heavy ChainsProtein TransportPseudopodiaTime-Lapse ImagingActinsAdaptor Proteins, Signal TransducingAPPL1 protein, humanMyosin Heavy Chainsmyosin VIactin dynamicsendosomesfilopodiamotor–cargo complexesunconventional myosins

Identifiers

PMID28143933
PMCPMC5320995
OpenAlexW2583133828

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.