Evidence map›Paper›PMID 30699046›Full record

ArticleMolecular biology of the cell2019

The adaptor protein melanophilin regulates dynamic myosin-Va:cargo interaction and dendrite development in melanocytes.

Christopher L Robinson, Richard D Evans, Kajana Sivarasa, Jose S Ramalho, Deborah A Briggs, Alistair N Hume

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. 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
1.2field-weighted citation impact, top 24% 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, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Fusion partners of NTRK3 affect subcellular localization of the fusion kinase and cytomorphology of melanocytes.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2021
    Article
  8. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    Review
  9. Article
  10. Review
  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

6 authors at 2 institutions in 2 countries.

Christopher L RobinsonSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
Richard D EvansSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
Kajana SivarasaSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
Jose S RamalhoCEDOC Faculdade de Ciencias Medicas, Universidade Nova de Lisboa, 1169-056 Lisbon, Portugal.
Deborah A BriggsSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
Alistair N HumeSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, United Kingdom.
University of Nottingham · GBUniversidade Nova de Lisboa · PT

Funding

Medical Research Council G1100063
6 · The paper itself

Abstract

The regulation of organelle transport by the cytoskeleton is fundamental for eukaryotic survival. Cytoskeleton motors are typically modular proteins with conserved motor and diverse cargo-binding domains. Motor:cargo interactions are often indirect and mediated by adaptor proteins, for example, Rab GTPases. Rab27a, via effector melanophilin (Mlph), recruits myosin-Va (MyoVa) to melanosomes and thereby disperses them into melanocyte dendrites. To better understand how adaptors regulate motor:cargo interaction, we used single melanosome fluorescence recovery after photobleaching (smFRAP) to characterize the association kinetics among MyoVa, its adaptors, and melanosomes. We found that MyoVa and Mlph rapidly recovered after smFRAP, whereas Rab27a did not, indicating that MyoVa and Mlph dynamically associate with melanosomes and Rab27a does not. This suggests that dynamic Rab27a:effector interaction rather than Rab27a melanosome:cytosol cycling regulates MyoVa:melanosome association. Accordingly, a Mlph-Rab27a fusion protein reduced MyoVa smFRAP, indicating that it stabilized melanosomal MyoVa. Finally, we tested the functional importance of dynamic MyoVa:melanosome interaction. We found that whereas a MyoVa-Rab27a fusion protein dispersed melanosomes in MyoVa-deficient cells, dendrites were significantly less elongated than in wild-type cells. Given that dendrites are the prime sites of melanosome transfer from melanocytes to keratinocytes, we suggest that dynamic MyoVa:melanosome interaction is important for pigmentation in vivo.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBiological TransportCell Culture TechniquesCytoskeletonDendritesHumansMelanocytesMelanosomesMiceMyosin Heavy ChainsMyosin Type VProtein Bindingrab27 GTP-Binding Proteinsrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingMLPH protein, humanMYO5A protein, humanMyosin Heavy ChainsMyosin Type Vrab27 GTP-Binding Proteinsrab GTP-Binding Proteins

Identifiers

PMID30699046
PMCPMC6589771
OpenAlexW2912655665

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.