Evidence map›Paper›PMID 17451552›Full record

ArticleTraffic (Copenhagen, Denmark)2007

The ternary Rab27a-Myrip-Myosin VIIa complex regulates melanosome motility in the retinal pigment epithelium.

Vanda S Lopes, José S Ramalho, Dylan M Owen, Mike O Karl, Olaf Strauss, Clare E Futter, Miguel C Seabra

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 92 citations in OpenAlex.

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  12. The cell biology of the retinal pigment epithelium.Progress in retinal and eye research · 2020
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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

7 authors at 4 institutions in 3 countries.

Vanda S LopesMolecular and Cellular Medicine, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK.
José S Ramalho
Dylan M Owen
Mike O Karl
Olaf Strauss
Clare E Futter
Miguel C Seabra
Imperial College London · GBUniversität Hamburg · DEAssociation for Innovation and Biomedical Research on Light and Image · PTUniversity College London · GB

Funding

Wellcome Trust 075498
6 · The paper itself

Abstract

The retinal pigment epithelium (RPE) contains melanosomes similar to those found in the skin melanocytes, which undergo dramatic light-dependent movements in fish and amphibians. In mammals, those movements are more subtle and appear to be regulated by the Rab27a GTPase and the unconventional myosin, Myosin VIIa (MyoVIIa). Here we address the hypothesis that a recently identified Rab27a- and MyoVIIa-interacting protein, Myrip, promotes the formation of a functional tripartite complex. In heterologous cultured cells, all three proteins co-immunoprecipitated following overexpression. Rab27a and Myrip localize to the peripheral membrane of RPE melanosomes as observed by immunofluorescence and immunoelectron microscopy. Melanosome dynamics were studied using live-cell imaging of mouse RPE primary cultures. Wild-type RPE melanosomes exhibited either stationary or slow movement interrupted by bursts of fast movement, with a peripheral directionality trend. Nocodazole treatment led to melanosome paralysis, suggesting that movement requires microtubule motors. Significant and similar alterations in melanosome dynamics were observed when any one of the three components of the complex was missing, as studied in ashen- (Rab27a defective) and shaker-1 (MyoVIIa mutant)-derived RPE cells, and in wild-type RPE cells transduced with adenovirus carrying specific sequences to knockdown Myrip expression. We observed a significant increase in the number of motile melanosomes, exhibiting more frequent and prolonged bursts of fast movement, and inversion of directionality. Similar alterations were observed upon cytochalasin D treatment, suggesting that the Rab27a-Myrip-MyoVIIa complex regulates tethering of melanosomes onto actin filaments, a process that ensures melanosome movement towards the cell periphery.

Indexed as

ActinsAnimalsBiological TransportCells, CulturedChlorocebus aethiopsCOS CellsCytochalasin DDyneinsEpithelial CellsImmunoprecipitationMelanosomesMiceMice, Inbred C57BLMice, KnockoutMyosinsMyosin VIIaActinsCytochalasin DDyneinsMyo7a protein, mouseMyosinsMyosin VIIaMYRIP protein, mouseNocodazoleRab27a protein, mouserab27 GTP-Binding Proteinsrab GTP-Binding ProteinsRNA, AntisenseVesicular Transport Proteins

Identifiers

PMID17451552
PMCPMC1920545
OpenAlexW2151326094

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.