ArticleJournal of muscle research and cell motility2006
Drosophila rolling pebbles colocalises and putatively interacts with alpha-Actinin and the Sls isoform Zormin in the Z-discs of the sarcomere and with Dumbfounded/Kirre, alpha-Actinin and Zormin in the terminal Z-discs.
Article in Journal of muscle research and cell motility, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Shared Disease Mechanisms in Neurodevelopmental Disorders: A Cellular and Molecular Biology Perspective.Brain sciences · 2025Review
- Transcriptome analysis identified long non-coding RNAs involved in the adaption of yak to high-altitude environments.Royal Society open science · 2020Article
- Kirrel3-Mediated Synapse Formation Is Attenuated by Disease-Associated Missense Variants.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Review
- Myotube migration to cover and shape the testis ofBiology open · 2017Article
- A new level of plasticity: Drosophila smooth-like testes muscles compensate failure of myoblast fusion.Development (Cambridge, England) · 2016Article
- Elastic proteins in the flight muscle of Manduca sexta.Archives of biochemistry and biophysics · 2015Article
- Article
- Distinct genetic programs guide Drosophila circular and longitudinal visceral myoblast fusion.BMC cell biology · 2014Article
- The function of the M-line protein obscurin in controlling the symmetry of the sarcomere in the flight muscle of Drosophila.Journal of cell science · 2012Article
- Article
- Characterisation of the role of Vrp1 in cell fusion during the development of visceral muscle of Drosophila melanogaster.BMC developmental biology · 2010Article
- Bringing together components of the fly renal system.Current opinion in genetics & development · 2009Review
- Article
- Tethering membrane fusion: common and different players in myoblasts and at the synapse.Journal of neurogeneticsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rolling pebbles gene of Drosophila encodes two proteins, one of which, Rols7, is essential for myoblast fusion. In addition, Rols 7 is expressed during myofibrillogenesis and in the mature muscles. Here it overlaps with alpha-Actinin (alpha-Actn) and the N-terminus of D-Titin/Kettin/Zormin in the Z-line of the sarcomeres. In the attachment sites of the somatic muscles, Rols7 and the immunoglobulin superfamily protein Dumbfounded/Kin of irreC (Duf/Kirre) colocalise. As Duf/Kirre is detectable only transiently, it may be involved in establishing the first contact of the outgrowing muscle fiber to the epidermal attachment site. We propose that Rols7 and Duf/Kirre link the terminal Z-disc to the cell membrane by direct interaction. This is supported by the fact that in yeast two hybrid assays the tetratricopeptide repeat E (TPR E) of Rols7 shows interaction with the intracellular domain of Duf/Kirre. The colocalisation of Rols7 with alpha-Actn and with D-Titin/Kettin/Zormin in the Z-dics is reflected in interactions with different domains of Rols7 in this assay. In summary, these data show that besides the role in myoblast fusion, Rols7 is a scaffold protein during myofibrillogenesis and in the Z-line of the sarcomere as well as in the terminal Z-disc linking the muscle to the epidermal attachment sites.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.