ArticleScientific reports2016
Identification of novel MYO18A interaction partners required for myoblast adhesion and muscle integrity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
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- Golgi dispersal in cancer stem cells promotes chemoresistance of colorectal cancer via the Golgi stress response.Cell death & disease · 2024Article
- Are the class 18 myosins Myo18A and Myo18B specialist sarcomeric proteins?Frontiers in physiology · 2024Review
- THUMPD3 regulates alternative splicing of ECM transcripts in human lung cancer cells and promotes proliferation and migration.PloS one · 2024Article
- The Adaptor Protein Lurap1 Is Required for Cell Cohesion during Epiboly Movement in Zebrafish.Biology · 2021Article
- Cutting Edge: Myosin 18A Is a Novel Checkpoint Regulator in B Cell Differentiation and Antibody-Mediated Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Multifaceted Function of Myosin-18, an Unconventional Class of the Myosin Superfamily.Frontiers in cell and developmental biology · 2021Review
- A novel isoform of myosin 18A (Myo18Aγ) is an essential sarcomeric protein in mouse heart.The Journal of biological chemistry · 2019Article
- MYO18A: An unusual myosin.Advances in biological regulation · 2018Review
- Leucine repeat adaptor protein 1 interacts with Dishevelled to regulate gastrulation cell movements in zebrafish.Nature communications · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unconventional myosin MYO18A that contains a PDZ domain is required for muscle integrity during zebrafish development. However, the mechanism by which it functions in myofibers is not clear. The presence of a PDZ domain suggests that MYO18A may interact with other partners to perform muscle-specific functions. Here we performed double-hybrid screening and co-immunoprecipitation to identify MYO18A-interacting proteins, and have identified p190RhoGEF and Golgin45 as novel partners for the MYO18A PDZ domain. We have also identified Lurap1, which was previously shown to bind MYO18A. Functional analyses indicate that, similarly as myo18a, knockdown of lurap1, p190RhoGEF and Golgin45 by morpholino oligonucleotides disrupts dystrophin localization at the sarcolemma and produces muscle lesions. Simultaneous knockdown of myo18a with either of these genes severely disrupts myofiber integrity and dystrophin localization, suggesting that they may function similarly to maintain myofiber integrity. We further show that MYO18A and its interaction partners are required for adhesion of myoblasts to extracellular matrix, and for the formation of the Golgi apparatus and organization of F-actin bundles in myoblast cells. These findings suggest that MYO18A has the potential to form a multiprotein complex that links the Golgi apparatus to F-actin, which regulates muscle integrity and function during early development.
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