ArticleBioscience reports2019
Regulation of Myosin-5b by Rab11a and the Rab11 family interacting protein 2.
Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- MYO5B deficiency is associated with altered MUC13 localization and DMBT1 accumulation in intestinal epithelial cells.American journal of physiology. Gastrointestinal and liver physiology · 2026Article
- Breast Cancer-Derived Extracellular Vesicles Modulate the Cytoplasmic and Cytoskeletal Dynamics of Blood-Brain Barrier Endothelial Cells.Journal of extracellular vesicles · 2025Article
- Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023Review
- Myo5b Transports Fibronectin-Containing Vesicles and Facilitates FN1 Secretion from Human Pleural Mesothelial Cells.International journal of molecular sciences · 2022Article
- Article
- To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021Review
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- The cargo adaptor proteins RILPL2 and melanophilin co-regulate myosin-5a motor activity.The Journal of biological chemistry · 2019Article
- Myosin Va and spermine synthase: partners in exosome transport.Bioscience reports · 2019Article
- Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering.Bioscience reports · 2019Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian myosin-5b (Myo5b) plays a critical role in the recycling of endosomes to the plasma membrane via the interactions with Rab11a and the Rab11 family interacting protein 2 (FIP2). However, it remains unclear on how Rab11a and FIP2 are coordinated in tethering Myo5b with the vesicles and activating the motor function of Myo5b. In the present study, we show that Rab11a binds to the globular tail domain (GTD) of Myo5b and this binding abolishes the head-GTD interaction of Myo5b, thus activating the motor function of Myo5b. On the other hand, FIP2 directly interacts with both Rab11a and the tail of Myo5b, and the binding of FIP2 to Myo5b does not affect Myo5b motor function. Moreover, Rab11a displays higher affinity to FIP2 than to Myo5b, suggesting that Rab11a binds preferentially to FIP2 than to Myo5b. Based on the current findings, we propose that the association of Myo5b with vesicles is mediated by FIP2, which bridges Myo5b and the membrane-bound Rab11a, whereas the motor function of Myo5b is regulated by Rab11a.
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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.