ArticleThe Journal of biological chemistry2017
Human Rab small GTPase- and class V myosin-mediated membrane tethering in a chemically defined reconstitution system.
Article in The Journal of biological chemistry, 2017. 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, 18 citations in OpenAlex.
- Golgi CATCHR complexes function as organizing hubs for vesicle tethering and fusion.bioRxiv : the preprint server for biology · 2026Article
- Urinary exosomal RAB11A serves as a novel non-invasive biomarker for diagnosis, treatment response monitoring, and prognosis in small cell lung cancer.Clinical proteomics · 2025Article
- Review
- Self-assemblies of Rab- and Arf-family small GTPases on lipid bilayers in membrane tethering.Biophysical reviews · 2021Review
- The Small GTPase Arf6 Functions as a Membrane Tether in a Chemically-Defined Reconstitution System.Frontiers in cell and developmental biology · 2021Article
- A Molecular Mechanism Underlying Genotype-Specific Intrahepatic Cholestasis Resulting From MYO5B Mutations.Hepatology (Baltimore, Md.) · 2020Article
- Curvature-sensitive trans-assembly of human Atg8-family proteins in autophagy-related membrane tethering.Protein science : a publication of the Protein Society · 2020Article
- Membrane Tethering Potency of Rab-Family Small GTPases Is Defined by the C-Terminal Hypervariable Regions.Frontiers in cell and developmental biology · 2020Article
- Homotypic and heterotypicThe Journal of biological chemistry · 2019Article
- Myosin Va and spermine synthase: partners in exosome transport.Bioscience reports · 2019Article
- Reconstitution of membrane tethering mediated by Rab-family small GTPases.Biophysical reviews · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane tethering is a fundamental process essential for the compartmental specificity of intracellular membrane trafficking in eukaryotic cells. Rab-family small GTPases and specific sets of Rab-interacting effector proteins, including coiled-coil tethering proteins and multisubunit tethering complexes, are reported to be responsible for membrane tethering. However, whether and how these key components directly and specifically tether subcellular membranes remains enigmatic. Using chemically defined proteoliposomal systems reconstituted with purified human Rab proteins and synthetic liposomal membranes to study the molecular basis of membrane tethering, we established here that Rab-family GTPases have a highly conserved function to directly mediate membrane tethering, even in the absence of any types of Rab effectors such as the so-called tethering proteins. Moreover, we demonstrate that membrane tethering mediated by endosomal Rab11a is drastically and selectively stimulated by its cognate Rab effectors, class V myosins (Myo5A and Myo5B), in a GTP-dependent manner. Of note, Myo5A and Myo5B exclusively recognized and cooperated with the membrane-anchored form of their cognate Rab11a to support membrane tethering mediated by
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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.