ArticleCommunicative & integrative biology2010
Myosin-1a: A motor for microvillar membrane movement and mechanics.
Article in Communicative & integrative biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Association of selected gene polymorphisms with thermotolerance traits in cattle - A review.Animal bioscience · 2022Article
- Disruption of Rab8a and Rab11a causes formation of basolateral microvilli in neonatal enteropathy.Journal of cell science · 2017Article
- Myosin 1b functions as an effector of EphB signaling to control cell repulsion.The Journal of cell biology · 2015Article
- Myosin VI mediates the movement of NHE3 down the microvillus in intestinal epithelial cells.Journal of cell science · 2014Article
- The tails of apical scaffolding proteins EBP50 and E3KARP regulate their localization and dynamics.Molecular biology of the cell · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Myosin-1a is one of eight monomeric, membrane binding class I myosins expressed in vertebrates.1 As the most abundant actin-based motor protein found in the enterocyte microvillus, myosin-1a has long been known to interact with the apical membrane via a highly basic C-terminal tail domain.2 Several recent studies shed light on possible functional consequences of this protein/lipid interaction. In vitro and in vivo studies of microvillar function have revealed that myosin-1a can move apical membrane along core actin bundles, leading to the release of small vesicles from microvillar tips.3,4 Additional studies indicate that myosin-1a and other class I myosins contribute to membrane-cytoskeleton adhesion, which enables the apical membrane to resist deformation.5 These findings clearly position myosin-1a as an important player in apical membrane movement and structural stability. How this motor is able to fulfill these two seemingly distinct functions is currently unclear, but will serve as the focus of our discussion below.
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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.