ArticleThe Journal of cell biology1990
Binding of brush border myosin I to phospholipid vesicles.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
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
57 citing papers in PubMed, 159 citations in OpenAlex.
- Myo1e/f regulate phagocytic podosomes to promote efficient cup closure in macrophages.bioRxiv : the preprint server for biology · 2026Article
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- Myosin-I synergizes with Arp2/3 complex to enhance the pushing forces of branched actin networks.Science advances · 2024Article
- Membrane binding of endocytic myosin-1s is inhibited by a class of ankyrin repeat proteins.Molecular biology of the cell · 2023Article
- Association of selected gene polymorphisms with thermotolerance traits in cattle - A review.Animal bioscience · 2022Article
- Myosin-I molecular motors at a glance.Journal of cell science · 2016Review
- Force Generation by Membrane-Associated Myosin-I.Scientific reports · 2016Article
- Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.Nature structural & molecular biology · 2015Article
- Shaping the intestinal brush border.The Journal of cell biology · 2014Review
- Membrane-bound myo1c powers asymmetric motility of actin filaments.Current biology : CB · 2012Article
- Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain.The Journal of biological chemistry · 2012Article
- Localization of myosin 1b to actin protrusions requires phosphoinositide binding.The Journal of biological chemistry · 2010Article
- Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.The EMBO journal · 2010Article
- Identification and characterization of an unusual class I myosin involved in vesicle traffic in Trypanosoma brucei.PloS one · 2010Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Myosin motor function: the ins and outs of actin-based membrane protrusions.Cellular and molecular life sciences : CMLS · 2010Review
- Molecular model of the microvillar cytoskeleton and organization of the brush border.PloS one · 2010Article
- Myosin-1a: A motor for microvillar membrane movement and mechanics.Communicative & integrative biology · 2010Article
- Kinetics of the interaction of myo1c with phosphoinositides.The Journal of biological chemistry · 2009Article
- Control of cell membrane tension by myosin-I.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The actin filament core within each microvillus of the intestinal epithelial cell is attached laterally to the plasma membrane by brush border (BB) myosin I, a protein-calmodulin complex belonging to the myosin I class of actin-based mechanoenzymes. In this report, the binding of BB myosin I to pure phospholipid vesicles was examined and characterized. BB myosin I demonstrated saturable binding to liposomes composed of anionic phospholipids, but did not associate with liposomes composed of only neutral phospholipids. The binding of BB myosin I to phosphatidylserine and phosphatidylglycerol vesicles reached saturation at 4-5 x 10(-3) nmol protein/nmol phospholipid, while the apparent dissociation constant was determined to be 1-3 x 10(-7) M. Similar to the free protein, membrane-associated BB myosin I bound F-actin in an ATP-sensitive manner and demonstrated actin-activated Mg-ATPase activity. Immunoblot analysis of peptides generated from controlled proteolysis of vesicle-bound BB myosin I provided structural information concerning the site responsible for the membrane interaction. Immunoblot staining with domain-specific mAbs revealed a series of COOH-terminal, liposome-associated peptides that were protected from digestion, suggesting that the membrane-binding domain is within the carboxy-terminal "tail" of the BB myosin I heavy chain.
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.