ArticleThe Journal of cell biology1995
Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- A conserved pressure-driven mechanism for regulating cytosolic osmolarity.Current biology : CB · 2023Article
- A conserved pressure-driven mechanism for regulating cytosolic osmolarity.bioRxiv : the preprint server for biology · 2023Article
- Discovery of the first unconventional myosin:Frontiers in physiology · 2023Review
- Superdiffusion dominates intracellular particle motion in the supercrowded cytoplasm of pathogenic Acanthamoeba castellanii.Scientific reports · 2015Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp.The Journal of cell biology · 2000Article
- Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization.The Journal of cell biology · 1998Article
- Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments.The Journal of cell biology · 1998Article
- The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function.Molecular biology of the cell · 1998Article
- The cell adhesion molecule DdCAD-1 in Dictyostelium is targeted to the cell surface by a nonclassical transport pathway involving contractile vacuoles.The Journal of cell biology · 1997Article
- Unconventional myosins in inner-ear sensory epithelia.The Journal of cell biology · 1997Article
- The amino acid sequence of the light chain of Acanthamoeba myosin IC.Journal of muscle research and cell motility · 1997Article
- p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Myosin I overexpression impairs cell migration.The Journal of cell biology · 1997Article
- Actin-, myosin- and ubiquitin-dependent endocytosis.Experientia · 1996Review
- Chicken myosin IB mRNA is highly expressed in lymphoid tissues.Journal of anatomy · 1996Article
- Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities.The Journal of cell biology · 1996Article
- Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The actin-activated Mg(2+)-ATPase activities of the three myosin I isoforms in Acanthamoeba castellanii are significantly expressed only after phosphorylation of a single site in the myosin I heavy chain. Synthetic phosphorylated and unphosphorylated peptides corresponding to the phosphorylation site sequences, which differ for the three myosin I isoforms, were used to raise isoform-specific antibodies that recognized only the phosphorylated myosin I or the total myosin I isoform (phosphorylated and unphosphorylated), respectively. With these antisera, the amounts of total and phosphorylated isoform were quantified, the phosphomyosin I isoforms localized, and the compartmental distribution of the phosphomyosin isoforms determined. Myosin IA, which was almost entirely in the actin-rich cortex, was 70-100% phosphorylated and particularly enriched under phagocytic cups. Myosins IB and IC were predominantly associated with plasma membranes and large vacuole membranes, where they were only 10-20% phosphorylated, whereas cytoplasmic myosins IB and IC, like cytoplasmic myosin IA, were mostly phosphorylated (60-100%). Moreover, phosphomyosin IB was concentrated in actively motile regions of the plasma membrane. More than 20-fold more phosphomyosin IC and 10-fold more F-actin were associated with the membranes of contracting contractile vacuoles (CV) than of filling CVs. As the total amount of CV-associated myosin IC remained constant, it must be phosphorylated at the start of CV contraction. These data extend previous proposals for the specific functions of myosin I isozymes in Acanthamoeba (Baines, I.C., H. Brzeska, and E.D. Korn. 1992. J. Cell Biol. 119: 1193-1203): phosphomyosin IA in phagocytosis, phosphomyosin IB in phagocytosis and pinocytosis, and phosphomyosin IC in contraction of the CV.
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