ArticleThe Journal of biological chemistry2008
Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- A cryptic sequence targets the adhesion complex scaffold ANKS4B to apical microvilli to promote enterocyte brush border assembly.The Journal of biological chemistry · 2020Article
- Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization ofMolecular biology of the cell · 2020Article
- Mammalian Nonmuscle Myosin II Binds to Anionic Phospholipids with Concomitant Dissociation of the Regulatory Light Chain.The Journal of biological chemistry · 2016Article
- Force Generation by Membrane-Associated Myosin-I.Scientific reports · 2016Article
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Selective localization of myosin-I proteins in macropinosomes and actin waves.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Non-muscle myosins in tumor progression, cancer cell invasion, and metastasis.Cytoskeleton (Hoboken, N.J.) · 2014Review
- Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.Biophysical journal · 2014Article
- Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Molecular basis of dynamic relocalization of Dictyostelium myosin IB.The Journal of biological chemistry · 2012Article
- Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain.The Journal of biological chemistry · 2012Article
- Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactions.Biophysical journal · 2010Article
- Myo1e binds anionic phospholipids with high affinity.Biochemistry · 2010Article
- Localization of myosin 1b to actin protrusions requires phosphoinositide binding.The Journal of biological chemistry · 2010Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- An experimentally based computer search identifies unstructured membrane-binding sites in proteins: application to class I myosins, PAKS, and CARMIL.The Journal of biological chemistry · 2010Article
- Control of cell membrane tension by myosin-I.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The tail of Acanthamoeba myosin IC (AMIC) has a basic region (BR), which contains a putative pleckstrin homology (PH) domain, followed by two Gly/Pro/Ala (GPA)-rich regions separated by a Src homology 3 (SH3) domain. Cryoelectron microscopy had shown that the tail is folded back on itself at the junction of BR and GPA1, and nuclear magnetic resonance spectroscopy indicated that the SH3 domain may interact with the putative PH domain. The BR binds to acidic phospholipids, and the GPA region binds to F-actin. We now show that the folded tail does not affect the affinity of AMIC for acidic phospholipids. AMIC binds phosphatidylinositol 4,5-bisphosphate (PIP2) with high affinity (approximately 1 microm), but binding is not stereospecific. When normalized to net negative charge, AMIC binds with equal affinity to phosphatidylserine (PS) and PIP2. This and other data show that the putative PH domain of AMIC is not a typical PIP2-specific PH domain. We have identified a 13-residue sequence of basic-hydrophobic-basic amino acids within the putative PH domain that may be a major determinant of binding of AMIC to acidic phospholipids. Despite the lack of stereospecificity, AMIC binds 10 times more strongly to vesicles containing 5% PIP2 plus 25% PS than to vesicles containing only 25% PS, suggesting that AMIC may be targeted to PIP2-enriched regions of the plasma membrane. In agreement with this, AMIC colocalizes with PIP2 at dynamic, protrusive regions of the plasma membrane. We discuss the possibility that AMIC binding to PIP2 may initiate the formation of a multiprotein complex at the plasma membrane.
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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.