ArticleMolecular biology of the cell1998
The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 65 citations in OpenAlex.
- Article
- 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
- PakB binds to the SH3 domain of Dictyostelium Abp1 and regulates its effects on cell polarity and early development.Molecular biology of the cell · 2013Article
- 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
- Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane.Molecular and cellular biology · 2011Article
- The three-dimensional dynamics of actin waves, a model of cytoskeletal self-organization.Biophysical journal · 2009Article
- GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex.Eukaryotic cell · 2009Article
- Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge.The Journal of biological chemistry · 2008Article
- CIB1 and CaBP1 bind to the myo1c regulatory domain.Journal of muscle research and cell motility · 2007Article
- Biological, biochemical, and kinetic effects of mutations of the cardiomyopathy loop of Dictyostelium myosin II: importance of ALA400.The Journal of biological chemistry · 2005Article
- Cellular distribution and functions of wild-type and constitutively activated Dictyostelium PakB.Molecular biology of the cell · 2005Article
- Functional characterization of myosin I tail regions in Candida albicans.Eukaryotic cell · 2004Article
- Myosin I is required for hypha formation in Candida albicans.Eukaryotic cell · 2002Article
- The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains.The Journal of cell biology · 2001Article
- Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp.The Journal of cell biology · 2000Article
- A dibasic motif in the tail of a class XIV apicomplexan myosin is an essential determinant of plasma membrane localization.Molecular biology of the cell · 2000Article
- A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex.The Journal of cell biology · 2000Article
- Myosin I contributes to the generation of resting cortical tension.Biophysical journal · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The class I myosins play important roles in controlling many different types of actin-based cell movements. Dictyostelium cells either lacking or overexpressing amoeboid myosin Is have significant defects in cortical activities such as pseudopod extension, cell migration, and macropinocytosis. The existence of Dictyostelium null mutants with strong phenotypic defects permits complementation analysis as a means of exploring important functional features of the myosin I heavy chain. Mutant Dictyostelium cells lacking two myosin Is exhibit profound defects in growth, endocytosis, and rearrangement of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. However, mutant forms of the myoB heavy chain in which a serine at the consensus phosphorylation site has been altered to an alanine or in which the C-terminal SH3 domain has been removed fail to complement the null phenotype. The wild-type and mutant forms of the myoB heavy chain appeared to be properly localized when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and SH3 domains do not play a role in the localization of myosin I, but are absolutely required for in vivo function.
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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.