ArticleThe Journal of cell biology1997
Myosin I overexpression impairs cell migration.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 77 citations in OpenAlex.
- Akt and SGK protein kinases are required for efficient feeding by macropinocytosis.Journal of cell science · 2019Article
- pERK1/2 Peripheral Recruitment and Filopodia Protrusion Augment Oligodendrocyte Progenitor Cell Migration: Combined Effects of PDGF-A and Fibronectin.Cellular and molecular neurobiology · 2017Article
- Selective localization of myosin-I proteins in macropinosomes and actin waves.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Article
- A Dictyostelium secreted factor requires a PTEN-like phosphatase to slow proliferation and induce chemorepulsion.PloS one · 2013Article
- Molecular basis of dynamic relocalization of Dictyostelium myosin IB.The Journal of biological chemistry · 2012Article
- Article
- Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.The EMBO journal · 2010Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Cellular distribution and functions of wild-type and constitutively activated Dictyostelium PakB.Molecular biology of the cell · 2005Article
- Mammalian class I myosin, Myo1b, is monomeric and cross-links actin filaments as determined by hydrodynamic studies and electron microscopy.Biophysical journal · 2005Article
- Modeling the role of myosin 1c in neuronal growth cone turning.Biophysical journal · 2003Article
- Toxoplasma gondii myosins B/C: one gene, two tails, two localizations, and a role in parasite division.The Journal of cell biology · 2001Article
- Reduced protein diffusion rate by cytoskeleton in vegetative and polarized dictyostelium cells.Biophysical journal · 2001Article
- 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
- A myosin I is involved in membrane recycling from early endosomes.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
- Myosin I contributes to the generation of resting cortical tension.Biophysical journal · 1999Article
- Association of myosin I alpha with endosomes and lysosomes in mammalian cells.Molecular biology of the cell · 1999Article
- 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
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dictyostelium myoB, a member of the myosin I family of motor proteins, is important for controlling the formation and retraction of membrane projections by the cell's actin cortex (Novak, K.D., M.D. Peterson, M.C. Reedy, and M.A. Titus. 1995. J. Cell Biol. 131:1205-1221). Mutants that express a three- to sevenfold excess of myoB (myoB+ cells) were generated to further analyze the role of myosin I in these processes. The myoB+ cells move with an instantaneous velocity that is 35% of the wild-type rate and exhibit a 6-8-h delay in initiation of aggregation when placed under starvation conditions. The myoB+ cells complete the developmental cycle after an extended period of time, but they form fewer fruiting bodies that appear to be small and abnormal. The myoB+ cells are also deficient in their ability both to form distinct F-actin filled projections such as crowns and to become elongate and polarized. This defect can be attributed to the presence of at least threefold more myoB at the cortex of the myoB+ cells. In contrast, threefold overexpression of a truncated myoB that lacks the src homology 3 (SH3) domain (myoB/SH3- cells) or myoB in which the consensus heavy chain phosphorylation site was mutated to an alanine (S332A-myoB) does not disturb normal cellular function. However, there is an increased concentration of myoB in the cortex of the myoB/SH3- and S332A-myoB cells comparable to that found in the myoB+ cells. These results suggest that excess full-length cortical myoB prevents the formation of the actin-filled extensions required for locomotion by increasing the tension of the F-actin cytoskeleton and/or retracting projections before they can fully extend. They also demonstrate a role for the phosphorylation site and SH3 domain in mediating the in vivo activity of myosin I.
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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.