ArticleThe Journal of cell biology1991
An increase or a decrease in myosin II phosphorylation inhibits macrophage motility.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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Who cites it
24 citing papers in PubMed, 75 citations in OpenAlex.
- Applying Antibodies Inside Cells: Principles and Recent Advances in Neurobiology, Virology and Oncology.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Generation of membrane structures during phagocytosis and chemotaxis of macrophages: role and regulation of the actin cytoskeleton.Immunological reviews · 2013Review
- Article
- A genetic strategy for the dynamic and graded control of cell mechanics, motility, and matrix remodeling.Biophysical journal · 2012Article
- Regulation of tyrosine phosphorylation in macrophage phagocytosis and chemotaxis.Archives of biochemistry and biophysics · 2011Review
- Heart-specific small subunit of myosin light chain phosphatase activates rho-associated kinase and regulates phosphorylation of myosin phosphatase target subunit 1.The Journal of biological chemistry · 2010Article
- Spatiotemporal organization, regulation, and functions of tractions during neutrophil chemotaxis.Blood · 2010Article
- Cytotoxic Effects on HL-60 Cells of Myosin Light Chain Kinase Inhibitor ML-7 Alone and in Combination with Flavonoids.Toxicological research · 2009Article
- Multivariate gene expression analysis reveals functional connectivity changes between normal/tumoral prostates.BMC systems biology · 2008Article
- Article
- Increased myosin light chain kinase expression in hypertension: Regulation by serum response factor via an insertion mutation in the promoter.Molecular biology of the cell · 2006Article
- Inhibiting myosin light chain kinase induces apoptosis in vitro and in vivo.Molecular and cellular biology · 2005Article
- Modulation of myosin light-chain phosphorylation by p21-activated kinase 1 in Escherichia coli invasion of human brain microvascular endothelial cells.Infection and immunity · 2003Article
- Saccharomyces boulardii interferes with enterohemorrhagic Escherichia coli-induced signaling pathways in T84 cells.Infection and immunity · 2003Article
- Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo.The Journal of cell biology · 1999Article
- p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts.The Journal of cell biology · 1999Article
- Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility.The Journal of cell biology · 1999Article
- Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton.The Journal of experimental medicine · 1998Article
- Differential expression and functions of cortical myosin IIA and IIB isotypes during meiotic maturation, fertilization, and mitosis in mouse oocytes and embryos.Molecular biology of the cell · 1998Article
- Signaling pathways underlying eosinophil cell motility revealed by using caged peptides.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosin II purified from mammalian non-muscle cells is phosphorylated on the 20-kD light chain subunit (MLC20) by the Ca2+/calmodulin-dependent enzyme myosin light chain kinase (MLCK). The importance of MLC20 phosphorylation in regulating cell motility was investigated by introducing either antibodies to MLCK (MK-Ab) or a Ca2+/calmodulin-independent, constitutively active form of MLCK (MK-) into macrophages. The effects of these proteins on cell motility were then determined using a quantitative chemotaxis assay. Chemotaxis is significantly diminished in macrophages containing MK-Ab compared to macrophages containing control antibodies. Moreover, there is an inverse relationship between the number of cells that migrate and the amount of MK-Ab introduced into cells. Interestingly, there is also an inverse relationship between the number of cells that migrate and the amount of MK- introduced into cells. Other experiments demonstrated that MK-Ab decreased intracellular MLC20 phosphorylation while MK- increased MLC20 phosphorylation. MK- also increased the amount of myosin associated with the cytoskeleton. These data demonstrate that the regulation of MLCK is an important aspect of cell motility and suggest that MLC20 phosphorylation must be maintained within narrow limits during translational motility by mammalian cells.
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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.