Mechanosensors in plants
Article Abstract:
In-gel kinase assays of mechanically stimulated alfalfa leaves were used to determine a potential role of protein kinases in the signal transduction of mechanical stimuli in plants. A protein kinase of relative molecular mass 44,000 (44K) is activated within a minute after a two-second mechanical stimulation, although this disappears after 10 minutes. The kinase was believed to belong to a class of mitogen-activated protein (MAP) kinases due to the molecular mass of the MBP kinase and its ability to phosphorylate. A test of this hypothesis indicated that a MAP kinase pathway is involved in mechanosensing in plants.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
Article Abstract:
LIM-kinase 1 (LIMK-1), a protein kinase with two amino-terminal LIM motifs, has dramatic and extremely characteristic effects on the actin cytoskeleton. This indicates that this protein could play a specific role in cytoskeletal regulation. This could be through reducing depolymerization of actin filaments. It appears that the pool of active cofilin is essential for regulation of the actin cytoskeleton and is regulated by phosphorylation. It is possible that local concentrations of active cofilin are controlled by cofilin kinases and phosphatases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Article Abstract:
Endothelial nitric oxide synthase (eNOS) maintains systemic blood pressure, vascular remodelling and angiogenesis, and is phosphorylated in response to certain types of cellular stimulation. The role of phosphorylation in the control of nitric oxide (NO) production is not well known. It is shown that serine/threonine protein kinase Akt directly phosphorylates eNOS on serine 1179. eNOS is a new type of Akt substrate substrate that links signal transduction by Akt to the release of NO.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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