Multi-OSL-thermochronometry using deep borehole core for thermal history over 0.1 Myr in Rokko Mountains
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Earth and Space Science Open Archive PosterOpen AccessYou are viewing the latest version by default [v1]Multi-OSL-thermochronometry using deep borehole core for thermal history over 0.1 Myr in Rokko MountainsAuthorsManabuOgataiDGeorginaKingFredericHermanRyujiYamadaKentaroOmuraShigeruSueokaiDSee all authors Manabu OgataiDCorresponding Author• Submitting AuthorJapan Atomic Energy AgencyiDhttps://orcid.org/0000-0003-1440-6127view email addressThe email was not providedcopy email addressGeorgina KingUniversity of Lausanneview email addressThe email was not providedcopy email addressFrederic HermanUniversity of Lausanneview email addressThe email was not providedcopy email addressRyuji YamadaNational Research Institute for Earth Science and Disaster Preventionview email addressThe email was not providedcopy email addressKentaro OmuraNational Research Institute for Earth Science and Disaster Preventionview email addressThe email was not providedcopy email addressShigeru SueokaiDJapan Atomic Energy AgencyiDhttps://orcid.org/0000-0002-5264-2713view email addressThe email was not providedcopy email addressKeywords:
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Myr 1 is a widely distributed mammalian myosin I molecule related to brush border myosin 1. A second widely distributed myosin I molecule similar to myr 1 and brush border myosin I, called myr 2, has now been identified. Specific antibodies and expression of epitope-tagged molecules were used to determine the subcellular localization of myr 1 and myr 2 in NRK cells. Myr 1 was detected at the plasma membrane and was particularly enriched in cell protrusions like lamellipodia, membrane ruffles and filopodia. In dividing cells myr 1 localized to the cleavage furrow. Myr 2 was localized in a discrete punctate pattern in resting cells and in cells undergoing cytokinesis. In subcellular fractionation experiments myr 1 and myr 2 were both partly soluble and partly associated with smooth membranes of medium density. The tail domains of myosin I molecules have been proposed to interact with a receptor and thereby determine the subcellular localization. To test this hypothesis we expressed the tail domains of myr 1 and myr 2 that lack the F-actin-binding myosin head domain in NRK cells. These tail domains also partly copurified with smooth membranes of medium density and immunolocalized similar to the respective endogenous myosin I; however, they exhibited a lower affinity for membranes and an increased diffuse cytosolic localization. These results suggest that the tail domains of myr 1 and myr 2 are sufficient for subcellular targeting but that their head domains also contribute significantly to maintaining a proper subcellular localization.
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