Two protein tyrosine phosphatases, PTp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast

Article Abstract:

The authors present their research into the role protein tyrosine phosphateses Ptp2 and Ptp3 play in modulating subcellular localization of the Hog1 MAP kinase in yeast.

Nuclear membranes, Nuclear membrane, Tyrosine metabolism

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Heat shock-induced activation of stress MAP kinase is regulated by threonine and tyrosine-specific phosphatases

Article Abstract:

Heat shock-induced activation of stress mitogen-activated protein (MAP) kinase (MAPK) is regulated by tyrosine- and threonine-specific phosphatases. Heat shock regulation of the fission yeast Spc1 stress-activated protein kinase (SAPK), a homolog of human p38 and budding yeast Hog1p, has been demonstrated. It seems PP2C enzymes have an important role in cutting back Spc1 activity in cells that are heat-shocked, so transient activation of Spc1 at heat shock is made certain by differential regulation of tyrosine and threonine phosphorylation.

Statistical Data Included, Cellular signal transduction, Heat shock proteins, Phosphorylation, Mitogens, Tyrosine, Threonine

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Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast

Article Abstract:

Two protein tyrosine phosphatases, Ptp2 and Ptp3, have a role in the localization of the Hog1 MAP kinase in yeast cells. It has been found that dephosphorylation is not needed for export. Hog1 nuclear export, however, correlates with its dephosphorylation.

Carrier proteins, Transport proteins, Cytochemistry, Protein kinases, Cell nuclei, Cell nucleus, Cytoplasm

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