タン白質リン酸化反応の3つの調節機構とその細胞内コンパートメント

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Cyclic AMP-dependent protein kinase has been well established to be composed of catalytic and regulatory subunits. Cyclic AMP dissociates these subunits to exhibit full enzymatic activity. In contrast, cyclic GMP-dependent protein kinase does not possess such a subunit structure and is activated by cyclic GMP simply in an allosteric manner. In addition to cyclic AMP-dependent and cyclic GMP-dependent protein kinases, another species of multifunctional protein kinase has been found in many mammalian tissues. This protein kinase is entirely independent of cyclic nucleotides and activated selectively by lower concentrations of Ca2+ in the presence of a membrane-associated factor. This factor appears to be a heat-stable and exclusively localized in membranes. Thus, the three species of protein kinases mentioned above are activated in different manners. All kinases have abilities to activate and inactivate muscle phosphorylase kinase and glycogen synthase, respectively, although the relative rates of reactions towards various substrates are markedly different. The Ca2+ -dependent protein kinase seems to be associated with membraneous components, whereas cyclic GMP-dependent protein kinase appears to be related to certain subcellular organella such as nucleus. Suggestive evidence is available implying that the cyclic AMP-, cyclic GMP- and Ca2+ -activated three sets of protein kinase systems may play each specific physiological roles presumably owing to their own subcellular compartments.
日本生物物理学会の論文

タン白質リン酸化反応の3つの調節機構とその細胞内コンパートメント

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