Calcium, calmodulin and cell cycle regulation
نویسندگان
چکیده
منابع مشابه
Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II.
Organelle transport by myosin-V is down-regulated during mitosis, presumably by myosin-V phosphorylation. We used mass spectrometry phosphopeptide mapping to show that the tail of myosin-V was phosphorylated in mitotic Xenopus egg extract on a single serine residue localized in the carboxyl-terminal organelle-binding domain. Phosphorylation resulted in the release of the motor from the organell...
متن کاملThe Function of Calcium/calmodulin Dependent Protein Kinase Ii in Cell Cycle Regulation
Ca/Calmodulin-dependent protein kinase II (CamKII) is a multifunctional enzyme that is activated by increases in intracellular Ca. CaMKII is expressed in all tissues but is most abundant in the brain. Diversity in subunit composition and Ca sensitivity permit the coordination of multiple cellular functions including muscle contraction, synaptic vesicle release, proliferation and differentiation...
متن کاملCalcium and cell cycle control.
The cell division cycle of the early sea urchin embryo is basic. Nonetheless, it has control points in common with the yeast and mammalian cell cycles, at START, mitosis ENTRY and mitosis EXIT. Progression through each control point in sea urchins is triggered by transient increases in intracellular free calcium. The Cai transients control cell cycle progression by translational and post-transl...
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Blockade of lysosomal calcium release due to lysosomal lipid accumulation has been shown to inhibit mTORC1 signaling. However, the mechanism by which lysosomal calcium regulates mTORC1 has remained undefined. Herein we report that proper lysosomal calcium release through the calcium channel TRPML1 is required for mTORC1 activation. TRPML1 depletion inhibits mTORC1 activity, while overexpression...
متن کاملMyosin V: regulation by calcium, calmodulin, and the tail domain
alcium activates the ATPase activity of tissue-purified myosin V, but not that of shorter expressed constructs. Here, we resolve this discrepancy by comparing an expressed full-length myosin V (dFull) to three shorter constructs. Only dFull has low ATPase activity in EGTA, and significantly higher activity in calcium. Based on hydrodynamic data and electron microscopic images, the inhibited sta...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)00492-7