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recruitment of BCK to submembrane domains, formation of dynamic actin-based protrusions
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isoforms M1, M2, B
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isoforms M1, M2, B
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isoforms M, B
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muscle-type cytosolic isozyme MM-CK, and brain-type cytosolic isozyme BB-CK
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HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK)
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cytosolic brain-type creatine kinase
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isozymes CK-MM, CK-BB, and CK-MB
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cytoplasmic, muscle-type isoform MCK
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cytosolic brain-type creatine kinase, mainly soluble brain BCK
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cytosolic brain-type creatine kinase, mainly soluble brain BCK
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isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
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isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
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acetylcholine receptor membrane
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
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acetylcholine receptor membrane
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overview on intramitochondrial localization
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accumulated in contact sites between inner and outer mitochondrial membrane
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mitochondrial isozyme MtCK
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there are two mitochondrial isoforms of CK: s-type (sarcomeric, expressed in skeletal and heart muscles only) and u-type (ubiquitous, expressed in many other tissues), which both exist as octamers in fish as well as in higher vertebrates and invertebrates. The mitochondrial s-type, rather than u-type, is predominantly expressed in herring eye
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overview on intramitochondrial localization
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accumulated in contact sites between inner and outer mitochondrial membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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accumulated in contact sites between inner and outer mitochondrial membrane
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accumulated in contact sites between inner and outer mitochondrial membrane
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mitochondrial isoform plays the most crucial role in maintaining cell viability by stabilizing contact sites between inner and outer mitochondrial membranse and maintaining local metabolic channeling
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HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK). The mitochondrial CK isoform plays the most crucial role in maintaining cell viability by stabilizing contact sites between inner and outer mitochondrial membranes and maintaining local metabolite channeling, thus avoiding transition pore opening which eventually results in activation of caspase cell-death pathways
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association with by brain-type creatine kinase
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octameric MtCK is situated in the mitochondrial intermembrane space, binding simultaneously to both mitochondrial inner and outer membranes, as well as in the cristae space bound to inner membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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accumulated in contact sites between inner and outer mitochondrial membrane
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sarcomeric, mitochondrial isoform sMiCK
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accumulated in contact sites between inner and outer mitochondrial membrane
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simulation of hyperglycemic conditions induces H2O2 production in a creatine sensitive manner
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in mitochondria from intact animals, mCK exists as a mixture of two oligomeric forms (dimer and octamer: 68 and 32%, respectively)
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head isozyme
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accumulated in contact sites between inner and outer mitochondrial membrane
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accumulated in contact sites between inner and outer mitochondrial membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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trout
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under energy-compromised conditions, CKM is recruited to the plasma membrane and co-localizes with NCX1
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association with by brain-type creatine kinase
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association with by brain-type creatine kinase, isolated from rat forebrains by separation from nerve-ending particles (synaptosomes). Synaptic vesicle BCK is indeed firmly anchored in the vesicle membrane and not just interacting electrostatically with the lipid headgroups or simply enclosed within the vesicles
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additional information
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overview
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additional information
Frog
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overview
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additional information
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overview
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additional information
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overview
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additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview
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additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview
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additional information
the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
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additional information
the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
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additional information
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overview
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additional information
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overview
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additional information
as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
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additional information
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as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
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