Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis

Article Abstract:

The importance of cytochrome c in apoptotic signaling pathways has been studied using genetically altered mice. It was found that cytochrome c is necessary for Apak-1-mediated activation of caspase -3 and for apoptosis brought on by common forms of cell stress, but not for apoptosis driven by TNF(alpha) and the death receptor pathway. Cytochrome c deficiency causes embryonic lethality. It also attenuates stress-induced apoptosis.

Cell death, Stress (Physiology), Cytochemistry, Cell cycle, Embryology, Experimental, Embryological research

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Activation of the IkB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain

Article Abstract:

Research reveals that a dimeric ubiquitin-conjugating enzyme complex Ubc13/Uev1A takes part not only in the assembly of polyubiquitin chains but also supports IkB kinase activation by the signal transducer TRAF6. Data further show that ubiquitin plays a regulatory role in activating the kinase through polyubiquitin chains.

Analysis, Enzymes, Protein kinases, Ubiquitin, Enzyme regulation, Enzyme activation

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A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber type

Article Abstract:

Slow- and fast-twitch myofibers of adult skeletal muscles express unique sets of muscle-specific genes. The distinctive programs of gene expression are regulated by changes in motor neuron activity. A calcineurin-dependent transcription pathway regulates type for skeletal muscle fiber. Calcineurin is a calcium-regulated cyclosporin-sensitive serine-threonine phosphatase. Its activation in skeletal myocytes up-regulates slow-fiber-specific gene promotors selectively.

Exercise, Exercise physiology, Muscle contraction, Genetic regulation, Gene expression, Genetic transcription, Transcription (Genetics), Muscle proteins, Myoglobin, Myosin

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