Authentic Biochemistry

HDAC 4 is a positive player in ALS muscle since it is not a functional histone deacetylase: The complexity of motor neuron disease reveals not-so-subtle differences in protein function

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Because HDAC4 closely resembles the structural component of the superfamily of histone deacetylases,  in might be assumed it functions to catalyze the removal of LYS bound acetate. But since HDAC4 does not contain the catalytically necessary TYR-OH but rather an HIS-imidizole it has no deacetylase enzymatic activity. However HDAC4 does interact with other proteins and the net result is protective of skeletal muscle atrophy and motor neuron degeneration in a murine mutant human SOD1 model of Amyotrophic Lateral Sclerosis (ALS). This Authentic Biochemistry podcast episode reveals once again that specificity in time and space with coordinated expression of biochemical species will be more complicated than previously reported once a sharper lens is used to examine the disease pathology at the biochemical/molecular level. --- Send in a voice message: https://anchor.fm/dr-daniel-j-guerra/message