Myosins were among the first group of proteins found to be associated with hereditary hearing loss. These motor molecules are divided into 17 classes based on analysis of their motor and tail domains and numbered in the order in which they were discovered (Myosin Homepage, http://www.mrc-lmb.cam.ac. uk/myosin/myosin.html). The myosins are comprised of a heavy chain with a conserved approximately 80 kDa catalytic domain (the head or motor domain), and most are followed by an a-helical light chain-binding region (the neck region) (Sellars 1999). All myosins contain an actin-binding domain and an ATP-binding domain in their head region, allowing them to move along actin filaments. Most myosins contain a C-terminal tail and in some cases, an N-terminal extension as well. The tail domains diverge from one another between myosin classes and are believed to confer the function of each different myosin. Following is a number of myosins that when mutated, were found to compromise both auditory and vestibular function, manifested clinically by various forms of hearing impairment.
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