High impact information on ck

• Myosin VIIa moves along actin filaments as a processive, double-headed single molecule when dimerized by the inclusion of a leucine zipper at the C terminus of the coiled-coil domain [1].
• We studied the molecular mechanism of Drosophila myosin VIIa, using transient kinetics and single-molecule motility assays [1].
• Mutations in myosin VIIA (myoVIIA), an unconventional myosin, lead to deafness and balance anomalies in humans, mice, and zebrafish; individuals are deaf, and stereocilia are disorganized [2].
• Amino acid sequence data comparisons suggest that D2 encodes a serine esterase with strong sequence identity to Torpedo acetylcholine esterase and a Drosophila esterase [3].
• Drosophila crinkled, mutations of which disrupt morphogenesis and cause lethality, encodes fly myosin VIIA [4].

Biological context of ck

• In this manuscript, we compare the complete derived amino acid sequence for D2 to two cloned and sequenced eukaryotic esterases and examine the requirement of the D2 gene product for development [3].

Anatomical context of ck

• This is a phenocopy of mutations in crinkled, and suggests mutations that cause branched hairs will be in genes that encode products that interact with the actin cytoskeleton [5].

Other interactions of ck

• Together, our data suggest a key role for ck/myoVIIA in the formation of cellular projections and other actin-based functions required for viability [4].

References