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anti-Human MYO3A Antibodies:
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Data show that myo3a is localized in actin-rich ellipsoids of fish cones.
MYO3A is more efficient than MYO3B (show MYO3B Antibodies) at increasing formation and elongation of stable microvilli on the surface of cultured epithelial cells.
Study reports an amino acid substitution in MYO3A motor-head domain disrupting its ATPase (show DNAH8 Antibodies) activity that can cause autosomal dominant progressive hereditary hearing loss. Also, these results uncovered a novel interaction between MYO3A and PCDH15 (show PCDH15 Antibodies) shedding new light on the function of myosin IIIA at stereocilia tips.
Data suggest that, in enterocytes, MYO3A autophosphorylation of kinase domain at Thr184/Thr188 regulates kinase activity, translocation of MYO3A to tips of microvilli, and stability of actin cytoskeleton.
The differential regulation of the kinase and motor activities allows for MYO3A to precisely self-regulate its concentration in the actin bundle-based structures of cells.
Results suggest that Myo3A motor activity is regulated through a mechanism involving concentration-dependent autophosphorylation.
behavioral inhibition-associated SNPs appear to be associated with differences in MYO3A- but not GAD2 (show GAD2 Antibodies) lymphoblastoid-mRNA expression levels
mutation in humans causes progressive nonsyndromic hearing loss DFNB30
class III myosin is an actin-based motor protein having a protein kinase activity
myosin IIIA can spend a majority of its ATP hydrolysis cycling time on actin
the actomyosin-ADP state may be important for the ability of myosin III to function as a cellular transporter and actin cross-linker in the actin bundles of sensory cells
The phenotype of the Myo3a knockout mice parallels the phenotype of human DFNB30.
The protein encoded by this gene belongs to the myosin superfamily. Myosins are actin-dependent motor proteins and are categorized into conventional myosins (class II) and unconventional myosins (classes I and III through XV) based on their variable C-terminal cargo-binding domains. Class III myosins, such as this one, have a kinase domain N-terminal to the conserved N-terminal motor domains and are expressed in photoreceptors. The protein encoded by this gene plays an important role in hearing in humans. Three different recessive, loss of function mutations in the encoded protein have been shown to cause nonsyndromic progressive hearing loss. Expression of this gene is highly restricted, with the strongest expression in retina and cochlea.
, myosin IIIA