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Protein-protein interaction assays and co-expression of complex partners reveal that pathogenic mutations in USH1G severely affect formation of the SANS/ush2a (show USH2A ELISA Kits)/whirlin (show DFNB31 ELISA Kits) complex. Translational read-through drug treatment, targeting the c.728C > A (p.S243X) nonsense mutation, restored SANS scaffold function. We conclude that USH1 and USH2 (show USH2A ELISA Kits) proteins function together in higher order protein complexes.
USH1G caused a non-syndromic hearing loss in a Dutch family. Compound heterozygous mutations in USH1G were found to segregate with the hearing loss, a missense (c.310A>G, p.Met104Val) and a frameshift mutation (c.780insGCAC, p.Tyr261Alafs*96).
In USH1G patients, mutations in SANS eliminate Magi2 bi (show MAGI2 ELISA Kits)nding and thereby deregulate endocytosis, lead to defective ciliary transport modules and ultimately disrupt photoreceptor cell function inducing retinal degeneration.
A novel p.S243X truncating mutation in USH1G that segregated with the disease phenotype has been identified in consanguineous Saudi Arabia siblings.
Pathogenic mutations in MYO7A (show MYO7A ELISA Kits), USH1C (show USH1C ELISA Kits), and USH1G have been found in four consanguineous Israeli Arab families with Usher syndrome type 1.
A role of the SANS-myomegalin (show PDE4DIP ELISA Kits) complex in microtubule-dependent inner segment cargo transport towards the ciliary base of photoreceptor cells.
crystal structure of MYO7A (show MYO7A ELISA Kits) MyTH4-FERM domains in complex with the central domain (CEN) of Sans at 2.8 angstrom resolution; MyTH4-FERM/CEN complex structure provides mechanistic explanations for known deafness-causing mutations in MYO7A (show MYO7A ELISA Kits) MyTH4-FERM
A frameshift mutation in SANS results in atypical Usher syndrome
Mutations in harmonin (show USH1C ELISA Kits) and Sans found in USH1 patients are shown to destabilize the complex formation of the two proteins
A novel D458V mutation in the USH1G PDZ (show INADL ELISA Kits) binding motif causes atypical Usher syndrome.
These results clearly show that the development of early-onset progressive hearing loss (ePHL) requires at least two mutant alleles of the Ush1g and Cdh23 (show CDH23 ELISA Kits) genes. Our results also suggest that because the SANS and CDH23 (show CDH23 ELISA Kits) proteins form a complex in the stereocilia, the interaction between these proteins may play key roles in the maintenance of stereocilia and the prevention of ePHL.
In Usher syndrome 1G, mutations in SANS eliminate Magi2 (show MAGI2 ELISA Kits) binding and thereby deregulate endocytosis, lead to defective ciliary transport modules and ultimately disrupt photoreceptor cell function inducing retinal degeneration.
USH1G (Sans) form the upper tip-link complex in adult mice
Usher type 1G protein sans is a critical component of the tip-link complex, a structure controlling actin polymerization in stereocilia.
we examine the effects of null mutation of the Ush1c (show USH1C ELISA Kits) gene on subcellular localization of Myo7a (show MYO7A ELISA Kits), Pcdh15 (show PCDH15 ELISA Kits) and Sans in the inner ear.
Sans may have an important role in development of the stereocilia bundles
This gene encodes a protein that contains three ankyrin domains, a class I PDZ-binding motif and a sterile alpha motif. The encoded protein interacts with harmonin, which is associated with Usher syndrome type 1C. This protein plays a role in the development and maintenance of the auditory and visual systems and functions in the cohesion of hair bundles formed by inner ear sensory cells. Mutations in this gene are associated with Usher syndrome type 1G (USH1G).
Usher syndrome type-1G protein
, scaffold protein containing ankyrin repeats and SAM domain
, Usher syndrome 1G homolog
, Usher syndrome type-1G protein homolog
, jackson shaker protein
, scaffold protein, amkyrin repeats and SAM domain containing
, scaffold protein, ankyrin repeats and SAM domain containing