Disease relevance of MYO1A

• Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line [1].
• Higher BBMI was predictive of a lower long-term weight gain, while dose was not a significant predictor of greater longer term weight change [2].

High impact information on MYO1A

• In contrast, arcs and rings contained no apparent enrichment of microtubules, brush border myosin-I immunogens, or myosin-V [3].
• MYO1A, which is located within the DFNA48 locus, is the first myosin I family member found to be involved in causing deafness and may be a major contributor to autosomal dominant-hearing loss [4].
• Here, we report the identification of a nonsense mutation, of a trinucleotide insertion leading to an addition of an amino acid, and of six missense mutations in MYO1A cDNA sequence in a group of hearing-impaired patients from Italy [4].
• Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss [4].
• We determined the rates for ATP binding to BBM-I and brush border actomyosin-I (actoBBM-I), the rate of actoBBM-I dissociation by ATP, and the rates for the steps in ADP dissociation from actoBBM-I [5].

Biological context of MYO1A

• To analyze whether a myosin was involved in endocytosis, we produced, in this polarized cell line, truncated, non-functional, brush border, myosin I proteins (BBMI) that we have previously demonstrated to have a dominant negative effect on endocytosis of unpolarized cells [6].

Anatomical context of MYO1A

• MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells [7].
• In situ hybridization indicated that BBMI mRNA localized to the basal region of human enterocytes, whereas the mRNA for I-fim distributed diffusely [8].
• Staining of tissue sections with these antibodies was specifically localized to the brush-border microvilli of small intestines, indicating an identical cellular localization for both MIHC and the 110-kDa protein [9].
• Brush border myosin-I (BBM-I) is a single-headed unconventional myosin found in the microvilli of intestinal epithelial cells [5].
• Using the techniques of cryoelectron microscopy and helical image analysis we have calculated three-dimensional (3D) maps of BBMI-decorated actin filaments prepared in the presence and absence of calcium [10].

Other interactions of MYO1A

• The identity of this myosin as human brush border myosin-I was verified based on similarity with other vertebrate sequences, as well as its expression profile at both the RNA and protein levels [11].
• Sequence analysis revealed no obvious similarity between the 3'-UTRs of BBMI and villin [8].

Analytical, diagnostic and therapeutic context of MYO1A

• Baseline body mass index (BBMI; kg/m2) and dose (mg/day) were investigated as predictors of long-term weight change experienced during olanzapine treatment [2].

References