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Myosin IA

brush border myosin I, BBMI, myosin IA, MYO1A
This gene encodes a member of the myosin superfamily. The protein represents an unconventional myosin; it should not be confused with the conventional skeletal muscle myosin-1 (MYH1). Unconventional myosins contain the basic domains characteristic of conventional myosins and are further distinguished from class members by their tail domains. They function as actin-based molecular motors. Mutations in this gene have been associated with autosomal dominant deafness. Alternatively spliced variants have been found for this gene. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: Actin, ATPase, myosin I, CAN, ACID
Papers on brush border myosin I
Variants in the genes DCTN2, DNAH10, LRIG3, and MYO1A are associated with intermediate Charcot-Marie-Tooth disease in a Norwegian family.
New
Russell et al., Oslo, Norway. In Acta Neurol Scand, Nov 2015
Exome sequencing revealed a singular heterozygous shared haplotype containing four genes, DCTN2, DNAH10, LRIG3, and MYO1A, with novel sequence variants.
Restoration of cytoskeletal and membrane tethering defects but not defects in membrane trafficking in the intestinal brush border of mice lacking both myosin Ia and myosin VI.
New
Mooseker et al., New Haven, United States. In Cytoskeleton (hoboken), Sep 2015
Myosin Ia (Myo1a), the most prominent plus-end directed motor and myosin VI (Myo6) the sole minus-end directed motor, together exert opposing tension between the microvillar (MV) actin core and the apical brush border (BB) membrane of the intestinal epithelial cell (IEC).
Targeted Exome Sequencing of Deafness Genes After Failure of Auditory Phenotype-Driven Candidate Gene Screening.
New
Choi et al., Seoul, South Korea. In Otol Neurotol, Jul 2015
Additionally, we also recapitulated the recent finding from other report arguing for the non-pathogenic potential of MYO1A variant.
Analysis of Low Frequency Protein Truncating Stop-Codon Variants and Fasting Concentration of Growth Hormone.
Melander et al., Malmö, Sweden. In Plos One, 2014
rs121909305 (NP_005370.1:p.R93*) [Minor Allele Frequency (MAF) = 0.8%] in the Myosin 1A gene (MYO1A) was associated with a 0.36 (95%CI, 0.04 to 0.54; p=0.02) increment of the standardized value of the natural logarithm of hs-GH per 1 minor allele and rs35699176 (NP_067040.1:p.Q100*) in the Zink Finger protein 77 gene (ZNF77) (MAF = 4.8%) was associated with a 0.12 (95%CI, 0.02 to 0.22; p = 0.02) increase of hs-GH.
The effect of novel mutations on the structure and enzymatic activity of unconventional myosins associated with autosomal dominant non-syndromic hearing loss.
Choi et al., Taegu, South Korea. In Open Biol, 2014
These genes encode the motor proteins myosin IA, IIIA, VI, VIIA and XVA.
Targeted and genomewide NGS data disqualify mutations in MYO1A, the "DFNA48 gene", as a cause of deafness.
Bolz et al., Nieder-Ingelheim, Germany. In Hum Mutat, 2014
MYO1A is considered the gene underlying autosomal dominant nonsyndromic hearing loss DFNA48, based on six missense variants, one small in-frame insertion, and one nonsense mutation.
Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.
Tyska et al., Nashville, United States. In Biophys J, 2014
To address this, we used single molecule total internal reflection fluorescence microscopy to examine the dynamics of the well-characterized myosin-1a isoform during interactions with the cortex of living cells.
Brush border myosin Ia inactivation in gastric but not endometrial tumors.
Arango et al., Barcelona, Spain. In Int J Cancer, 2013
Brush border Myosin Ia (MYO1A) has been shown to be frequently mutated in colorectal tumors with microsatellite instability (MSI) and to have tumor suppressor activity in intestinal tumors.
Myosin Ia is required for CFTR brush border membrane trafficking and ion transport in the mouse small intestine.
Ameen et al., New Haven, United States. In Traffic, 2012
The subapical localization of Myo6 is dependent on myosin Ia (Myo1a) the major plus-end motor associated with the BBM, suggestive of functional synergy between these two motors.
Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain.
GeneRIF
Tyska et al., Nashville, United States. In J Biol Chem, 2012
Myo1a targeting to microvilli is driven by membrane binding potential that is distributed throughout TH1 rather than localized to a single motif.
Brush border myosin Ia has tumor suppressor activity in the intestine.
GeneRIF
Arango et al., Barcelona, Spain. In Proc Natl Acad Sci U S A, 2012
results identify MYO1A as a unique tumor-suppressor gene in colorectal cancer and demonstrate that the loss of structural brush border proteins involved in cell polarity are important for tumor development
Myosin I can act as a molecular force sensor.
Impact
GeneRIF
Ostap et al., Philadelphia, United States. In Science, 2008
Sensing molecular tension is crucial for a wide array of cellular processes. Myosin I dramatically alters its motile properties in response to tension.
Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a.
GeneRIF
Tyska et al., In Biophys J, 2008
These data are the first to suggest that mechanical activity is essential for proper localization of Myo1a in microvilli.
From transcription to transport: emerging roles for nuclear myosin I.
GeneRIF
de Lanerolle et al., Chicago, United States. In Biochem Cell Biol, 2006
This movement is based on an active and directed process that is facilitated by an acto-NMI complex, establishing for the first time a functional role for a motor complex consisting of actin and a myosin in the nucleus.
A 32 degree tail swing in brush border myosin I on ADP release.
Impact
Milligan et al., Los Angeles, United States. In Nature, 1996
Brush border myosin I (BBMI) is a single-headed, unconventional myosin from intestinal microvilli, composed of a heavy chain of relative molecular mass 119,000 (M(r) 119K) and three calmodulin light chains.
Molecular evolution of the myosin superfamily: application of phylogenetic techniques to cell biological questions.
Review
Goodson, Stanford, United States. In Soc Gen Physiol Ser, 1993
Furthermore, brush border myosin I, a type of protein initially thought to be specific to specialized metazoan tissues, probably has relatives that are much more broadly distributed.
Differential regulation of vertebrate myosins I and II.
Review
Matsudaira et al., Cambridge, United States. In J Cell Sci Suppl, 1990
The activities and regulation of brush border myosin I provide insight into conserved and unique features of the myosin mechanoenzymes and suggest how the functions of myosins I and II are divided in vertebrate cells.
Myosin I: a new insight into the mechanism and cellular significance of actin-based motility.
Review
Matsudaira et al., Cambridge, United States. In Adv Biophys, 1990
From our work on brush border myosin I structure, activity, regulation, and function, we can begin to understand the significance of the diversification of myosin proteins.
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