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E2 and NM1 associate via their N-terminal domains and this interaction is ATP dependent.
The results establish a mechanistic connection between the calcium regulation of the motor function of myosin IC in the cytoplasm and the induction of its import into the nucleus.
NTR(35), which harbors the R21G mutation, was unable to confer MYO1C(35)-like kinetic behavior. Thus, the NTRs affect the specific nucleotide-binding properties of MYO1C isoforms, adding to their kinetic diversity. We propose that this level of fine-tuning within MYO1C broadens its adaptability within cells.
Cells expressing excess of MYO1C had low basal level of phosphorylated protein kinase B.
Upon DNA damage, an increase in the levels of chromatin bound motor protein nuclear myosin 1 (NM1) ensues, which appears to be functionally linked to Upsilon-H2AX signaling.
Study presents structural demonstration of a cargo protein, Neph1, attached to Myo1c, providing novel insights into the role of Myo1c in intracellular movements of this critical slit diaphragm protein.
In glioblastoma 1321 N1 cells, we recently identified Myo1c as a new interactor of SHIP2. SHIP2 localization at lamellipodia and ruffles is impaired in Myo1c depleted cells. In the absence of Myo1c, N1 cells tend to associate to form clusters.
Overexpression of MYO1C is associated with gastric cancer.
Ablating MYO1C function causes abnormal cholesterol distribution, which has a major selective impact on the autophagy pathway
Myo1c significantly increases the frequency of kinesin-1-driven microtubule-based runs that begin at actin/microtubule intersections. The actin-binding protein tropomyosin 2 abolishes Myo1c-specific effects on both run initiation and run termination.
NM1 phosphorylation by GSK3beta blocks NM1 ubiquitination by UBR5 and degradation by the proteasome, leads to NM1 association with the chromatin and promotes rDNA transcription activation at G1.
The relationship between MYO1C and KAT6B suggests that the two are interacting in chromatin remodelling for gene expression in human masseter muscle. This is the nuclear myosin1 (NM1) function of MYO1C.
myosin 1c manipulations lead to loss of the actin filaments and to similar endoplasmic reticulum phenotype as observed after actin depolymerization.
The structural context and the chemical environment of Myo1c mutations that are involved in sensorineural hearing loss in humans are described and their impact on motor function is discussed.
These results suggest a unique structural role for NM1 in which the interaction with SNF2h stabilizes B-WICH at the gene promoter and facilitates recruitment of the HAT PCAF
Both nucleolar localization signals are functional and necessary for nucleolar localization of specifically myosin IC isoform B.
This is the first report demonstrating that Myo1c is an important mediator of VEGF-induced VEGFR2 delivery to the cell surface and plays a role in angiogenic signaling.
Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion.
Myo1c plays a critical role in the translocation of Neph1 complexes in podocytes. Myo1c's ability to interact with membranes, F-actin, Neph1, and nephrin indicates that it actively contributes to the dynamic organization of the filtration slit.
NM1 facilitates maturation and accompanies export-competent preribosomal subunits to the nuclear pore complex, thus modulating export.
Myo1c ensembles can generate forces parallel to lipid bilayers.
We propose a novel genome-wide mechanism where myosin synergizes with Pol II-associated actin to link the polymerase machinery with permissive chromatin for transcription activation.
Our observations demonstrate specific changes in the expression of myosin IC isoform A that are concurrent with the occurrence of prostate cancer in the TRAMP mouse prostate cancer model that closely mimics clinical prostate cancer
Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail.
The v-Crk-myosin-1c interaction, which modulates membrane dynamics by regulating Rac1 activity, is crucial for cell adhesion and spreading.
Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus.
Myo1c functions as a slow transporter rather than a tension-sensitive anchor.
the novel specific NLS brings to the cell nucleus not only the "nuclear" isoform of myosin I (NM1 protein) but also its "cytoplasmic" isoform (Myo1c protein)
The data suggest that Myosin 1c is involved in the cytoskeleton dynamics and membrane protein anchoring or sorting in B lymphocytes
A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity
The strength and attachment lifetime of single myo1c molecules as they bind beads coated with a bilayer of 2% phosphatidylinositol 4,5-bisphosphate and 98% phosphatidylcholine, were measured.
Myo1c is a novel mediator of both insulin-stimulated and contraction-stimulated glucose uptake in skeletal muscle.
Mutations in the Myo1c gene affect the interaction of Myo1c with nucleotides and actin.
myosin Myo1c functions in a PI(3)K-independent insulin signalling pathway that controls the movement of intracellular GLUT4-containing vesicles to the plasma membrane
localized membrane remodeling driven by the Myo1c motor appears to facilitate the fusion of exocytic GLUT4-containing vesicles with the adipocyte plasma membrane
These data are consistent with Myo1c participating in the regulation of the Na+ channel after antidiuretic hormone stimulation.
These results suggest that mechanical activity of myosin-1c is required for fast adaptation in vestibular hair cells.
myo1c does not bind to physiological concentrations of phosphatidylserine but rather binds tightly to phosphatidylinositol 4,5-bisphosphate
Motor protein Myo1c and its receptor protein NEMO act cooperatively to form the IKK-IRS-1 complex and function in TNF-alpha-induced insulin resistance.
Subcellular localization of class I and class II myosin during B cell spreading showed differences, following CD44 cross-linking, myosin-1c was polarized to lamellipodia while the distribution of cytosplasmic nonmuscle class II myosin was not altered.
Vectorial transport of G-actin was shown in live migrating endothelial cells. Myo1c (an unconventional F-actin-binding motor protein) was identified as a major G-actin-interacting protein. The cargo-binding tail domain of Myo1c interacted with G-actin.
XlMyo1c couples polymerizing actin to membranes and so mediates force production during compensatory endocytosis.
Results indicate a potential role for Myo1 in the maintenance and formation of furrow, blastodisc morphology, cell-division and lipid droplets (LDs) organization within the blastodisc during early embryogenesis.
Myo1c is necessary for podocyte morphogenesis.
Patronin and Shot then act to polarise microtubules along the apical-basal axis to enable apical transport of Rab11 endosomes by the Nuf-Dynein microtubule motor complex. Finally, Rab11 endosomes are transferred to the MyoV (also known as Didum in Drosophila) actin motor to deliver the key microvillar determinant Cadherin 99C to the apical membrane to organise the biogenesis of actin microvilli.
data indicate that myosin V and VI, but not II, play related but distinct roles in regulating microtubule (MT)-based mitochondrial movement: they oppose, rather than complement, protracted MT-based movements and perhaps facilitate organelle docking
the mechanical properties of coiled-coil regions of myosin v
analysis of the motor mechanism of Drosophila Myosin V
MyoV was associated with membranes, microtubule, and actin structures required for spermatid maturation.
Myosin V delivers morphogenic secretory traffic along polarized actin filaments of the subcortical terminal web to the exocytic plasma membrane target, the rhabdomere base.
Data show that didum, encoding the Drosophila actin-based motor Myosin-V, is a new posterior group gene that promotes posterior accumulation of Oskar.
This gene encodes a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus. The nuclear isoform associates with RNA polymerase I and II and functions in transcription initiation. The mouse ortholog of this protein also functions in intracellular vesicle transport to the plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene. The related gene myosin IE has been referred to as myosin IC in the literature, but it is a distinct locus on chromosome 19.
myosin I beta
, myosin-I beta
, nuclear myosin I
, unconventional myosin-Ic
, nuclear myosin I beta
, myosin IC-like
, myosin heavy chain myr 2
, unconventional myosin Myr2 I heavy chain
, nuclear myosin 1
, myosin IC
, Myosin I beta
, Myosin I beta-A
, unconventional myosin-Ic-A
, CG2146 gene product from transcript CG2146-RA
, myosin V