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Cells expressing excess of MYO1C had low basal level of phosphorylated protein kinase B (show AKT1 Antibodies).
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 (show H2AFX Antibodies) signaling.
The ERK (show EPHB2 Antibodies) signaling pathway thus promotes cell motility through regulation of the subcellular localization of Myo1E (show MYO1E Antibodies).
Study presents structural demonstration of a cargo protein, Neph1 (show NEPH1 Antibodies), 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 (show INPPL1 Antibodies). SHIP2 (show INPPL1 Antibodies) 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.
Coinheritance of COL4A5 (show COL4a5 Antibodies) and MYO1E (show MYO1E Antibodies) mutations accentuate the severity of kidney disease.
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 (show KPTN Antibodies) tropomyosin 2 (show TPM2 Antibodies) abolishes Myo1c-specific effects on both run initiation and run termination.
NM1 phosphorylation by GSK3beta (show GSK3b Antibodies) blocks NM1 ubiquitination by UBR5 (show UBR5 Antibodies) and degradation by the proteasome, leads to NM1 association with the chromatin and promotes rDNA transcription activation at G1.
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 (show DPT Antibodies) 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 (show ALDH1A2 Antibodies) brings to the cell nucleus not only the "nuclear" isoform of myosin I (show MYO1A Antibodies) (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 (show SGMS2 Antibodies), were measured.
Results indicate a potential role for Myo1 (show DNAH8 Antibodies) 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.
Vectorial transport of G-actin (show ACTB Antibodies) was shown in live migrating endothelial cells. Myo1c (an unconventional F-actin-binding motor protein (show MYO7A Antibodies)) was identified as a major G-actin (show ACTB Antibodies)-interacting protein. The cargo-binding tail domain of Myo1c interacted with G-actin (show ACTB Antibodies).
This gene encodes a member of the nonmuscle class I myosins which are a subgroup of the unconventional myosin protein family. The unconventional myosin proteins function as actin-based molecular motors. Class I myosins are characterized by a head (motor) domain, a regulatory domain and a either a short or long tail domain. Among the class I myosins, this protein is distinguished by a long tail domain that is involved in crosslinking actin filaments. This protein localizes to the cytoplasm and may be involved in intracellular movement and membrane trafficking. Mutations in this gene are the cause of focal segmental glomerulosclerosis-6. This gene has been referred to as myosin IC in the literature but is distinct from the myosin IC gene located on chromosome 17.
, nuclear myosin 1
, 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
, MYO1E variant protein
, unconventional myosin 1E
, unconventional myosin-Ie
, Myosin I beta