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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 (zeige AKT1 Proteine).
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 (zeige H2AFX Proteine) signaling.
Study presents structural demonstration of a cargo protein, Neph1 (zeige NEPH1 Proteine), 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 (zeige INPPL1 Proteine). SHIP2 (zeige INPPL1 Proteine) 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 (zeige KPTN Proteine) tropomyosin 2 (zeige TPM2 Proteine) 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.
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 (zeige DPT Proteine) 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 (zeige ALDH1A2 Proteine) brings to the cell nucleus not only the "nuclear" isoform of myosin I (zeige MYO1A Proteine) (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 (zeige SGMS2 Proteine), were measured.
Vectorial transport of G-actin (zeige ACTB Proteine) was shown in live migrating endothelial cells. Myo1c (an unconventional F-actin-binding motor protein) was identified as a major G-actin (zeige ACTB Proteine)-interacting protein. The cargo-binding tail domain of Myo1c interacted with G-actin (zeige ACTB Proteine).
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 (zeige MYO5A Proteine) 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 (zeige MYO5A Proteine)
analysis of the motor mechanism of Drosophila Myosin V (zeige MYO5A Proteine)
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 (zeige ACTB Proteine)-based motor Myosin-V (zeige MYO5A Proteine), 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-A
, unconventional myosin-Ic-A
, CG2146 gene product from transcript CG2146-RA
, myosin V