Browse our Myosin VI Proteins (MYO6)

Fruit Fly (Drosophila melanogaster) Myosin VI (MYO6) interaction partners

1. These observations support the notion that a major function of Myosin VI in the nerve terminal is tethering synaptic vesicles to proper sub-cellular location within the bouton

2. These data demonstrate that generating an organized and functional actin (show ACTB Proteins) structure in this cell requires multiple activities coordinated by myosin VI.

3. The androcam structure and its binding to the myosin VI structural (Insert 2) and regulatory (IQ) light chain sites are distinct from those of calmodulin.

4. data indicate that myosin V (show MYO5A Proteins) 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

5. MyoVI is required for border cell migration where it stabilizes E-cadherin (show CDH1 Proteins) and Arm.

6. Myosin VI is crucial for correct cell morphology and maintenance of adhesive cellular contacts within epithelial cell layers.

7. Myosin VI stabilizes a branched actin network in actin structures (cones) that mediate the separation of the syncytial spermatids. I

8. The spatial and temporal expression of Myosin VI was examined by expressing a Green Fluorescent Protein tagged Myosin VI molecule, under the control of a Myosin VI-Gal4 (show LGALS4 Proteins) line.

9. Data suggest that Echinoid mediates the dimerization of myosin VI/Jaguar in vivo which in turn regulates the reorganization and/or contraction of actin (show ACTB Proteins) filaments to control changes in cell shape.

10. Miranda protein forms an apical crescent at interphase, but is ubiquitously localized at prophase in a Myosin-II-dependent manner.

Human Myosin VI (MYO6) interaction partners

1. we describe a novel nonsense MYO6 mutation that was responsible for the hearing loss in a Brazilian family

2. this is the first ILDR1 (show ILDR1 Proteins) and MYO6 mutations recognized in the southwest Iran. Our data expands the spectrum of mutations in ILDR1 (show ILDR1 Proteins) and MYO6 genes

3. MYO6 could play an essential role in the growth of OSCC cells via regulation of cell cycle progression and apoptosis.

4. characterisation of the human myosin VI deafness mutant (R1166X) suggests that defects in cargo binding may leave myosin VI in a primed/activated state with an increased actin-binding ability

5. PRAS40 (show AKT1S1 Proteins) was downregulated in the DU145 cells following MYO6 knockdown.

6. knockdown of MYO6 slightly arrested cell cycle in G0/G1 phase, but remarkably increased the proportion of the sub-G1 phase of cell with the increase of apoptotic cells in colorectal cancer

7. study indicates that MYO6 may play an important role in gastric cancer tumorigenesis and may serve as a potential therapeutic target in human gastric cancer.

8. This study identified an isoform-specific regulatory helix, named the alpha2-linker, that defines specific conformations and hence determines the target selectivity of human myosin VI.

9. Interaction of myosin VI and its binding partner DOCK7 plays an important role in NGF (show NGFB Proteins)-stimulated protrusion formation in PC12 cells.

10. Knockdown of myosin VI significantly suppressed melanoma cell viability and proliferation.

Mouse (Murine) Myosin VI (MYO6) interaction partners

1. both AKT phosphorylation and RAC-dependent membrane ruffling were markedly reduced by depletion of either APPL1 or MYO6. These results place MYO6 and its binding partners at a central nexus in cellular signaling linking actin dynamics at the cell surface and endosomal signaling in the cell cortex.

2. GIPC1 (show GIPC1 Proteins) forms a domain-swapped dimer in an autoinhibited conformation that hinders binding of both PlexinD1 and myosin VI. PlexinD1 binding to GIPC1 (show GIPC1 Proteins) releases the autoinhibition, promoting its interaction with myosin VI. GIPCs and myosin VI interact through two distinct interfaces and form an open-ended alternating array.

3. indicated that decreased MYO6 levels in ksv/ksv mutants disrupt actin networks in the apical region of hair cells, thereby maintaining the normal structure of the cuticular plates and rootlets, and additionally provided a cellular basis for stereociliary fusion in Myo6 mutants

4. We propose that myosin VI, by removing stereociliary elements such as CDH23 (show CDH23 Proteins) as a component of the transient lateral links (which are probably required for the integrity of the immature hair bundles), allows the hair bundle and its transduction apparatus to progress in their development, so that the mechano-electrical transducer channels acquire their physiological resting tension and Ca2 (show CA2 Proteins)+-dependent adaptation properties

5. a plaque accretion defect as the primary manifestation of myosin VI loss in Cx43 (show GJA1 Proteins) homeostasis, is reported.

6. the Turner mutation was mapped to a critical region of 11 cM on chromosome 9 that includes myosin VI.

7. Myo1a (show MYO1A Proteins) and Myo6 play essential roles in response to intestinal mucosal injury

8. Disruption in optineurin (show OPTN Proteins) and myosin VI-mediated cellular trafficking is associated with amyotrophic lateral sclerosis.

9. We postulate that this novel interaction linking MVI with the PKA pathway could be important for targeting AKAP9-PKA complex within cells and/or providing PKA to phosphorylate MVI tail domain.

10. Dysfunction of myosin VI is associated with slow retinal optic neuropathy and age-related macular degeneration.

Pig (Porcine) Myosin VI (MYO6) interaction partners

1. Data suggest that cells direct the movement of vesicles around a cell by altering the relative number of myosin Va (show MYO5A Proteins) from Gallus gallus and myosin VI from Sus scrofa.

2. A myosin VI deafness mutation, D179Y, uncoupled the release of the ATP hydrolysis product, inorganic phosphate (Pi), from dependency on actin binding and destroyed the ability of single dimeric molecules to move processively on actin filaments.

3. model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling mode

4. The stepping dynamics of single quantum-dot-labeled myoV and myoVI motors linked to a common cargo, was studied.

5. These results suggest that myosin VI kinetics are tuned such that the motor maintains a consistent level of mechanical tension within the cell, a property potentially shared by other mechanosensitive proteins.

6. a mechanism is proposed of myosin VI stepping that predicts a regulation through load of the motor's roles as transporter and anchor

7. 2.4-A structure of a truncated version of the reverse-direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulin molecules

8. Data demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 mum in approximately 30 nm, hand-over-hand steps.

9. further adaptations within the motor increase the magnitude and variability of the plus-end directed converter movements, and unexpectedly provide the source of the highly variable myosin VI step size

10. Results suggest that myosin VI and vinculin (show VCL Proteins) form a molecular apparatus that generates cohesive cell-cell contacts in cultured mammalian epithelia.

Cow (Bovine) Myosin VI (MYO6) interaction partners

1. MVI, but not myosins IB or IIB, was detected in chromaffin granules isolated from bovine medulla and found to be tightly associated with the granule apical surface.