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Rab11 and the associated motor protein Myosin V play essential roles in both endogenous and ectopic apical constriction, and might be involved in Vangl2 trafficking to the cell surface.
When actin and microtubules were present simultaneously, melanophilin's phosphorylation state enforced track selection of the Rab27a/melanophilin/myosin Va transport complex.
In the motor domain-IQ1/Ca(2+)-CaM structure, the N-lobe and the C-lobe of Ca(2+)-CaM adopt an open conformation and grip the C-terminal and the N-terminal portions of the IQ1, respectively.
The authors determined crystal structures of MyoVa-globular tail domain bound either to the Spir-2 motif or to Rab11 and show that a Spir-2:MyoVa:Rab11 complex can form.
function of two coupled myosin va motors on actin filaments and bundles
MyoVa-Ca(2+) channel interactions are required for proper long-range axon growth in developing spinal cord in vivo.
Myo5c-globular tail domain and Myo5a-globular tail domain are not interchangeable in terms of inhibiting the motor function.
This study showed that spontaneous Myo5a mutations causing cerebellar pathology are impaired in motor functions during the neonatal period.
These results visualize many of the critical unknown aspects of the stepping mechanism of myosin 5 including head-head coordination, the origin of lever-arm motion and the spatiotemporal dynamics of the translocating head during individual steps.
deletion mutation results in Griscelli syndrome type 3-like phenotype
Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.
Microtubules retard a centrifugal transport process that is dependent on myosin-Va and a population of dynamic F-actin. Functional analysis of mutant proteins indicates that myosin-Va works as a transporter dispersing melanosomes along actin tracks.
Normal physiological processes of relaxation of gastric and cavernosal smooth muscles that facilitate food accommodation and penile erection, respectively, may be disrupted under conditions of myosin Va deficiency.
Data demonstrate that myosin-Va is a component of a heterogeneous population of ribonucleoprotein particles of different sizes and composition, both in brain and peripheral nervous system
Myosin Va associates with FMRP and is required for its correct intracellular localisation.
MYO5A plays a role in the surface trafficking of Kv1.5 and connexin-43 but not KCNH2. It participates in anterograde trafficking
Data show at the single-molecule level that melanophilin (Mlph) increases the number of processively moving myoVa motors by 17-fold.
Introduction of a myosin 2-specific repulsive interaction into myosin 5a via the I67K mutation perturbs the strong-binding interaction of myosin 5a with actin.
This study demonistrated that Myosin Va mutant mouse with disruptions in glutamate synaptic development and mature plasticity in visual cortex in mice.
myosin Va has no non-redundant role in the secretion of dense and alpha-granules or other functional responses in platelets.
Data suggest that Rab27a and Rab27b regulate distinct steps in the bone marrow-derived mast cells (BMMC) degranulation pathway, with Rab27a/Mlph/MyoVa regulating cortical actin stability upstream of Rab27a/b/Munc13-4-dependent granule exocytosis.
our studies revealed RPGRIP1L as a novel MyoVa-binding protein - the first to be demonstrated to interact with MyoVa at the centrosome - and uncover an unprecedented link between MyoVa and ciliogenesis, providing new perspectives for studies aiming to better understand why defects in MyoVa cause neurological disorders in Griscelli syndrome patients.
MYO5A, having rare amino acid mutations p.R849Q and p.V1601G, was involved in the biological network of known MODY genes.
the essential melanocyte-specific transcription factor MITF regulates expression of the MYO5A gene, which encodes the molecular motor myosin-Va.
human cytomegalovirus capsids associate with nuclear myosin Va and F-actin and that antagonism of myosin Va impairs capsid localization toward the nuclear rim and nuclear egress.
Mechanochemical cycle of myosin-V has been reported.
Data suggest that membrane tethering mediated by endosomal RAB11A is drastically and selectively stimulated by its cognate Rab effectors, class V myosins (MYO5A and MYO5B), in a GTP-dependent manner. (RAB11A = ras-related GTPase Rab-11A; MYO5 = myosin class V)
ETV6-NTRK3, MYO5A-NTRK3 and MYH9-NTRK3 fusions are identified in Spitz tumours and demonstrated that NTRK3 fusions constitutively activate the mitogen-activated protein kinase, phosphoinositide 3-kinase and phospholipase Cgamma1 pathways in melanocytes.
the inhibited Myo5a is equilibrated between the folded state, in which the Mlph-binding site is buried, and the preactivated state, in which the Mlph-binding site is exposed, and that Mlph is able to bind to the Myo5a in preactivated state and activates its motor function.
These findings reveal a new fast-acting energy conservation strategy halting growth by immobilizing myosin V in a newly described state on selectively stabilized actin cables.
Structural insights into the globular tails of the human type v myosins Myo5a, Myo5b, And Myo5c.
Data indicate that myosin Va interacted with multiple new Rab subfamilies including Rab6, Rab14 and Rab39B.
several crystal structures of the myosin Va or the myosin Vb globular tail domain that gives insights into how the motor is linked to the recycling membrane compartments via Rab11 or the melanophilin adaptor that binds to Rab27a.
the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb, and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process
myosin-Va promotes adhesion dynamics, anchorage-independent survival, migration, and invasion in vitro
Myosin Va plays a role in the transport and turnover of mRNA. [Review]
Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a.
A Rab27a/MyRIP/myosin Va complex is involved in linking von-Willebrand factor (Vwf) to the peripheral actin cytoskeleton of endothelial cells to allow full maturation and prevent premature secretion of vWF.
Myo5a and Rab3A are direct binding partners and interact on synaptic vesicles and the Myo5a/Rab3A complex is involved in transport of neuronal vesicles
Myosin Va is required for P body but not stress granule formation.
Myo5a is activated in cells during HSV-1 infection to help transport virion- and glycoprotein-laden vesicles from the TGN, through the cortical actin, to the plasma membrane.
This gene is one of three myosin V heavy-chain genes, belonging to the myosin gene superfamily. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined.
, heavy polypeptide 12
, myosin VA (heavy polypeptide 12, myoxin)
, myosin Va
, myosin va
, dilute myosin heavy chain, non-muscle
, myosin 5a
, unconventional myosin-Va
, dilute lethal-20J protein
, myosin 5A
, myosin I heavy chain isoform
, myosin VA (heavy chain 12, myoxin)
, myosin heavy chain P190
, myosin V
, myosin, heavy polypeptide kinase