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Rab11 (zeige RAB11A Proteine) 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.
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 (zeige SPIRE2 Proteine) motif or to Rab11 (zeige RAB11A Proteine) and show that a Spir-2 (zeige SPIRE2 Proteine):MyoVa:Rab11 complex can form.
function of two coupled myosin va motors on actin filaments and bundles
MyoVa-Ca(2 (zeige CA2 Proteine)+) 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.
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.
human cytomegalovirus capsids associate with nuclear myosin Va and F-actin and that antagonism of myosin Va impairs capsid localization toward the nuclear rim (zeige RBBP8 Proteine) 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 (zeige MLPH Proteine)-binding site is buried, and the preactivated state, in which the Mlph (zeige MLPH Proteine)-binding site is exposed, and that Mlph (zeige MLPH Proteine) 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 (zeige HRB Proteine) subfamilies including Rab6 (zeige RAB6A Proteine), Rab14 (zeige RAB14 Proteine) and Rab39B (zeige RAB39B Proteine).
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 (zeige RAB11A Proteine) or the melanophilin (zeige MLPH Proteine) adaptor that binds to Rab27a (zeige RAB27A Proteine).
the cargo-binding domain (CBD (zeige OPN1MW Proteine)) 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 (zeige OPN1MW Proteine) dimerization process
Calmodulin (zeige KRIT1 Proteine) bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a.
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