MYO6 Antibody - #DF9654

Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription.

Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK).

Golgi apparatus>trans-Golgi network membrane>Peripheral membrane protein. Golgi apparatus. Nucleus. Cytoplasm>Perinuclear region. Membrane>Clathrin-coated pit. Cytoplasmic vesicle>Clathrin-coated vesicle. Cell projection>Filopodium. Cell projection>Ruffle membrane. Cell projection>Microvillus. Cytoplasm>Cytosol.
Note: Also present in endocyctic vesicles (PubMed:16507995). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (PubMed:16507995). Recruited into membrane ruffles from cell surface by EGF-stimulation (PubMed:9852149). Colocalizes with DAB2 in clathrin-coated pits/vesicles (PubMed:11967127). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity).

Cytoplasmic vesicle>Clathrin-coated vesicle membrane.

Cytoplasmic vesicle>Clathrin-coated vesicle membrane. Cell projection>Ruffle membrane.

Expressed in most tissues examined including heart, brain, placenta, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon. Highest levels in brain, pancreas, testis and small intestine. Also expressed in fetal brain and cochlea. Isoform 1 and isoform 2, containing the small insert, and isoform 4, containing neither insert, are expressed in unpolarized epithelial cells.

Homodimer; dimerization seems to implicate the unfolding of the three-helix bundle region creating an additional calmodulin binding site, and cargo binding (By similarity). Able to function as a monomer under specific conditions in vitro. Forms a complex with CFTR and DAB2 in the apical membrane of epithelial cells. Component of the DISP/DOCK7-induced septin displacement complex, at least composed of DOCK7, LRCH3 and MYO6. Binding to calmodulin through a unique insert, not found in other myosins, located in the neck region between the motor domain and the IQ domain appears to contribute to the directionality reversal (By similarity). This interaction occurs only if the C-terminal lobe of calmodulin is occupied by calcium (By similarity). Interaction with F-actin/ACTN1 occurs only at the apical brush border domain of the proximal tubule cells (By similarity). Interacts with DAB2. In vitro, the C-terminal globular tail binds a C-terminal region of DAB2 (By similarity). Interacts with CFTR. Interacts with OPTN (By similarity). Interacts with CABP5 (By similarity).

Divided into three regions: a N-terminal motor (head) domain, followed by a neck domain consisting of a calmodulin-binding linker domain and a single IQ motif, and a C-terminal tail region with a three-helix bundle region, a SAH domain and a unique globular domain required for interaction with other proteins such as cargo-binding.

The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds (PubMed:18511944). Its contribution to the mechanism confering the myosin movement on actin filaments is debated (PubMed:18511944).

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.