Mira Krendel and Mark S . Mooseker Myosins : Tails ( and Heads ) of Functional Diversity
نویسنده
چکیده
منابع مشابه
Myosin 1E interacts with synaptojanin-1 and dynamin via its SH3 domain
Myosin 1E is one of two “long-tailed” human Class I myosins that contain an SH3 domain within the tail region. SH3 domains of yeast and amoeboid myosins I interact with activators of the Arp2/3 complex, an important regulator of actin polymerization. No binding partners for the SH3 domains of myosins I have been identified in higher eukaryotes. In the current study, we show that two proteins wi...
متن کاملDisruption of Myosin 1e promotes podocyte injury.
Myosin 1e (Myo1e) is one of two Src homology 3 domain-containing "long-tailed" type I myosins in vertebrates, whose functions in health and disease are incompletely understood. Here, we demonstrate that Myo1e localizes to podocytes in the kidney. We generated Myo1e-knockout mice and found that they exhibit proteinuria, signs of chronic renal injury, and kidney inflammation. At the ultrastructur...
متن کاملMyosin Superfamily: Diversity of Structural Motifs and Mechanochemical Properties
that use the energy of ATP hydrolysis to move along actin filaments. In the past 20 years many novel members of the myosin superfamily have been identified, with 16 new myosin classes joining founding members of this protein family: Myo1 and 2.* Several recent reviews have discussed the myosins’ functions, with particular focus on Myo6, Myo1c, and Myo5, and the role of myosins in sensory functi...
متن کاملMyosin-IXb is a single-headed and processive motor.
Class IX myosins are unique among the many classes of known actin-based motors in that the tail region of these myosins contains a GTPase-activating protein domain for the small GTP-binding protein, Rho. Previous studies on human myosin-IXb indicate that this myosin is mechanochemically active and exhibits actin-binding properties similar to the processive motor, myosin-Va. Motility analysis of...
متن کاملBrain myosin-V is a two-headed unconventional myosin with motor activity.
Chicken myosin-V is a member of a recently recognized class of myosins distinct from both the myosins-I and the myosins-II. We report here the purification, electron microscopic visualization, and motor properties of a protein of this class. Myosin-V molecules consist of two heads attached to an approximately 30 nm stalk that ends in a globular region of unknown function. Myosin-V binds to and ...
متن کامل