Myosin VI: cellular functions and motor properties
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منابع مشابه
Myosin VI: cellular functions and motor properties.
Myosin VI has been localized in membrane ruffles at the leading edge of cells, at the trans-Golgi network compartment of the Golgi complex and in clathrin-coated pits or vesicles, indicating that it functions in a wide variety of intracellular processes. Myosin VI moves along actin filaments towards their minus end, which is the opposite direction to all of the other myosins so far studied (to ...
متن کاملMyosin VI: a multifunctional motor.
Myosin VI moves towards the minus end of actin filaments unlike all the other myosins so far studied, suggesting that it has unique properties and functions. Myosin VI is present in clathrin-coated pits and vesicles, in membrane ruffles and in the Golgi complex, indicating that it has a wide variety of functions in the cell. To investigate the cellular roles of myosin VI, we have identified a v...
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All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent on the quality of the copy submitted. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. ABSTRACT Myosin VI is one of the myosin superfamily members that are acti...
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New work shows that the motor protein myosin VI, acting through vinculin, plays a key role in the maturation of cadherin-based adherens junctions in epithelial cells.
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The recent discovery that the class VI myosin is minus end-directed (Schliwa, 1999; Wells et al., 1999) allows new mechanisms of actin-based motility to exist in cells. This will prompt reexamination of a broad range of cell movements previously difficult to explain by conventional force generating mechanisms. Myosins are a large family of molecular motor proteins divided into 15 or more classe...
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ژورنال
عنوان ژورنال: Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
سال: 2004
ISSN: 0962-8436,1471-2970
DOI: 10.1098/rstb.2004.1563