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Kinesin Protocols (Hardcover, 2001 ed.)
Loot Price: R3,180
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Kinesin Protocols (Hardcover, 2001 ed.)
Series: Methods in Molecular Biology, 164
Expected to ship within 12 - 17 working days
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By the end of the 1980s only two microtubule-dependent motors, the
plus end-directed kinesin and the minus end-directed cytoplasmic
dynein, had been identified. At the time, these two motors seemed
almost sufficient to explain directional motility events on polar
microtubule tracks in the cell. No- theless, shortly after, the tip
of the iceberg began to emerge with the identi- cation of proteins
containing in their sequences a domain found in kinesin. This
domain, called the "motor domain," conferred on these proteins the
essential property of moving on microtubules, using the energy
derived from ATP hydro- sis. Since then, the identification of new
proteins belonging to the kinesin superfamily of
microtubule-dependent motors has gone at such a pace that nowadays
more than 200 entries with motor domain sequences are deposited in
the database. Kinesin family members are found in all eukaryotic
org- isms tested. They present a wide range of domain organizations
with a motor domain located at different positions in the molecule.
Their motility prop- ties are also variable in directionality,
velocity, and such other characteristics as bundling activity and
processivity. Finally, and most important, they p- ticipate in a
multitude of cellular functions. Our understanding of many cel- lar
events, such as mitotic spindle assembly and neuronal transport, to
cite only two, has progressed substantially in the last few years
thanks to the id- tification of these motors.
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