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3. Small globular head: Binds to vesicles via adaptors Kinesins are a large family; each member has
specialized roles in the cell Kinesin superfamily motor proteins and intracellular transport. Hirokawa N, Noda Y, Tanaka Y,
Niwa S. Nat Rev Mol Cell Biol. 2009 Oct;10(10):682-96. Kinesin movement is ATP-dependent Kinesin families Catastrophe
Traffic control: regulation of kinesin motors. Verhey KJ, Hammond JW. Nat Rev Mol Cell Biol.
2009 Nov;10(11):765-77. Figure 16-62 Molecular Biology of the Cell (© Garland Science 2008) Kinesin processivity
1. Kinesin head contains ADP before binding to
2. Microtubule binding causes ADP release and
replacement with ATP
3. ATP binding causes neck linker to bind to
catalytic core, throwing the other head forward
4. Trailing head hydrolyzes ATP, releasing
phosphate, and the neck attachment
5. Leading head exchanges ADP for ATP and
the cycle resumes. Animation of kinesin dynamics Ron Vale lab Animation of kinesin dynamics Ron Vale lab Molecular structure of dyneins
kinesin dynein Dyneins - composed of 2-3 heavy chains with total MW of 1,000kD
and several light chains
Like Kinesins, Dyneins use ATP to move processively along
microtubules Two major families of dyneins Figure 16-59 Molecular Biology of the Cell (© Garland Science 2008) Cytoplasmic Dynein Ron Vale lab Basic Structure of Cilia and Flagella
Inner dynein Bridge connecting
Plasma membrane Outer dynein
arm Central p...
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This note was uploaded on 02/23/2014 for the course MCDB 165A taught by Professor Iruela-arispe during the Winter '08 term at UCLA.
- Winter '08