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Immediately after clathrin-coated pits pinch off from the cell membrane to form clathrin-coated vesicles, clathrin dissociates from the vesicles. In vitro studies suggest that this dissociation is carried out by the uncoating ATPase, a constitutive member of the 70-kDa heat shock family. Aside from the requirement for ATP, nothing is known about the regulation of the uncoating process. We now show that clathrin baskets prepared from highly purified clathrin and AP2, the assembly protein associated with plasma membrane coated vesicles, cannot be uncoated by the bovine brain uncoating ATPase alone. A 100-kDa protein cofactor, which was isolated from coated vesicles, is essential for uncoating by the uncoating ATPase. This cofactor restores normal uncoating when present at a molar ratio of about 1 to 10 to clathrin and uncoating ATPase.
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
February 2005,
The Journal of biological chemistry,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
January 1987,
The Journal of biological chemistry,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
September 1993,
Plant physiology,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
January 1984,
Nature,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
March 1994,
The Journal of biological chemistry,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
April 1990,
The Journal of biological chemistry,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
April 1988,
Journal of molecular biology,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
December 2000,
Nature cell biology,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
November 1985,
The Journal of biological chemistry,
K Prasad, and
W Barouch, and
L Greene, and
E Eisenberg
September 1989,
The Journal of biological chemistry,
