ATPase activity associated with the uncoating of clathrin baskets by Hsp70. 1994

W Barouch, and K Prasad, and L E Greene, and E Eisenberg
Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.

In the presence of ATP, bovine brain hsp70 has been shown to remove clathrin from bovine brain clathrin-coated vesicles in a rapid stoichiometric initial burst followed by slow steady-state uncoating. In addition, it has been found recently that a 100-kDa cofactor is required for hsp70 to uncoat clathrin baskets prepared with the assembly protein AP-2. In this study the ATPase activity associated with uncoating was investigated, with baskets formed from clathrin and assembly proteins. Mixed assembly proteins or assembly protein AP-2 could not be used in ATPase studies because they activated the hsp70 ATPase activity even in the absence of clathrin. However, this was not the case with assembly protein AP180. A stoichiometric initial burst of ATP hydrolysis was found to accompany the initial burst of uncoating of AP180-clathrin baskets by hsp70, with 1 mol of hydrolyzed ATP/mol of released clathrin heavy chain. Furthermore, the presence of a 100-kDa cofactor was needed for both processes. These results suggest that an initial burst of uncoating occurs with all clathrin baskets, that an initial burst of ATP hydrolysis accompanies this initial burst of uncoating, and that a 100-kDa cofactor is required for both.

UI MeSH Term Description Entries
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002966 Clathrin The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D018840 HSP70 Heat-Shock Proteins A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures. Heat-Shock Proteins 70,Heat Shock 70 kDa Protein,Heat-Shock Protein 70,HSP70 Heat Shock Proteins,Heat Shock Protein 70,Heat Shock Proteins 70,Heat-Shock Proteins, HSP70

Related Publications

W Barouch, and K Prasad, and L E Greene, and E Eisenberg
February 2005, The Journal of biological chemistry,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
September 1993, Plant physiology,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
April 1990, The Journal of biological chemistry,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
January 1987, The Journal of biological chemistry,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
March 1994, The Journal of biological chemistry,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
April 1988, Journal of molecular biology,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
January 1984, Nature,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
July 2006, Molecular biology of the cell,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
February 1994, The Journal of biological chemistry,
W Barouch, and K Prasad, and L E Greene, and E Eisenberg
March 1995, Journal of cell science,
Copied contents to your clipboard!