Keep the traffic moving: mechanism of the Hsp70 motor.
Hsp70s are ubiquitous chaperones that use ATP hydrolysis to drive a variety of protein processing reactions, including a number of steps in protein trafficking. Recent studies have shed light on how ATP might generate conformational changes in an Hsp70 molecule and how such changes might be harnessed to drive processes as diverse as protein import into subcellular organelles and uncoating of clathrin-coated vesicles.
Sousa
Rui
R
Department of Biochemistry, University of Texas Health, Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA. Sousa@biochem.uthscsa.edu
Lafer
Eileen M
EM
D000818:Animals; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism*; D009711:Nucleotides / Q000737:chemistry / Q000378:metabolism; D015388:Organelles / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport
D018840:HSP70 Heat-Shock Proteins; D020409:Molecular Motor Proteins; D009711:Nucleotides