Slipping up: partial substrate degradation by ATP-dependent proteases.
ATP-dependent proteases are present in all organisms, where they are responsible for much of intracellular protein degradation. Most proteins are processively unfolded and degraded into small peptides; however, in a few so-called slippery substrates, the protease stalls at a folded domain and releases a large protein fragment. In this review, we describe the properties of physiological slippery substrates that are processed in this manner by ATP-dependent proteases and the recent advances that have been made in understanding the mechanism underlying their partial degradation.
Department of Chemistry, Villanova University, Villanova, PA, USA.
Nicholas D
ND
Nassif
Samantha E
SE
Cambray
Daniel A
DA
Kraut
D049069:ATP-Dependent Proteases / Q000737:chemistry / Q000502:physiology*; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000502:physiology; D017434:Protein Structure, Tertiary; D059748:Proteolysis; D057149:Ubiquitinated Proteins / Q000378:metabolism
D001426:Bacterial Proteins; D010446:Peptide Fragments; D057149:Ubiquitinated Proteins; D049069:ATP-Dependent Proteases; D046988:Proteasome Endopeptidase Complex
ATP-dependent protease; chaperones; proteasome; protein degradation