The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation.
In this review we briefly describe the lysosomal system, consider the evidence for multiplicity of protein degradation pathways in vivo, discuss in detail the ubiquitin-mediated pathway of intracellular ATP-dependent protein degradation, and also the possible significance of ubiquitin-histone conjugates in chromatin. For detailed discussions of the various characteristics and physiological roles of intracellular protein breakdown, the reader is referred to earlier reviews [1-7] and reports of recent symposia [8-10]. Information on the ubiquitin system prior to 1981 was described in an earlier review [11]. Hershko has briefly reviewed more recent information [12].
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002474:Cell-Free System; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004734:Energy Metabolism; D006657:Histones / Q000378:metabolism; D008025:Ligases / Q000235:genetics; D008247:Lysosomes / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D011506:Proteins / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins
D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D011506:Proteins; D014452:Ubiquitins; D000255:Adenosine Triphosphate; D044767:Ubiquitin-Protein Ligases; D008025:Ligases