REGgamma: a shortcut to destruction.
Destruction of intact cellular proteins is largely orchestrated by ATP-dependent ubiquitination and subsequent degradation by the 26S proteasome. The REG-20S proteasome, however, only degrades short peptides. In this issue of Cell, challenge this notion by revealing that the proteasomal activator REGgamma directs degradation of the steroid receptor coactivator SRC-3 by the 20S proteasome in an ATP- and ubiquitin-independent manner.
Zhou
Pengbo
P
Department of Pathology and Laboratory Medicine, Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA. pez2001@med.cornell.edu
D000123:Acetyltransferases / Q000378:metabolism*; D001324:Autoantigens / Q000502:physiology*; D051548:Histone Acetyltransferases; D056921:Nuclear Receptor Coactivator 3; D015513:Oncogene Proteins / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism* / Q000502:physiology; D015534:Trans-Activators / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism
D001324:Autoantigens; C099558:Ki antigen; D015513:Oncogene Proteins; D015534:Trans-Activators; D025801:Ubiquitin; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D056921:Nuclear Receptor Coactivator 3; D046988:Proteasome Endopeptidase Complex