TY - JOUR TI - Ubiquitin-mediated proteolysis in Xenopus extract AU - McDowell, GaryS. AU - Philpott, Anna T2 - The International Journal of Developmental Biology AB - The small protein modifier, ubiquitin, can be covalently attached to proteins in the process of ubiquitylation, resulting in a variety of functional outcomes. In particular, the most commonly-associated and well-studied fate for proteins modified with ubiquitin is their ultimate destruction: degradation by the 26S proteasome via the ubiquitin-proteasome system, or digestion in lysosomes by proteolytic enzymes. From the earliest days of ubiquitylation research, a reliable and versatile “cell-in-a-test-tube” system has been employed in the form of cytoplasmic extracts from the eggs and embryos of the frog Xenopus laevis. Biochemical studies of ubiquitin and protein degradation using this system have led to significant advances particularly in the study of ubiquitin-mediated proteolysis, while the versatility of Xenopus as a developmental model has allowed investigation of the in vivo consequences of ubiquitylation. Here we describe the use and history of Xenopus extract in the study of ubiquitin-mediated protein degradation, and highlight the versatility of this system that has been exploited to uncover mechanisms and consequences of ubiquitylation and proteolysis. PY - 2016 DO - 10.1387/ijdb.160186gm VL - 60 IS - 7-8-9 SP - 263 EP - 270 J2 - Int. J. Dev. Biol. LA - en SN - 0214-6282 SN - 1696-3547 UR - https://ijdb.ehu.eus/article/160186gm Y2 - 2024/04/30/09:11:26 ER -