Ubiquitin junction, whats your function 英文参考文献.docVIP

/2001/2/10/reports/4025.1 Meeting report Ubiquitin junction, what’s your function? Traci A Lee and Mike Tyers Address: Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada. Correspondence: Mike Tyers. E-mail: tyers@mshri.on.ca Published: 26 September 2001 GenomeBiology 2001, 2(10):reports4025.1–4025.3 The electronic version of this article is the complete one and can be found online at /2001/2/10/reports/4025 ? BioMed Central Ltd (Print ISSN 1465-6906; Online ISSN 1465-6914) which the variable F-box protein component recruits different substrates to the core complex. Avram Hershko (Technion- Israel Institute of Technology, Haifa, Israel) kicked off the meeting by reporting the identification of Cks1, previously known as a subunit of cyclin dependent kinases, as a protein required for p27 ubiquitination; it probably acts by bridging the F-box protein Skp2 to phosphorylated p27. Michele Pagano (New York University Medical Center, USA) con- tinued coverage of p27 by showing that p27 polyubiquitina- tion is dependent both on cell adhesion, as a result of the adhesion-dependent expression of Skp2, and on phosphory- lation of the tumor suppressor protein Rb. A Degradation FASEB summer conference, Saxtons River, USA, 23-28 June 2001. report on the Ubiquitin and Intracellular Protein The modification of proteins by polyubiquitin is now well known as an elaborate signal that targets substrates for rapid degradation by the 26S proteasome, a multiprotein compart- mentalized protease particle that contains clusters of pro- teases within its barrel-shaped cavity. It has become apparent, however, that ubiquitin signals a host of other processes, as illustrated during the recent FASEB summer conference ‘Ubiquitin and Intracellular Protein Degrada- tion’. In addition to covering new findings about conven- tional ubiqu