噬骏纳米抗体文献.pdf

A Role for the Nucleoporin Nup170p in Chromatin Structure and Gene Silencing David W. Van de Vosse,1,6 Yakun Wan,2,3,6 Diego L. Lapetina,1 Wei-Ming Chen,2,4 Jung-Hsien Chiang,4 John D. Aitchison,2,5,* and Richard W. Wozniak1,* 1Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada 2 Institute for Systems Biology, Seattle, WA 98109, USA 3The Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Institute of Life Sciences, Southeast University, Nanjing 210096, China 4Department of Computer Science and Information Engineering, National Cheng Kung University, Tainan 701, Taiwan 5Seattle Biomedical Research Institute, Seattle, WA 98109, USA 6These authors contributed equally to this work *Correspondence: john.aitchison@ (J.D.A.), rick.wozniak@ualberta.ca (R.W.W.) /10.1016/j.cell.2013.01.049 SUMMARY of only 30 proteins, termed nucleoporins or Nups, which are present in multiple copies (Rout et al., 2000). The NPC is com- Embedded in the nuclear envelope, nuclear pore posed of membrane proteins, a symmetrical core scaffold con- complexes (NPCs) not only regulate nuclear trans- taining the Nup84p and Nup170p-Nup157p complexes, and port but also interface with transcriptionally active FG-Nups that populate the central channel and form cyto- euchromatin, largely silenced heterochromatin, as plasmic fibrils and a nuclear basket structure. The FG-Nups well as the boundaries between these regions. It is interact with transport factors and directly facilitate nucleocyto- unclear what functional role NPCs play in establish- plasmic transport.