首页 | 本学科首页   官方微博 | 高级检索  
     


The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegans
Authors:Linn Gazda  Wojciech Pokrzywa  Doris Hellerschmied  Thomas Löwe  Ignasi Forné  Felix Mueller-Planitz  Thorsten Hoppe  Tim Clausen
Affiliation:1. Research Institute of Molecular Pathology, Dr. Bohrgasse 7, 1030 Vienna, Austria;2. Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Zülpicher Str. 47a, 50674 Cologne, Germany;3. Protein Analysis Unit, Adolf-Butenandt Institute and Center for Integrated Protein Science (CIPSM), Ludwig Maximilian University, Butenandtstr. 5-13, 81377 Munich, Germany;4. Molecular Biology Unit, Adolf-Butenandt Institute and Center for Integrated Protein Science (CIPSM), Ludwig Maximilian University, Butenandtstr. 5-13, 81377 Munich, Germany
Abstract:
><ol class=
  • Download : Download high-res image (299KB)
  • Download : Download full-size image
  • Highlights? UNC-45 self-assembles a docking platform for multiple chaperone and client proteins ? Hsp70/90 and myosin bind to specific sites on the TPR and UCS domains of UNC-45 ? The UNC-45 multimer offers the proper spacing to couple myosin folding and assembly ? In vivo, UNC-45 chains support the formation of fully functional sarcomeric repeats
    Keywords:
    本文献已被 ScienceDirect 等数据库收录!
    设为首页 | 免责声明 | 关于勤云 | 加入收藏

    Copyright©北京勤云科技发展有限公司  京ICP备09084417号