Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function

• Verfasst von: Flemming, Dirk [VerfasserIn]
• Verfasst von: Stelter, Philipp [VerfasserIn]
• Verfasst von: Hurt, Ed [VerfasserIn]
• Titel: Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function
• Verf.angabe: Dirk Flemming, Philipp Stelter, and Ed Hurt
• E-Jahr: 2014
• Jahr: 20 May 2014
• Umfang: 17 S.
• Fussnoten: Gesehen am 30.09.2020
• Titel Quelle: Enthalten in: Nuclear pore complexes and nucleocytoplasmic transport
• Ausgabe Quelle: First edition
• Ort Quelle: San Diego, CA : Academic Press, 2014
• Jahr Quelle: 2014
• Band/Heft Quelle: (2014), Seite 99-115
• ISBN Quelle: 978-0-12-417178-7
• ISBN Quelle: 0-12-417178-8
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: DID
• Sach-SW: Dynein2
• Sach-SW: Electron microscopy
• Sach-SW: FG repeats
• Sach-SW: Label
• Sach-SW: Negative stain
• Sach-SW: NPC
• Sach-SW: Transport channel
• K10plus-PPN: 1734006781

Abstract

The discovery of dynein light chain 2 (Dyn2) as a member of the nucleoporins in yeast led to a series of applications to study NPC structure and function. Its intriguing ability to act as a hub for the parallel dimerization of two short amino acid sequence motifs (DID) prompted us to utilize it as a tool for probing nucleocytoplasmic transport in vivo. Further, the distinct structure of the Dyn2-DID rod, which is easily visible in the electron microscope, allowed us to develop a precise structural label on proteins or protein complexes. This label was used to identify the position of subunits in NPC subcomplexes or to derive at pseudo-atomic models of single large Nups. The versatility for various applications of the DID-Dyn2 system makes it an attractive molecular tool beyond the nuclear pore and transport field.