Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function
Authors: Flemming D, Stelter P1, Hurt E
CellNetworks People: Hurt Ed
Journal: Methods Cell Biol. 2014;122:99-115. doi: 10.1016/B978-0-12-417160-2.00005-9

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.