TY - JOUR
T1 - The Nup153-Nup50 protein interface and its role in nuclear import
AU - Makise, Masaki
AU - Mackay, Douglas R.
AU - Elgort, Suzanne
AU - Shankaran, Sunita S.
AU - Adam, Stephen A.
AU - Ullman, Katharine S.
PY - 2012/11/9
Y1 - 2012/11/9
N2 - Interactions between Nup50 and soluble transport factors underlie the efficiency of certain nucleocytoplasmic transport pathways. The platform on which these interactions take place is important to building a complete understanding of nucleocytoplasmic trafficking. Nup153 is the nucleoporin that provides this scaffold for Nup50. Here, we have delineated requirements for the interaction between Nup153 and Nup50, revealing a dual interface. An interaction between Nup50 and a region in the unique N-terminal region of Nup153 is critical for the nuclear pore localization of Nup50. A second site of interaction is at the distal tail of Nup153 and is dependent on importin α. Both of these interactions involve the N-terminal domain of Nup50. The configuration of the Nup153-Nup50 partnership suggests that the Nup153 scaffold provides not just a means of pore targeting for Nup50 but also serves to provide a local environment that facilitates bringing Nup50 and importin α together, as well as other soluble factors involved in transport. Consistent with this, disruption of the Nup153-Nup50 interface decreases efficiency of nuclear import.
AB - Interactions between Nup50 and soluble transport factors underlie the efficiency of certain nucleocytoplasmic transport pathways. The platform on which these interactions take place is important to building a complete understanding of nucleocytoplasmic trafficking. Nup153 is the nucleoporin that provides this scaffold for Nup50. Here, we have delineated requirements for the interaction between Nup153 and Nup50, revealing a dual interface. An interaction between Nup50 and a region in the unique N-terminal region of Nup153 is critical for the nuclear pore localization of Nup50. A second site of interaction is at the distal tail of Nup153 and is dependent on importin α. Both of these interactions involve the N-terminal domain of Nup50. The configuration of the Nup153-Nup50 partnership suggests that the Nup153 scaffold provides not just a means of pore targeting for Nup50 but also serves to provide a local environment that facilitates bringing Nup50 and importin α together, as well as other soluble factors involved in transport. Consistent with this, disruption of the Nup153-Nup50 interface decreases efficiency of nuclear import.
UR - http://www.scopus.com/inward/record.url?scp=84869046670&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84869046670&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.378893
DO - 10.1074/jbc.M112.378893
M3 - Article
C2 - 23007389
AN - SCOPUS:84869046670
SN - 0021-9258
VL - 287
SP - 38515
EP - 38522
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 46
ER -