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Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores

¹ Centre for Biochemistry and ² Department of Neurobiology, University of Heidelberg, D-69120 Heidelberg, Germany
³ The School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK

Correspondence to Ed Hurt: ed.hurt{at}bzh.uni-heidelberg.de

How individual nucleoporins (Nups) perform their role in nuclear pore structure and function is largely unknown. In this study, we examined the structure of purified Nup170 to obtain clues about its function. We show that Nup170 adopts a crescent moon shape with two structurally distinct and separable domains, a β-propeller N terminus and an -solenoid C terminus. To address the individual roles of each domain, we expressed these domains separately in yeast. Notably, overexpression of the Nup170 C domain was toxic in nup170 cells and caused accumulation of several Nups in cytoplasmic foci. Further experiments indicated that the C-terminal domain anchors Nup170 to nuclear pores, whereas the N-terminal domain functions to recruit or retain a subset of Nups, including Nup159, Nup188, and Pom34, at nuclear pores. We conclude that Nup170 performs its role as a structural adapter between cytoplasmically oriented Nups and the nuclear pore membrane.

Abbreviations used in this paper: FAS, fatty acid synthase; NE, nuclear envelope; NPC, nuclear pore complex; Nup, nucleoporin; TEV, tobacco etch virus; SDC, synthetic dextrose complete; SRC, synthetic raffinose complete.

© 2009 Flemming et al.
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This article has been cited by other articles:

• Whittle, J. R. R., Schwartz, T. U. (2009). Architectural Nucleoporins Nup157/170 and Nup133 Are Structurally Related and Descend from a Second Ancestral Element. J. Biol. Chem. 284: 28442-28452 [Abstract] [Full Text]  
• Rexach, M. (2009). Piecing together nuclear pore complex assembly during interphase. JCB 185: 377-379 [Abstract] [Full Text]  

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