Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex.

Abstract:

:Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope. Here, we discovered an unexpected role for yeast dynein light chain (Dyn2) in the NPC. Dyn2 is a previously undescribed nucleoporin that functions as molecular glue to dimerize and stabilize the Nup82-Nsp1-Nup159 complex, a module of the cytoplasmic pore filaments. Biochemical analyses showed that Dyn2 binds to a linear motif (termed DID(Nup159)) inserted between the Phe-Gly repeat and coiled-coil domain of Nup159. Electron microscopy revealed that the reconstituted Dyn2-DID(Nup159) complex forms a rigid rod-like structure, in which five Dyn2 homodimers align like 'pearls on a string' between two extented DID(Nup159) strands. These findings imply that the rigid 20 nm long Dyn2-DID(Nup159) filament projects the Nup159 Phe-Gly repeats from the Nup82 module. Thus, it is possible that dynein light chain plays a role in organizing natively unfolded Phe-Gly repeats within the NPC scaffold to facilitate nucleocytoplasmic transport.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Stelter P,Kunze R,Flemming D,Höpfner D,Diepholz M,Philippsen P,Böttcher B,Hurt E

doi

10.1038/ncb1604

subject

Has Abstract

pub_date

2007-07-01 00:00:00

pages

788-96

issue

7

eissn

1465-7392

issn

1476-4679

pii

ncb1604

journal_volume

9

pub_type

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