S.Bilokapic
and
T.U.Schwartz
(2012).
Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.
Proc Natl Acad Sci U S A,
109,
15241-15246.
PubMed id: 22955883
Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.
S.Bilokapic,
T.U.Schwartz.
ABSTRACT
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs),
enormous assemblies composed of multiple copies of ∼30 different proteins
called nucleoporins. To unravel the basic scaffold underlying the NPC, we have
characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS.
Both proteins integrate directly via Nup120/160 into the universally conserved
heptameric Y-complex, the critical unit for the assembly and functionality of
the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in
complex with Nup120, a 174-kDa subassembly that forms one of the two short arms
of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein,
potentially stabilizing the relative orientation of its two domains. By means of
reconstitution assays, we pinpoint residues crucial for this interaction. In
vivo and in vitro results show that ELY5 binds near an interface of the
Nup120-Nup37 complex. Complementary biochemical and cell biological data refine
and consolidate the interactions of Nup120 within the current Y-model. Finally,
we propose an orientation of the Y-complex relative to the pore membrane,
consistent with the lattice model.
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