AI Article Synopsis
- Nucleoporin 153 (Nup153) is an important and flexible protein in nuclear pores, playing a key role in managing the interactions between transport receptors and their cargo.
- Nup153 contains four zinc finger motifs, with the second one (Nup153ZnF2) having the strongest binding affinity to the protein Ran, and this interaction is unaffected by phosphorylation.
- The crystal structure of the Nup153-ZnF2 and Ran complex shows a unique interface that prevents the formation of a Ran-importin-beta complex, suggesting Nup153 helps regulate Ran activity at the nuclear pore and aids in terminating import processes efficiently.
Article Abstract
Nucleoporin (Nup) 153 is a highly mobile, multifunctional, and essential nuclear pore protein. It contains four zinc finger motifs that are thought to be crucial for the regulation of transport-receptor/cargo interactions via their binding to the small guanine nucleotide binding protein, Ran. We found this interaction to be independent of the phoshorylation state of the nucleotide. Ran binds with the highest affinity to the second zinc finger motif of Nup153 (Nup153ZnF2). Here we present the crystal structure of this complex, revealing a new type of Ran-Ran interaction partner interface together with the solution structure of Nup153ZnF2. According to our complex structure, Nup153ZnF2 binding to Ran excludes the formation of a Ran-importin-beta complex. This finding suggests a local Nup153-mediated Ran reservoir at the nucleoplasmic distal ring of the nuclear pore, where nucleotide exchange may take place in a ternary Nup153-Ran-RCC1 complex, so that import complexes are efficiently terminated.
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| http://dx.doi.org/10.1016/j.str.2008.03.014 | DOI Listing |
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