Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin α

Karuna Ganesh, Febe Van Maldegem, Stephanie B. Telerman, Paul Simpson, Christopher M. Johnson, Roger L. Williams, Michael S. Neuberger, Cristina Rada

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5 Citations (Scopus)


CTNNBL1 is a spliceosome-associated protein that binds nuclear localization signals (NLSs) in splice factors CDC5L and Prp31 as well as the antibody diversifying enzyme AID. Here, crystal structures of human CTNNBL1 reveal a distinct structure from its closest homologue karyopherin-α. CTNNBL1 comprises a HEAT-like domain (including a nuclear export signal), a central armadillo domain, and a coiled-coil C-terminal domain. Structure-guided mutations of the region homologous to the karyopherin-α NLS-binding site fail to disrupt CTNNBL1-NLS interactions. Our results identify CTNNBL1 as a unique selective NLS-binding protein with striking differences from karyopherin-αs.

Original languageEnglish
Pages (from-to)21-27
Number of pages7
JournalFEBS letters
Issue number1
Publication statusPublished - 3 Jan 2014
Externally publishedYes


  • Armadillo domain
  • Nuclear import
  • Splicing

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