@article{2d669d79fd22412986d65b6ad19afe7d,
title = "Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin α",
abstract = "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.",
keywords = "Armadillo domain, Nuclear import, Splicing",
author = "Karuna Ganesh and {Van Maldegem}, Febe and Telerman, {Stephanie B.} and Paul Simpson and Johnson, {Christopher M.} and Williams, {Roger L.} and Neuberger, {Michael S.} and Cristina Rada",
note = "Funding Information: Thanks to Alan Warren and Anita Chandra for advice and discussions and to the staff scientist at DSL beamlines I02 and I04-1 for their help. We are grateful for the support from the Leukaemia & Lymphoma Research to F.v.M. and Lucy Cavendish College, Cambridge to S.B.T. This work was supported by the Medical Research Council [MRC reference number MC_U105178806 ]. ",
year = "2014",
month = jan,
day = "3",
doi = "10.1016/j.febslet.2013.11.013",
language = "English",
volume = "588",
pages = "21--27",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "1",
}