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Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo‐relative, karyopherin α
Author(s) -
Ganesh Karuna,
van Maldegem Febe,
Telerman Stephanie B.,
Simpson Paul,
Johnson Christopher M.,
Williams Roger L.,
Neuberger Michael S.,
Rada Cristina
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.11.013
Subject(s) - karyopherin , armadillo , nuclear localization sequence , biology , spliceosome , nuclear transport , nls , plakoglobin , genetics , microbiology and biotechnology , rna splicing , cell nucleus , signal transduction , gene , wnt signaling pathway , rna , catenin
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.