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

Ganesh Karuna | Zendy; van Maldegem Febe | Zendy; Telerman Stephanie B. | Zendy; Simpson Paul | Zendy; Johnson Christopher M. | Zendy; Williams Roger L. | Zendy; Neuberger Michael S. | Zendy; Rada Cristina | Zendy

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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.

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