[HTML][HTML] Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin α
K Ganesh, F Van Maldegem, SB Telerman, P Simpson… - FEBS letters, 2014 - Elsevier
FEBS letters, 2014•Elsevier
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 …
(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 …
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.
Elsevier
