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Distinct hydrophobic "patches" in the N- and C-tails of beta-catenin contribute to nuclear transport.

Abstract：

:β-catenin is a key mediator of Wnt signaling and its deregulated nuclear accumulation can drive cancer progression. While the central armadillo (Arm) repeats of β-catenin stimulate nuclear entry, the N- and C-terminal "tail" sequences are thought to regulate turnover and transactivation. We show here that the N- and C-tails are also potent transport sequences. The unstructured tails of β-catenin, when individually fused to a GFP-reporter, could enter and exit the nucleus rapidly in live cells. Proximity ligation assays and pull-down assays identified a weak interaction between the tail sequences and the FG-repeats of nucleoporins, consistent with a possible direct translocation of β-catenin through the nuclear pore complex. Extensive alanine mutagenesis of the tail sequences revealed that nuclear translocation of β-catenin was dependent on specific uniformly distributed patches of hydrophobic residues, whereas the mutagenesis of acidic amino acids had no effect. Moreover, the mutation of hydrophobic patches within the N-tail and C-tail of full length β-catenin reduced nuclear transport rate and diminished its ability to activate transcription. We propose that the tail sequences can contribute to β-catenin transport and suggest a possible similar role for hydrophobic unstructured regions in other proteins.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Sharma M,Jamieson C,Lui C,Henderson BR

doi

10.1016/j.yexcr.2016.09.009

subject

Has Abstract

pub_date

2016-11-01 00:00:00

pages

132-145

issue

2

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(16)30289-0

journal_volume

348

pub_type

杂志文章

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