title: beta-Catenin shows an overlapping sequence requirement but distinct molecular interactions for its bidirectional passage through nuclear pores.
abstract: beta-Catenin is an example of a typical molecule that can be translocated bidirectionally through nuclear pore complexes (NPCs) on its own in a facilitated manner. In this work the nuclear import and export of beta-catenin were examined to compare the sequence requirement of this molecule and to determine whether molecular interactions required for its bidirectional NPC passage are distinct or not. Deletion analysis of beta-catenin revealed that armadillo repeats 10-12 and the C terminus comprise the minimum region necessary for nuclear migration activity. Further dissection of this fragment showed that the C terminus tail plays an essential role in nuclear migration. The region of beta-catenin required for export substantially overlapped the region required for import. Therefore, the NPC translocation of beta-catenin is apparently reversible, which is consistent with findings reported previously. However, different translocating molecules blocked nuclear import and export of beta-catenin differentially. The data herein indicate that beta-catenin shows an overlapping sequence requirement for its import and export but that bidirectional movement through the NPC proceeds through distinct molecular interactions.
authors.affiliation: Cellular Dynamics Laboratory, Discovery Research Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
authors.forename: Makiko
authors.initials: M
authors.lastname: Koike
authors.forename: Shingo
authors.initials: S
authors.lastname: Kose
authors.forename: Maiko
authors.initials: M
authors.lastname: Furuta
authors.forename: Naoko
authors.initials: N
authors.lastname: Taniguchi
authors.forename: Fumihiko
authors.initials: F
authors.lastname: Yokoya
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Yoneda
authors.forename: Naoko
authors.initials: N
authors.lastname: Imamoto
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D001667:Binding, Competitive; D001692:Biological Transport / Q000187:drug effects; D002459:Cell Fusion; D002467:Cell Nucleus / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017353:Gene Deletion; D005982:Glutathione Transferase / Q000235:genetics; D049452:Green Fluorescent Proteins; D006367:HeLa Cells; D006801:Humans; D008164:Luminescent Proteins / Q000235:genetics; D016296:Mutagenesis; D022022:Nuclear Pore / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D012091:Repetitive Sequences, Nucleic Acid; D013329:Structure-Activity Relationship; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051176:beta Catenin; D028961:beta Karyopherins / Q000494:pharmacology
chemical_list: C495270:CTNNB1 protein, human; D003598:Cytoskeletal Proteins; D008164:Luminescent Proteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D015534:Trans-Activators; D051176:beta Catenin; D028961:beta Karyopherins; D049452:Green Fluorescent Proteins; D000255:Adenosine Triphosphate; D005982:Glutathione Transferase