ArticleBMC molecular biology2009
Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif.
Article in BMC molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- The Cby3/ciBAR1 complex positions the annulus along the sperm flagellum during spermiogenesis.The Journal of cell biology · 2024Article
- Structural validation and assessment of AlphaFold2 predictions for centrosomal and centriolar proteins and their complexes.Communications biology · 2022Article
- BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis.Molecular and cellular biology · 2016Article
- Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition.Protein science : a publication of the Protein Society · 2016Article
- Structural Analysis of the 14-3-3ζ/Chibby Interaction Involved in Wnt/β-Catenin Signaling.PloS one · 2015Article
- Chibby functions in Xenopus ciliary assembly, embryonic development, and the regulation of gene expression.Developmental biology · 2014Article
- Chibby promotes ciliary vesicle formation and basal body docking during airway cell differentiation.The Journal of cell biology · 2014Article
- No important role for genetic variation in the Chibby gene in monogenic and complex obesity.Molecular biology reports · 2013Article
- Article
- Chibby suppresses growth of human SW480 colon adenocarcinoma cells through inhibition of β-catenin signaling.Journal of molecular signaling · 2012Article
- Carbon storage regulator A (CsrA(Bb)) is a repressor of Borrelia burgdorferi flagellin protein FlaB.Molecular microbiology · 2011Article
- Generation and characterization of monoclonal antibodies against human Chibby protein.Hybridoma (2005) · 2011Article
- Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway.Biochemistry · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe Wnt/beta-catenin signaling pathway plays crucial roles in embryonic development and in maintenance of organs and tissues in adults. Chibby (Cby) is an evolutionarily conserved molecule that physically interacts with the key downstream coactivator beta-catenin and represses its transcriptional activation potential. Although Cby harbors a predicted coiled-coil motif in the C-terminal region, its molecular nature and functional importance remain largely unexplored.
resultsHere we report that Cby forms a stable complex with itself. Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. The Cby oligomer predominantly exists as a homodimer. Furthermore, we found that dimerization-deficient Cby mutants still retain the ability to bind to beta-catenin and to repress beta-catenin-dependent gene activation. More importantly, Cby homodimerization is required for its efficient interaction with the nuclear import receptor importin-alpha and subsequent nuclear translocation.
conclusionOur comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization. Although monomeric Cby is sufficient to bind to beta-catenin and block beta-catenin-mediated transcriptional activation, homodimer formation of Cby is indispensable for its efficient nuclear import.
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