ABSTRACT The F-actin–binding cytoskeletal protein α-catenin interacts with β-catenin–cadherin complexes and stabilizes cell-cell junctions. The β-catenin–α-catenin complex cannot bind

F-actin, whereas interactions of α-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly

full-length human α-catenin at 3.7-Å resolution. α-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This

results in a left handshake–like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric α-catenin has a higher affinity for

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institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS DISTINCT INTER-DOMAIN INTERACTIONS OF DIMERIC VERSUS MONOMERIC Α-CATENIN LINK 

CELL JUNCTIONS TO FILAMENTS Article Open access 16 March 2023 ACTIN-DEPENDENT Α-CATENIN OLIGOMERIZATION CONTRIBUTES TO ADHERENS JUNCTION ASSEMBLY Article Open access 20 February 2025

Α-CATENIN SWITCHES BETWEEN A SLIP AND AN ASYMMETRIC CATCH BOND WITH F-ACTIN TO COOPERATIVELY REGULATE CELL JUNCTION FLUIDITY Article Open access 03 March 2022 ACCESSION CODES PRIMARY

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  CAS  Google Scholar  Download references ACKNOWLEDGEMENTS We are indebted to our colleagues at Scripps Florida: J. Cleveland for discussions and critical review of the manuscript, Z. Wu

and P. Bois for sequencing and P. Bois for fruitful discussions. We thank C. Vonrhein and G. Bricogne (Global Phasing Ltd.) for analyses and helpful discussions. We are grateful to the staff

at the SER-CAT (BM22) and SSRL (11-1) for synchrotron support. T.I. is supported by grants from the US National Institute of General Medical Sciences from the US National Institutes of

Health (GM071596 and GM094483) and by start-up funds provided to Scripps Florida from the State of Florida. This is publication no. 21863 from The Scripps Research Institute. AUTHOR

INFORMATION AUTHORS AND AFFILIATIONS * Department of Cancer Biology, Scripps Research Institute, Jupiter, Florida, USA Erumbi S Rangarajan & Tina Izard Authors * Erumbi S Rangarajan View

author publications You can also search for this author inPubMed Google Scholar * Tina Izard View author publications You can also search for this author inPubMed Google Scholar

CONTRIBUTIONS Both authors contributed to the design and interpretation of all aspects of this work. E.S.R. performed all of the experiments. T.I. wrote the manuscript. CORRESPONDING AUTHOR

Correspondence to Tina Izard. ETHICS DECLARATIONS COMPETING INTERESTS The authors declare no competing financial interests. SUPPLEMENTARY INFORMATION SUPPLEMENTARY TEXT AND FIGURES

Supplementary Figures 1–4 and Supplementary Table 1 (PDF 39296 kb) RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Rangarajan, E., Izard, T. Dimer

asymmetry defines α-catenin interactions. _Nat Struct Mol Biol_ 20, 188–193 (2013). https://doi.org/10.1038/nsmb.2479 Download citation * Received: 02 August 2012 * Accepted: 27 November

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