Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin

The Journal of Biological Chemistry
Sabine PokuttaWilliam I Weis

Abstract

alpha-Catenin is an integral component of adherens junctions, where it links cadherins to the actin cytoskeleton. alpha-Catenin is also required for the colocalization of the nectin/afadin/ponsin adhesion system to adherens junctions, and it specifically associates with the nectin-binding protein afadin. A proteolytic fragment of alpha-catenin, residues 385-651, contains the afadin-binding site. The three-dimensional structure of this fragment comprises two side-by-side four-helix bundles, both of which are required for afadin binding. The alpha-catenin fragment 385-651 binds afadin more strongly than the full-length protein, suggesting that the full-length protein harbors a cryptic binding site for afadin. Comparison of the alpha-catenin 385-651 structure with the recently solved structure of the alpha-catenin M-fragment (Yang, J., Dokurno, P., Tonks, N. K., and Barford, D. (2001) EMBO J. 20, 3645-3656) reveals a surprising flexibility in the orientation of the two four-helix bundles. alpha-Catenin and the actin-binding protein vinculin share sequence and most likely structural similarity within their actin-binding domains. Despite this homology, actin binding requires additional sequences adjacent to this region.

References

Feb 1, 1992·The Journal of Cell Biology·M Ozawa, R Kemler
Oct 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·K HerrenknechtR Kemler
Mar 1, 1991·Acta Crystallographica. Section A, Foundations of Crystallography·T A JonesM Kjeldgaard
Sep 12, 1995·Proceedings of the National Academy of Sciences of the United States of America·D L RimmJ S Morrow
May 23, 1995·Proceedings of the National Academy of Sciences of the United States of America·T S JouJ A Marrs
Oct 1, 1996·The Journal of Cell Biology·W M BrieherB M Gumbiner
Feb 1, 1997·Trends in Biochemical Sciences·S TsukitaS Tsukita
Oct 3, 1998·Acta Crystallographica. Section D, Biological Crystallography·A T BrüngerG L Warren
Feb 2, 1999·Journal of Molecular Biology·L Lo ConteJ Janin
Oct 6, 1999·Current Opinion in Cell Biology·M S Steinberg, P M McNutt
Nov 9, 2000·The Journal of Biological Chemistry·D PradhanJ S Morrow
Nov 1, 1994·Acta Crystallographica. Section D, Biological Crystallography·E A Merritt, M E Murphy
Jan 1, 1997·Methods in Enzymology·Zbyszek Otwinowski, Wladek Minor

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Citations

Mar 28, 2008·Histochemistry and Cell Biology·Klaus Ebnet
Apr 18, 2002·Current Opinion in Structural Biology·Sabine Pokutta, William I Weis
Jun 15, 2004·Nature·Constantina BakolitsaRobert C Liddington
Dec 3, 2003·Nature Cell Biology·Agnieszka KobielakElaine Fuchs
May 11, 2010·Nature Cell Biology·Shigenobu YonemuraMai Shibata
Feb 19, 2013·Nature Cell Biology·Ridhdhi DesaiUlrich Tepass
Sep 16, 2004·Nature Reviews. Molecular Cell Biology·Agnieszka Kobielak, Elaine Fuchs
Jul 24, 2008·Nature Reviews. Molecular Cell Biology·Yoshimi TakaiHisakazu Ogita
Jun 24, 2010·Nature Reviews. Molecular Cell Biology·Tony J C Harris, Ulrich Tepass
Aug 31, 2012·Nature Reviews. Molecular Cell Biology·Aparna Ratheesh, Alpha S Yap
Jan 8, 2013·Nature Structural & Molecular Biology·Erumbi S Rangarajan, Tina Izard
Aug 7, 2010·Proceedings of the National Academy of Sciences of the United States of America·Adam V KwiatkowskiJeff Hardin
May 16, 2012·Proceedings of the National Academy of Sciences of the United States of America·Hee-Jung ChoiWilliam I Weis
Apr 12, 2012·The Journal of Biological Chemistry·Erumbi S Rangarajan, Tina Izard
Dec 26, 2012·The Journal of Biological Chemistry·William A ThomasSylvie Dufour
Sep 29, 2006·The Journal of Biological Chemistry·William I Weis, W James Nelson
May 18, 2012·Molecular Biology of the Cell·Nariaki IwasawaIzumi Oinuma
Apr 2, 2004·Biology of Reproduction·Nikki P Y Lee, C Yan Cheng
Aug 26, 2006·Applied Immunohistochemistry & Molecular Morphology : AIMM·Deepak ShuklaTibor Valyi-Nagy
Jan 13, 2010·Cold Spring Harbor Perspectives in Biology·Lawrence Shapiro, William I Weis
Jan 13, 2010·Cold Spring Harbor Perspectives in Biology·Nikolaos GiagtzoglouHugo J Bellen
May 17, 2008·Pharmacological Reviews·Dolores D MrukC Yan Cheng
May 18, 2007·Annual Review of Biochemistry·Soichiro Yamada, W James Nelson
Jun 2, 2007·Annual Review of Cell and Developmental Biology·Sabine Pokutta, William I Weis
Jul 3, 2008·Annual Review of Cell and Developmental Biology·Yoshimi TakaiYoshiyuki Rikitake
Jun 14, 2008·The Journal of Neuroscience : the Official Journal of the Society for Neuroscience·Zhong XiePeter Penzes
Mar 11, 2009·Frontiers in Bioscience (Landmark Edition)·Allison M Lynch, Jeff Hardin
Jan 1, 2010·Yi chuan = Hereditas·Chao-Bo LiLei Lei
Apr 8, 2014·Proceedings of the National Academy of Sciences of the United States of America·Rebecca L DaughertyCara J Gottardi
Aug 1, 2014·Nature Communications·Mingxi YaoJie Yan
Feb 13, 2014·Cell and Tissue Research·Joppe Oldenburg, Johan de Rooij
Apr 9, 2013·Cellular and Molecular Life Sciences : CMLS·Floor Twiss, Johan de Rooij
Jan 13, 2016·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Claudia G Vasquez, Adam C Martin
Feb 7, 2016·Seminars in Cell & Developmental Biology·Kun Huang, Wing-Yee Lui

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