Cadherins can dimerize via asymmetric interactions.

AFM force measurements X-dimer classical cadherins molecular dynamics strand-swap dimer trans interactions

Journal

FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157

Informations de publication

Date de publication:
07 2022
Historique:
revised: 28 04 2022
received: 11 02 2022
accepted: 02 05 2022
pubmed: 10 5 2022
medline: 14 7 2022
entrez: 9 5 2022
Statut: ppublish

Résumé

Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmetrically incorporates key elements of both strand-swap dimers and X-dimers. Our results clarify the biophysical rules for cadherin binding and demonstrate that cadherins interact in a more diverse range of conformations than previously understood.

Identifiants

pubmed: 35532156
doi: 10.1002/1873-3468.14373
pmc: PMC9829383
mid: NIHMS1859033
doi:

Substances chimiques

Cadherins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

1639-1646

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM121885
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM133880
Pays : United States

Informations de copyright

© 2022 Federation of European Biochemical Societies.

Références

Structure. 2011 Feb 9;19(2):244-56
pubmed: 21300292
Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18815-20
pubmed: 23112161
Cell Commun Adhes. 2013 Dec;20(6):201-12
pubmed: 24205985
Elife. 2018 Jul 12;7:
pubmed: 29999492
Structure. 2009 Aug 12;17(8):1075-81
pubmed: 19646884
Science. 1994 Sep 9;265(5178):1599-600
pubmed: 8079175
Science. 2002 May 17;296(5571):1308-13
pubmed: 11964443
Proc Natl Acad Sci U S A. 2013 Oct 8;110(41):16462-7
pubmed: 24067646
Proc Natl Acad Sci U S A. 2020 Dec 8;117(49):31157-31165
pubmed: 33229577
Methods Enzymol. 2013;529:227-40
pubmed: 24011049
Proc Natl Acad Sci U S A. 2021 Jul 27;118(30):
pubmed: 34301871
Curr Opin Biomed Eng. 2019 Dec;12:43-50
pubmed: 31742239
Nat Struct Mol Biol. 2010 Mar;17(3):348-57
pubmed: 20190754
Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):109-14
pubmed: 19114658
Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15755-60
pubmed: 18852468
J Chem Phys. 2018 Mar 28;148(12):123301
pubmed: 29604850
J Cell Biol. 2011 Mar 21;192(6):1073-83
pubmed: 21422232
Biophys J. 1997 Apr;72(4):1541-55
pubmed: 9083660
Nature. 2021 Aug;596(7873):583-589
pubmed: 34265844
Oncogene. 2018 Aug;37(35):4769-4780
pubmed: 29780167
Science. 1978 May 12;200(4342):618-27
pubmed: 347575
Trends Cell Biol. 2012 Jun;22(6):299-310
pubmed: 22555008
Proc Natl Acad Sci U S A. 2016 Sep 27;113(39):E5711-20
pubmed: 27621473
EMBO J. 1999 Apr 1;18(7):1738-47
pubmed: 10202138

Auteurs

Andrew Vae Priest (AV)

Department of Biomedical Engineering, University of California, Davis, CA, USA.

Ramesh Koirala (R)

Department of Biomedical Engineering, University of California, Davis, CA, USA.

Sanjeevi Sivasankar (S)

Department of Biomedical Engineering, University of California, Davis, CA, USA.

Articles similaires

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Fucosyltransferases Drug Repositioning Molecular Docking Simulation Molecular Dynamics Simulation Humans
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics

Structural basis for molecular assembly of fucoxanthin chlorophyll

Koji Kato, Yoshiki Nakajima, Jian Xing et al.
1.00
Diatoms Photosystem I Protein Complex Chlorophyll Binding Proteins Cryoelectron Microscopy Light-Harvesting Protein Complexes

Classifications MeSH