%0 Journal Article
%A Song, Jae-Geun
%A Kostan, Julius
%A Drepper, Friedel
%A Knapp, Bettina
%A de Almeida Ribeiro, Euripedes
%A Konarev, Petr V.
%A Grishkovskaya, Irina
%A Wiche, Gerhard
%A Gregor, Martin
%A Svergun, Dmitri I.
%A Warscheid, Bettina
%A Djinović-Carugo, Kristina
%T Structural Insights into Ca<sup>2+</sup>-Calmodulin Regulation of Plectin 1a-Integrin β4 Interaction in Hemidesmosomes
%J Structure
%V 23
%N 3
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M PUBDB-2016-00545
%P 558 - 570
%D 2015
%X The mechanical stability of epithelial cells, whichprotect organisms from harmful external factors, ismaintained by hemidesmosomes via the interactionbetween plectin 1a (P1a) and integrin a6b4. Bindingof calcium-calmodulin (Ca 2+ -CaM) to P1a togetherwith phosphorylation of integrin b4 disrupts thiscomplex, resulting in disassembly of hemidesmo-somes. We present structures of the P1a actin bind-ing domain either in complex with the N-ter lobe ofCa 2+ -CaM or with the first pair of integrin b4 fibro-nectin domains. Ca 2+ -CaM binds to the N-ter iso-form-specific tail of P1a in a unique manner, via itsN-ter lobe in an extended conformation. Structural,cell biology, and biochemical studies suggest thefollowing model: binding of Ca 2+ -CaM to an intrinsi-cally disordered N-ter segment of plectin convertsit to an a helix, which repositions calmodulin todisplace integrin b4 by steric repulsion. This modelcould serve as a blueprint for studies aimed at under-standing how Ca 2+ -CaM or EF-hand motifs regulateF-actin-based cytoskeleton.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000350886100014
%$ pmid:25703379
%R 10.1016/j.str.2015.01.011
%U https://bib-pubdb1.desy.de/record/293456