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<!DOCTYPE html>
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<title>Intrinsically disordered region of talin’s FERM domain functions as an initial PIP2 recognition site</title>
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<h1><p>Intrinsically disordered region of talin’s FERM domain functions as an initial PIP2 recognition site</p></h1>
<div class="author">
<span style="white-space: pre">Jannik Buhr</span><sup>1,2</sup> (jannik.buhr@h-its.org, <a href="https://jmbuhr.de">jmbuhr.de</a>), <span style="white-space: pre">Florian Franz</span><sup>1,2</sup>, <span style="white-space: pre">Frauke Gräter</span><sup>1,2</sup>
</div>
<div class="affiliation">
<ol>
<li>Heidelberg Institute for Theoretical Studies (HITS)</li>
<li>Heidelberg University</li>
</ol>
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<p><img src="www/hits-logo-large-negative.png" id="logo-hits" class="logo img-fluid"> <img src="www/logo-hbigs-inv.png" id="logo-hbigs" class="logo img-fluid"> <img src="www/logo-uni-hd-bw-inv.png" id="logo-uni-hd" class="logo img-fluid"></p>
<h1 id="unstructured-loop-of-talins-ferm-domain-can-serve-as-a-flexible-membrane-anchor">Unstructured loop of Talin’s FERM domain can serve as a flexible membrane anchor</h1>
<p>This allows for interaction with PIP<sub>2</sub> even in Talin’s autoinhibited form and paves the way to establish known binding surfaces.</p>
<p><img src="assets/blender/render/frame0002.png" class="img-fluid"></p>
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<p>Follow the QR code or visit <a href="https://github.com/hits-mbm-dev/paper-talin-loop" class="uri">https://github.com/hits-mbm-dev/paper-talin-loop</a> for the repository of the paper draft. Or even better yet, talk to me in front of the poster!</p>
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<h2 id="abstract" class="anchored">Abstract</h2>
<div id="fig-structure" class="quarto-figure quarto-figure-center anchored">
<figure>
<p><img src="assets/blender/render-align/frame0000.png" class="wrapping img-fluid"></p>
<p></p><figcaption>Figure 1: The autoinhibited (Cryo-EM) structure of Talin1 found by <span class="citation" data-cites="deddenArchitectureTalin1Reveals2019a">Dedden et al. (<a href="#ref-deddenArchitectureTalin1Reveals2019a" role="doc-biblioref">2019</a>)</span> aligned with the structure of the FERM domain by <span class="citation" data-cites="elliottStructureTalinHead2010">Elliott et al. (<a href="#ref-elliottStructureTalinHead2010" role="doc-biblioref">2010</a>)</span> and the modelled flexible loop in F1 (darker cyan)</figcaption><p></p>
</figure>
</div>
<p>Focal adhesions mediate the interaction of the cytoskeleton with the extracellular matrix (ECM). Talin is a central regulator and adaptorprotein of the multiprotein focal adhesion complexes and is responsible for integrin activation and force-sensing. We evaluated direct interactions of talin with the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP<sub>2</sub>) by means of molecular dynamics simulations. A newly published autoinhibitory structure of talin, where common PIP<sub>2</sub> interaction sites are covered up, sparked our curiosity for a hitherto less examined loop as a potential site of first contact. We show that this unstructured loop in the F1 subdomain of the talin1 FERM domain is able to interact with PIP<sub>2</sub> and can facilitate further interactions by serving as a flexible membrane anchor.</p>
<div id="fig-rot-sample" class="quarto-figure quarto-figure-center anchored">
<figure>
<p><img src="assets/results/plots/f0f1-ri-angle-npip-1.png" class="center img-fluid" style="width:80.0%"></p>
<p></p><figcaption>Figure 2: A rotational sampling of the F0F1 domain reaveals the strong propensity of the F1 loop to interact with the membrane. Even in the most unfavorable position, the loop still has a high probability to find the membrane and interact with PIP<sub>2</sub> due to the large search space it can cover.</figcaption><p></p>
</figure>
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<div id="fig-f0f1-residues" class="quarto-figure quarto-figure-center anchored">
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<p><img src="./assets/vmd/f0f1/residues.png" class="center img-fluid" style="width:80.0%"></p>
<p></p><figcaption>Figure 3: The residues of F0F1 interacting with PIP<sub>2</sub> are highlighted in blue, with their CA-atoms labelled</figcaption><p></p>
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<p><img src="assets/results/plots/f0f1-retention-1.png" class="img-fluid"></p>
<p></p><figcaption> </figcaption><p></p>
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<p><img src="assets/results/plots/f0f1-vert-pull-1.png" class="img-fluid"></p>
<p></p><figcaption> </figcaption><p></p>
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<p></p><figcaption>Figure 4: <strong>Left</strong>: Once a certain number of residues are interacting, it becomes highly unlikely for F0F1 to dissociate from the membrane. <strong>Right</strong>: Pulling bound F0F1 from the membrane does need some force, but the most important aspect for remaining bound is its flexibility. This allows it to remain in contact with PIP<sub>2</sub> even at large distances.</figcaption><p></p>
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<p><img src="./assets/vmd/ferm/ferm-residues-transparent-arrows.png" class="img-fluid"></p>
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<figure>
<p><img src="assets/results/plots/ferm-ri-npip-1.png" class="img-fluid"></p>
<p></p><figcaption>Figure 5: Once contact has been established via the loop, simulations with the full lenght FERM domain show that known PIP<sub>2</sub> interaction sites are recovered. The location of binding surfaces found by <span class="citation" data-cites="chinthalapudiInteractionTalinCell2018a">Chinthalapudi, Rangarajan, and Izard (<a href="#ref-chinthalapudiInteractionTalinCell2018a" role="doc-biblioref">2018</a>)</span> are highlighted with red lines on the schematic: K272 of F2 and K316, K324, E342, and K343 of F3.</figcaption><p></p>
</figure>
</div>
<h2 id="acknowledgments" class="anchored">Acknowledgments</h2>
<p>This project has received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement No. 101002812)</p>
<p>This poster was made <code>betterposter</code> <span class="citation" data-cites="rbetterposter">(<a href="#ref-rbetterposter" role="doc-biblioref">Aden-Buie 2022</a>)</span> R package and quarto <span class="citation" data-cites="quarto">(<a href="#ref-quarto" role="doc-biblioref">Allaire et al. 2022</a>)</span>.</p>
<h2 id="references" class="anchored">References</h2>
<div id="refs" class="references csl-bib-body hanging-indent" role="doc-bibliography">
<div id="ref-rbetterposter" class="csl-entry" role="doc-biblioentry">
Aden-Buie, Garrick. 2022. <em>Betterposter: <span>A</span> Better Scientific Poster</em>. Manual.
</div>
<div id="ref-quarto" class="csl-entry" role="doc-biblioentry">
Allaire, J. J., Charles Teague, Carlos Scheidegger, Yihui Xie, and Christophe Dervieux. 2022. <span>“Quarto.”</span> <a href="https://doi.org/10.5281/zenodo.5960048">https://doi.org/10.5281/zenodo.5960048</a>.
</div>
<div id="ref-chinthalapudiInteractionTalinCell2018a" class="csl-entry" role="doc-biblioentry">
Chinthalapudi, Krishna, Erumbi S. Rangarajan, and Tina Izard. 2018. <span>“The Interaction of Talin with the Cell Membrane Is Essential for Integrin Activation and Focal Adhesion Formation.”</span> <em>Proceedings of the National Academy of Sciences of the United States of America</em> 115 (41): 10339–44. <a href="https://doi.org/10.1073/pnas.1806275115">https://doi.org/10.1073/pnas.1806275115</a>.
</div>
<div id="ref-deddenArchitectureTalin1Reveals2019a" class="csl-entry" role="doc-biblioentry">
Dedden, Dirk, Stephanie Schumacher, Charlotte F. Kelley, Martin Zacharias, Christian Biertümpfel, Reinhard Fässler, and Naoko Mizuno. 2019. <span>“The <span>Architecture</span> of <span>Talin1 Reveals</span> an <span>Autoinhibition Mechanism</span>.”</span> <em>Cell</em> 179 (1): 120–131.e13. <a href="https://doi.org/10.1016/j.cell.2019.08.034">https://doi.org/10.1016/j.cell.2019.08.034</a>.
</div>
<div id="ref-elliottStructureTalinHead2010" class="csl-entry" role="doc-biblioentry">
Elliott, Paul R., Benjamin T. Goult, Petra M. Kopp, Neil Bate, J. Günter Grossmann, Gordon C. K. Roberts, David R. Critchley, and Igor L. Barsukov. 2010. <span>“The <span>Structure</span> of the <span>Talin Head Reveals</span> a <span>Novel Extended Conformation</span> of the <span>FERM Domain</span>.”</span> <em>Structure(London, England:1993)</em> 18 (10-13): 1289–99. <a href="https://doi.org/10.1016/j.str.2010.07.011">https://doi.org/10.1016/j.str.2010.07.011</a>.
</div>
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