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<p class="MsoNormal"><span style="font-size:15.0pt">There will be a <b><span style="color:red">virtual</span></b><span style="color:red">
</span>Modern Optics and Spectroscopy Seminar held <b>TODAY at 12pm. </b>A short Q&A segment will immediately follow the conclusion of the seminar.</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt"> </span><o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:15.0pt">Zoom link:<i><span style="color:red">
<a href="https://mit.zoom.us/j/99714325465?pwd=S2V6Q1p6UUkxTktPeEh1aU1XRUl0dz09">
<span style="color:red">https://mit.zoom.us/j/99714325465?pwd=S2V6Q1p6UUkxTktPeEh1aU1XRUl0dz09</span></a></span><br>
</i>Password: <span style="color:red">337483</span><o:p></o:p></span></b></p>
<p class="MsoNormal"><b><span style="font-size:15.0pt">__________________________</span></b><o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:18.0pt"><br>
Shwetha Srinivasan<br>
</span></b><b><span style="font-size:17.0pt">MIT – Schlau-Cohen Group</span></b><i><span style="font-size:14.0pt"><br>
<br>
</span></i><b><i><span style="font-size:16.0pt">“Resolving conformational coupling across the membrane bilayer<br>
of Epidermal Growth Factor Receptor with single-molecule spectroscopy”<o:p></o:p></span></i></b></p>
<p class="MsoNormal"><i><br>
Membrane receptors reside in complex environments along with their numerous extracellular binding partners or ligands to transduce information across the lipid bilayer. One such receptor protein is the epidermal growth factor receptor (EGFR) which plays a crucial
role in cell signaling and is implicated in cancer. While the structures of the extracellular and intracellular regions of EGFR have been well elucidated individually, conformational coupling connecting these two regions during signal transduction is challenging
to probe due to the mixture of hydrophobic and hydrophilic domains intrinsic to membrane proteins. We overcome these limitations by combining nanodiscs, which provide a near-native membrane environment to isolate full-length receptors, and single-molecule
spectroscopy, which resolves the heterogeneous nature of these protein motions, to identify previously unknown coupling between the extracellular and intracellular domains of the epidermal growth factor receptor (EGFR). Furthermore, we untangle (1) the role
of the complex membrane environment in the extracellular/intracellular conformational coupling of EGFR, uncovering the specific task of anionic lipids and cholesterol; and (2) the influence of the binding partners which determine EGFR’s downstream signaling
and cellular process, ascertaining ligand-specific EGFR conformations. These results could be universal to other membrane receptors which share the same structural homology and perform other significant functions.<o:p></o:p></i></p>
<p class="MsoNormal"><i><o:p> </o:p></i></p>
<p class="MsoNormal"><i><br>
_____________________</i><i><span style="font-size:11.0pt"><br>
</span></i> <o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:11.0pt">Christine Brooks</span></b><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Administrative Assistant</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Massachusetts Institute of Technology</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Department of Chemistry</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">77 Massachusetts Ave, 6-333</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Cambridge, MA 02139</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">p: 617.253.7239</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">e: <a href="mailto:cbrooks@mit.edu">cbrooks@mit.edu</a></span><o:p></o:p></p>
<p class="MsoNormal"> <o:p></o:p></p>
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