Presented By: LSA Biophysics
Biophysics Virtual Seminar Series
Ph.D. Candidate Zhenyu Tan & Posdoctoral Researcher Thomas Paul
Please see below for the link to join the Zoom livestream
The Biophysics Virtual Seminar Series Presents:
Zhenyu Tan - Biophysics Ph.D. Candidate (Cianfrocco Group)
The mitochondrial cargo adaptor TRAK1 has overlapping binding sites for kinesin-1 and dynein
Abstract: Positioning of axonal mitochondria into target locations is critical for the physiology of neurons as they supply energy and calcium buffering capacity. The outer mitochondrial membrane protein Miro cooperates with TRAK1 and TRAK2 to scaffold kinesin and dynein, driving anterograde and retrograde mitochondrial transport. To understand how TRAK1 regulates both kinesin and dynein, we utilized biochemical reconstitution to define the minimal region of TRAK1 sufficient for promoting motor activation. We characterized that TRAK1 has overlapping binding sites for kinesin-1 and dynein that is capable of activating both motors in vitro.
Thomas Paul - Postdoctoral Researcher (Brooks Group)
pH Dependent Dissociation of Folate from Folic Acid Receptors
Abstract: The pH dependent binding and release of folate from folic acid receptors (FRs) is not well understood. Therefore, we have studied pKa shifts for two isoforms of FRs (FOLR1 and FOLR2) in their apo and holo forms using explicit solvent constant pH molecular dynamics (CPHMD^MSλD). Our key findings highlight amino acid residues that have upward pKa shifts that contribute significantly to destabilizing the FRs:folate complex at pH values consistent with an endosomal environment which allows us to propose a potential mechanism of release.
Zoom passcode: 677763
The Biophysics Virtual Seminar Series Presents:
Zhenyu Tan - Biophysics Ph.D. Candidate (Cianfrocco Group)
The mitochondrial cargo adaptor TRAK1 has overlapping binding sites for kinesin-1 and dynein
Abstract: Positioning of axonal mitochondria into target locations is critical for the physiology of neurons as they supply energy and calcium buffering capacity. The outer mitochondrial membrane protein Miro cooperates with TRAK1 and TRAK2 to scaffold kinesin and dynein, driving anterograde and retrograde mitochondrial transport. To understand how TRAK1 regulates both kinesin and dynein, we utilized biochemical reconstitution to define the minimal region of TRAK1 sufficient for promoting motor activation. We characterized that TRAK1 has overlapping binding sites for kinesin-1 and dynein that is capable of activating both motors in vitro.
Thomas Paul - Postdoctoral Researcher (Brooks Group)
pH Dependent Dissociation of Folate from Folic Acid Receptors
Abstract: The pH dependent binding and release of folate from folic acid receptors (FRs) is not well understood. Therefore, we have studied pKa shifts for two isoforms of FRs (FOLR1 and FOLR2) in their apo and holo forms using explicit solvent constant pH molecular dynamics (CPHMD^MSλD). Our key findings highlight amino acid residues that have upward pKa shifts that contribute significantly to destabilizing the FRs:folate complex at pH values consistent with an endosomal environment which allows us to propose a potential mechanism of release.
Zoom passcode: 677763
Related Links
Livestream Information
ZoomSeptember 18, 2020 (Friday) 12:00pm
Meeting ID: 97068405681
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