BEGIN:VCALENDAR VERSION:2.0 PRODID:-//jEvents 2.0 for Joomla//EN CALSCALE:GREGORIAN METHOD:PUBLISH BEGIN:VEVENT UID:4f8de526060915378ac8606753303ad8 CATEGORIES:Seminar CREATED:20171201T155122 SUMMARY:Dr. Neel Shah LOCATION:Life Sciences Auditorium DESCRIPTION:Dr. Neel ShahUC BerkeleyDecember 19, 2017\nLife Sciences Auditorium 11:00 A M\n"Tyrosine Kinase Specificity in T Cell Receptor Signaling"\nOne of the h allmarks of eukaryotic cell signaling is the expansion of enzyme families t o include hundreds of specialized members that carry out diverse biological processes. Protein kinases represent one such family, where a conserved pr otein fold and core biochemical function have been elaborated on through th e introduction of distinct substrate specificities and divergent modes of r egulation. Dissecting the molecular basis for specialization within this la rge enzyme family will guide our understanding of the architectures of cell signaling pathways and aid in the design of selective kinase-targeted drug s. These efforts may be augmented by the recent development of high-through put biochemical approaches that couple the analysis of protein function to next-generation DNA sequencing. I will discuss my efforts to dissect the ev olution and specialization of the protein tyrosine kinases involved in T ce ll receptor signaling using a high-throughput platform to interrogate kinas e substrate specificity. These experiments point to divergent molecular rec ognition features of two essential kinases, Lck and ZAP-70, that ensure fai thful signaling during the early stages of T cell activation. T cells play a central role in modern cancer immunotherapies, and these insights may be useful for the development and improvement of such therapies. Furthermore, the high-throughput biochemical techniques described in my talk will be val uable tools for the characterization of other signaling enzymes.\n~Coffee/t ea will be served prior to lecture.~\n X-ALT-DESC;FMTTYPE=text/html:
December 19, 2017
Life Sciences Auditorium 11:00 AM
"Tyrosi ne Kinase Specificity in T Cell Receptor Signaling"
One of the hallma rks of eukaryotic cell signaling is the expansion of enzyme families to inc lude hundreds of specialized members that carry out diverse biological processes. Protein kinases represent one such family, where a conserved protein fold and core biochem ical function have been elaborated on through the introduction of dist inct substrate specificities and divergent modes of regulation. Dissecting the molecular basis for specialization within this large enzyme family will guide our understanding of the architectures of cell signaling pathways an d aid in the design of selective kinase-targeted drugs. These efforts may b e augmented by the recent development of high-throughput biochemical a pproaches that couple the analysis of protein function to next-generation D NA sequencing. I will discuss my efforts to dissect the evolution and speci alization of the protein tyrosine kinases involved in T cell receptor signa ling using a high-throughput platform to interrogate kinase substrate speci ficity. These experiments point to divergent molecular recognition features of two essential kinases, Lck and ZAP-70, that ensure faithful signaling d uring the early stages of T cell activation. T cells play a central role in modern cancer immunotherapies, and these insights may be useful for the de velopment and improvement of such therapies. Furthermore, the high-throughp ut biochemical techniques described in my talk will be valuable tools for t he characterization of other signaling enzymes.
~Coffee/t ea will be served prior to lecture.~
DTSTAMP:20240329T095347 DTSTART:20171219T160000 DTEND:20171219T170000 SEQUENCE:0 TRANSP:OPAQUE END:VEVENT END:VCALENDAR