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UID:DSC-22892
DTSTART;TZID=Europe/Berlin:20260611T110000
SEQUENCE:1781156240
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20260611T120000
URL:https://dresden-science-calendar.org/calendar/de/detail/22892
LOCATION:MPI-CBG\, Pfotenhauerstraße 10801307 Dresden
SUMMARY:Schumann: Chemical Precision Tools to Dissect Protein Glycosylation
CLASS:PUBLIC
DESCRIPTION:Speaker: Benjamin Schumann\nInstitute of Speaker: TU Dresden\nT
 opics:\n\n Location:\n  Name: MPI-CBG (MPI-CBG CBG Large Auditorium)\n  St
 reet: Pfotenhauerstraße 108\n  City: 01307 Dresden\n  Phone: +49 351 210-
 0\n  Fax: +49 351 210-2000\nDescription: Alterations in glycoprotein expre
 ssion and composition are an undisputed corollary of developmental process
 es\, host-pathogen interactions and cancer formation. Consequently\, some 
 of the most important tumor biomarkers are heavily glycosylated. Understan
 ding cellular glycoproteome changes is paramount but hampered by experimen
 tal limitations. Protein glycosylation is mediated by the activities of &g
 t\;200 glycosyltransferases mainly located in the secretory pathway. Since
  these transferases are interdependent through compensation and competitio
 n\, traditional methods of molecular cell biology fail to fully address th
 e complexity of glycoprotein biosynthesis. Furthermore\, workflows in mass
  spec-glycoproteome analysis are often restricted to isolated cell lines t
 hat do not adequately reflect the interactions within tissues or between t
 umor and microenvironment. Thus\, we lack strategies to understand 1) the 
 protein substrate specificities of individual glycosyltransferases and 2) 
 which glycoproteins are made by cells in response to their microenvironmen
 t. We also 3) miss chemical probes to investigate and disrupt cancer-relev
 ant glycosylation. Here\, I describe our development of chemical “Precis
 ion Tools” to dissect cellular glycosylation. We employ bump-and-hole (B
 H) engineering to render glycosyltransferases receptive to a chemically mo
 dified nucleotide-sugar substrate that carries a bioorthogonal tag and is 
 not used by wildtype transferases. Engineering individual transferases all
 ows differential profiling of their protein substrate specificities. We fo
 und that establishing cellular BH systems required innovation in the deliv
 ery of corresponding nucleotide-sugarsto the secretory pathway. We have al
 so taken initiative in the development of small molecule inhibitors agains
 t cancer-relevant glycosylation enzymes. Thus\, chemical Precision Tools a
 llow us to profile protein glycosylation as a key player in cancer biology
 .
DTSTAMP:20260618T073013Z
CREATED:20260512T053711Z
LAST-MODIFIED:20260611T053720Z
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