Abstract
The covalent attachment of lipid moieties to proteins represents an important subclass of co- or post-translational modifications in the cell. The 16-carbon fully saturated lipid palmitate is preferentially conjugated to free cysteines of peripheral or integral membrane proteins. The thioester bond formed can be reversibly hydrolyzed and thereby modulates a proteins function with regard to trafficking, compartmentation within the membrane or lipid-induced conformational changes in a cyclic manner.
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Eliot Morrison 2006–2010 Biochemiestudium an der Portland State University, Portland OR, USA. 2010–2012 Biochemie-Masterstudium an der San Francisco State University, San Francisco CA, USA. Seit 2012 Doktorand an der FU Berlin.
Britta Brügger 1988–1994 Biologie- und Biochemiestudium an der Universität Frankfurt a. M. 1994–1998 Promotion am Biochemie-Zentrum der Universität Heidelberg. 1998–2000 Postdoc am Memorial Sloan Kettering Cancer Center New York, NY, USA. 2000–2002 Postdoc am Biochemie-Zentrum der Universität Heidelberg; hier 2002–2014 Akademische Rätin/Oberrätin. Seit 2014 Professorin für Biochemie und Chemische Biologie an der Universität Heidelberg.
Hannah Wiedemann 2009–2015 Chemiestudium an der Universität Heidelberg. Seit 2016 Promotion am Biochemie-Zentrum der Universität Heidelberg.
Christian Freund 1983–1989 Chemiestudium an der Universität Düsseldorf und der LMU München. Hier 1989–1990 Diplomarbeit am Biochemischen Institut. 1990–1994 Promotion am Max-Planck-Institut für Biochemie/LMU München. 1994–1997 Postdoc an der Universität Zürich, Schweiz. 1997–2000 Postdoc an der Harvard Medical School, Boston, MA, USA. 2000–2011 unabhängiger Gruppenleiter am Leibniz-Institut für Molekulare Pharmakologie, Berlin. Seit 2011 Professor für Bio chemie an der FU Berlin.
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Morrison, E., Wiedemann, H., Brügger, B. et al. Reversible Palmitoylierung von Proteinen. Biospektrum 23, 32–35 (2017). https://doi.org/10.1007/s12268-017-0763-y
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DOI: https://doi.org/10.1007/s12268-017-0763-y