Abstract
Proteins that fail to fold correctly in the endoplasmic reticulum (ER) are retrotranslocated back into the cytosol where they become ubiquitinated and are eventually degraded by the proteasome. This process is called ER-associated protein degradation (ERAD). Recent research revealed that the ER-membrane protein Hrd1, an E3 ubiquitin ligase, forms a minimal system to translocate misfolded proteins across the membrane of the ER.
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Alexander Stein 1998–2003 Biochemiestudium an der FU Berlin. 2003–2008 Promotion am Max-Planck-Institut für biophysikalische Chemie, Göttingen, dort 2008–2009 Postdoc. 2010–2014 Postdoc bei Prof. Dr. T. A. Rapoport, Harvard Medical School, Boston, MA, USA. Seit 2014 Gruppenleiter am Max-Planck-Institut für biophysikalische Chemie, Göttingen.
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Stein, A. Retrotranslokation über die ER-Membran durch die Ubiquitinligase Hrd1. Biospektrum 22, 459–461 (2016). https://doi.org/10.1007/s12268-016-0711-2
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DOI: https://doi.org/10.1007/s12268-016-0711-2