Research Topics
| Stefan G KreftSummaryAffiliation: University of Konstanz Country: Germany Publications
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Detail Information
Publications
An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzymeStefan G Kreft
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 8114, USA
J Biol Chem 286:20163-74. 2011..These results suggest that the TEB4-Doa10 domain regulates Doa10 association with the Ubc6 membrane anchor, thereby controlling the degradation rate of the E2...
Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligaseEric M Rubenstein
Deptartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
J Cell Biol 197:761-73. 2012..Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon...
Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathwaysTommer Ravid
Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
EMBO J 25:533-43. 2006..Thus, while Doa10 ubiquitinates both membrane and soluble proteins, the mechanisms of subsequent proteasome targeting differ...
Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)Stefan G Kreft
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 8114, USA
J Biol Chem 281:4646-53. 2006..Finally, we provide evidence that the likely human Doa10 ortholog, TEB4 (MARCH-VI), adopts a topology similar to that of Doa10...
