Membrane Protein Dislocation by the Rhomboid Pseudoprotease Dfm1: No Pore Needed?

Dönem Avci; Marius K Lemberg

doi:10.1016/j.molcel.2017.12.031

Membrane Protein Dislocation by the Rhomboid Pseudoprotease Dfm1: No Pore Needed?

Mol Cell. 2018 Jan 18;69(2):161-162. doi: 10.1016/j.molcel.2017.12.031.

Authors

Dönem Avci¹, Marius K Lemberg²

Affiliations

¹ Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
² Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. Electronic address: m.lemberg@zmbh.uni-heidelberg.de.

PMID: 29351840
DOI: 10.1016/j.molcel.2017.12.031

Abstract

Defective ER-resident membrane proteins need to be ejected into the cytoplasm in order to be degraded by the proteasome, but the exact mechanism remains unclear. In this issue of Molecular Cell, Neal et al. (2018) reveal that the rhomboid pseudoprotease Dfm1 defines the central ERAD component for membrane protein dislocation.

Publication types

Comment

MeSH terms

Endoplasmic Reticulum
Endoplasmic Reticulum-Associated Degradation*
Membrane Proteins*
Proteasome Endopeptidase Complex

Substances

Membrane Proteins
Proteasome Endopeptidase Complex