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Trends Cell Biol. 2013 May;23(5):210-7. doi: 10.1016/j.tcb.2013.01.002. Epub 2013 Jan 28.

Sampling the membrane: function of rhomboid-family proteins.

Author information

1
Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. m.lemberg@zmbh.uni-heidelberg.de

Abstract

Rhomboids constitute a conserved protein superfamily that specifically binds membrane proteins and directs them into various different cellular pathways ranging from regulated secretion to endoplasmic reticulum (ER)-associated degradation (ERAD). Rhomboid proteases are known to release protein domains from membranes by a cut in their membrane anchor, whereas an emerging new class of rhomboid-family proteins lacks key catalytic residues and is not proteolytically active. Recent work has shown that these rhomboid pseudoproteases, including iRhoms and derlins, bind membrane proteins to regulate their fate, but the underlying molecular mechanism is not known. This review summarizes recent advances in the molecular understanding of rhomboid-family proteins and discusses common principles in how they recognize and bind proteins in the plane of the membrane.

PMID:
23369641
DOI:
10.1016/j.tcb.2013.01.002
[Indexed for MEDLINE]

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