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PROSITE documentation PDOC51848 |
A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The "bivalent Mical/EHBP Rab binding" (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element [1].
The bMERB domain has a completely α-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix (see <PDB:5SZJ>) [1].
Some proteins known to contain a bMERB domain are listed below:
The profile we developed covers the entire bMERB domain.
Last update:November 2017 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Rai A. Oprisko A. Campos J. Fu Y. Friese T. Itzen A. Goody R.S. Gazdag E.M. Muller M.P. |
Title | bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. | |
Source | Elife 5:0-0(2016). | |
PubMed ID | 27552051 | |
DOI | 10.7554/eLife.18675 |