PROSITE documentation PDOC51848
bMERB domain profile


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:

  • Animal proteins of the Molecules Interacting with CasL (Mical) family, multidomain, mainly cytoplasmic, proteins, which participate in the control of actin cytoskeleton dynamics.
  • Animal Eps15-homolgy (EH) domain binding proteins (EHBPs), couple vesicular transport to the actin cytoskeleton.
  • Animal C16orf45 proteins.

The profile we developed covers the entire bMERB domain.

Last update:

November 2017 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

BMERB, PS51848; bMERB domain profile  (MATRIX)


1AuthorsRai A. Oprisko A. Campos J. Fu Y. Friese T. Itzen A. Goody R.S. Gazdag E.M. Muller M.P.
TitlebMERB domains are bivalent Rab8 family effectors evolved by gene duplication.
SourceElife 5:0-0(2016).
PubMed ID27552051

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