Fig. 1: Domain architecture and cellular localization of human EHBP1.
From: The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members
a EHBP1 contains an N-terminal C2-like domain (NT-C2), a central CH (calponin homology) domain, and a C-terminal a coiled-coil bMERB (bivalent Mical/EHBP Rab binding) domain. At the end of the bMERB domain, EHBP1 also has a C-terminal prenylation motif (CaaX box). In addition to these domains, EHBP1 harbors five NPF motifs. Isoform 1 is composed of 1231 amino acids and isoform 3 lacks residues 212–246 and residues 905–940. b Cellular localization of different EGFP tagged EHBP1 constructs. Scale bar: 10 µm. c, d EGFP-EHBP1 shows strong co-localization with mCherry tagged Rab8aQ67L and mCherry tagged Rab10Q68L. Scale bar: 10 µm. Experiments were repeated at least three times independently with similar results. e Lipid-binding activity of NT-C2 domain of EHBP1. Lipid spots present on the PIP strip are indicated in the left panel. LPA Lysophosphatidic Acid, LPC lysophosphatidylcholine, PtdIns phosphatidylinositol, PI(3)P phosphatidylinositol-3-phosphate, PI(4)P phosphatidylinositol-4-phosphate, PI(5)P phosphatidylinositol-5-phosphate, PE phosphatidylethanolamine, PC phosphatidylcholine, S1P sphingosine-1-phosphate, PI(3,4)P2 phosphatidylinositol-3,4-bisphosphate, PI(3,5)P2 phosphatidylinositol-3,5-bisphosphate, PI(4,5)P2 phosphatidylinositol-4,5-bisphosphate, PI(3,4,5)P3 phosphatidylinositol-3,4,5-trisphosphate, PA phosphatidic acid, PS phosphatidylserine. Experiments were repeated at least three times independently with similar results.
