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Abstract
The Elmo protein family members are important mediators of small G protein activity, regulating actin-mediated processes such as chemotaxis and engulfment. Until recently,1 Elmo function has not been explored in professional phagocytes such as Dictyostelium discoideum. We discuss the significance of this family with respect to pathways that regulate Rac signaling, we present a comparison of Elmo proteins between representative taxa, and discuss our findings on ElmoA, one of six Elmo proteins found in D. discoideum.
Acknowledgements
This commentary is supported by NIAID/NIH intramural funds.
Figures and Tables
Figure 1 A relatedness tree of Elmo domains from proteins of five species is shown. The domain borders (indicated after each protein name below) were identified by a protein blast query of the full-length sequence. Species represented are Dictyostelium discoideum (Dd; red; elmoA: 364–551; elmoB: 106–266; elmoC: 363–547; elmoD: 288–456; elmoE (split domain): 477–566, 628–700; and elmoF (split domain): 259–350, 410–478), Homo sapiens (Hs; black; ELMO1: 300–482; ELMO2: 292–475; ELMO3: 175–356; ELMOD1: 115–304; ELMOD2: 112–272; ELMOD3: 151–314), Caenorhabditis elegans (Ce; green; C56G7.3: 123–293; Ced-12: 362–475), Drosophila melanogaster (Dm; purple; CG10068-PA: 121–290; Ced-12: 297–480) and Aspergillus niger (An; blue; AnCG5336: 220–410). Note that the Dd Elmo domains of elmoE and elmoF are split by poly-glutamine stretches, common in Dictyostelium proteins, which have been eliminated for the alignment. Highlighted in light blue are Elmo proteins reported to promote GEF activity. Highlighted in yellow are Elmo proteins speculated to promote GAP activity based on their proximity to the functionally characterized human ElmoD1 and D2 proteins and on preliminary results. Sequences were aligned with ClustalW2 (http://www.ebi.ac.uk/Tools/clustalw2/index.html). The resulting guide tree (dnd) was used to create a circular tree in the Java phylogenetic tree viewer Hypertree (http://kinase.com/tools/HyperTree.html; and ref. Citation24).
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