ELMO (protein)

ELMO/CED-12 family
Identifiers
SymbolELMO_CED12
PfamPF04727
InterProIPR006816
PROSITEPDOC51335
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

ELMO (Engulfment and Cell Motility) is a family of related proteins (~82 kDa) involved in intracellular signalling networks. These proteins have no intrinsic catalytic activity and instead function as adaptors which can regulate the activity of other proteins through their ability to mediate protein-protein interactions.

This family contains members in all animals. In humans there are three paralogous isoforms:

The ELMO domain was first characterized in the CED-12 proteins of Caenorhabditis elegans and Drosophila melanogaster, which is a homolog to the ELMO protein found in mammals. This protein is involved in Rac-GTPase activation, apoptotic cell phagocytosis, cell migration, and cytoskeletal rearrangements.[1][2]

Structure and function of ELMO proteins

The ELMO family are evolutionarily conserved orthologs of the C. elegans protein CED-12. All isoforms contain a series of armadillo repeats, which begin at the N-terminus and extend around two thirds of the way along the protein, as well as a C-terminal proline-rich motif and a central PH domain.[3] They function as part of a protein complex with Dock180-related proteins to form a bipartite guanine nucleotide exchange factor for Rac (a member of the Rho family of small G proteins).[4] The Dock180-ELMO interaction requires the ELMO PH domain and also involves binding of the ELMO proline-rich motif to the Dock180 SH3 domain.[5]

References

  1. ^ Brody, Thomas. "Ced-12". The Interactive Fly. Retrieved November 11, 2015.
  2. ^ Zhou Z, Caron E, Hartwieg E, Hall A, Horvitz HR (October 2001). "The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway". Developmental Cell. 1 (4): 477–89. doi:10.1016/s1534-5807(01)00058-2. PMID 11703939.
  3. ^ Lu M, Ravichandran KS (2006). "Dock180–ELMO Cooperation in Rac Activation". Regulators and Effectors of Small GTPases: Rho Family. Methods in Enzymology. Vol. 406. pp. 388–402. doi:10.1016/S0076-6879(06)06028-9. ISBN 9780121828110. PMID 16472672.
  4. ^ Gumienny TL, Brugnera E, Tosello-Trampont AC, Kinchen JM, Haney LB, Nishiwaki K, et al. (October 2001). "CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration" (PDF). Cell. 107 (1): 27–41. doi:10.1016/S0092-8674(01)00520-7. PMID 11595183. S2CID 15232864. Archived from the original (PDF) on 2021-09-22. Retrieved 2020-06-06.
  5. ^ Komander D, Patel M, Laurin M, Fradet N, Pelletier A, Barford D, Côté JF (November 2008). "An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling". Molecular Biology of the Cell. 19 (11): 4837–51. doi:10.1091/mbc.E08-04-0345. PMC 2575150. PMID 18768751.
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