| 词条 | ELMO (protein) |
| 释义 |
| Symbol = ELMO_CED12 | Name = ELMO/CED-12 family | Pfam= PF04727 | InterPro= IPR006816 | SMART= | PROSITE = PDOC51335 | SCOP = | TCDB = | PDB = }} 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 three paralogous isoforms:
Structure and functionThe 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.[1] 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).[2] The Dock180-ELMO interaction requires the ELMO PH domain and also involves binding of the ELMO proline-rich motif to the Dock180 SH3 domain.[3] References1. ^{{cite journal | vauthors = Lu M, Ravichandran KS | title = Dock180-ELMO cooperation in Rac activation | journal = Meth. Enzymol. | volume = 406 | issue = | pages = 388–402 | year = 2006 | pmid = 16472672 | doi = 10.1016/S0076-6879(06)06028-9| url = }} {{protein-stub}}2. ^{{cite journal | vauthors = Gumienny TL, Brugnera E, Tosello-Trampont AC | title = CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration | journal = Cell | volume = 107 | issue = 1 | pages = 27–41 | year = 2001 | pmid = 11595183 | doi = 10.1016/S0092-8674(01)00520-7| url = |display-authors=etal}} 3. ^{{cite journal | vauthors = Komander D, Patel M, Laurin M | title = An Alpha-Helical Extension of the ELMO1 Pleckstrin Homology Domain Mediates Direct Interaction to DOCK180 and Is Critical in Rac Signaling| journal = Mol. Biol. Cell| volume = 19 | issue = 11| pages = 4837–51|date=September 2008 | pmid = 18768751 | doi = 10.1091/mbc.E08-04-0345| url = | issn = | pmc = 2575150 |display-authors=etal}} 1 : Protein families |
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