Identification of a novel protein interaction between Elmo1 and Cdc27.

Elmo has no intrinsic catalytic activity but coordinate multiple cellular processes via their interactions with other proteins. Studies thus have been focused on identifying Elmo binding partners, but the number of characterized Elmo-interacting proteins remains limited. Here, we report Cdc27 as a novel Elmo1-interacting protein. In yeast and mammalian cells, ...
Cdc27 specifically interacted with the C-terminal region of Elmo1 essential for Dock1 association and function. The interaction of Elmo1 with Dock1 abrogated binding between Elmo1 and Cdc27, but the Dock1-Elmo1 interaction was unaffected by Cdc27. Similarly, cellular phagocytotic functions mediated by the Elmo1-Dock1-Rac module were unaffected by Cdc27 levels. In summary, a novel binding partner, Cdc27, was identified for Elmo1 and they appear to be independent of Elmo-Dock1-Rac-mediated processes.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome, Binding Sites, HEK293 Cells, Humans, Phagocytosis, Protein Interaction Mapping, rac GTP-Binding Proteins
Biochem. Biophys. Res. Commun.
Date: Mar. 18, 2016
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