Identification of a novel protein interaction between Elmo1 and Cdc27

Biochem Biophys Res Commun. 2016 Mar 18;471(4):497-502. doi: 10.1016/j.bbrc.2016.02.046. Epub 2016 Feb 13.

Abstract

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.

Keywords: Cdc27; Dock1; Efferocytosis; Elmo; Interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome / genetics
  • Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome / metabolism*
  • Binding Sites
  • HEK293 Cells / metabolism
  • Humans
  • Phagocytosis / physiology
  • Protein Interaction Mapping / methods
  • rac GTP-Binding Proteins / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome
  • CDC27 protein, human
  • DOCK1 protein, human
  • ELMO1 protein, human
  • rac GTP-Binding Proteins