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Identification of a novel protein interaction between Elmo1 and Cdc27
- Source :
- Biochemical and biophysical research communications. 471(4)
- Publication Year :
- 2016
-
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.
- Subjects :
- 0301 basic medicine
Binding Sites
Novel protein
Chemistry
Biophysics
Cell Biology
Biochemistry
Yeast
Cell biology
rac GTP-Binding Proteins
03 medical and health sciences
030104 developmental biology
0302 clinical medicine
ELMO1
Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome
HEK293 Cells
CDC27
Phagocytosis
030220 oncology & carcinogenesis
Protein Interaction Mapping
Humans
Identification (biology)
Molecular Biology
Function (biology)
Adaptor Proteins, Signal Transducing
Subjects
Details
- ISSN :
- 10902104
- Volume :
- 471
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....911b92a8d5b773b095c7b959977930a0