1. Copine A Interacts with Actin Filaments and Plays a Role in Chemotaxis and Adhesion.
- Author
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Buccilli MJ, Ilacqua AN, Han M, Banas AA, Wight EM, Mao H, Perry SP, Salter TS, Loiselle DR, Haystead TAJ, and Damer CK
- Subjects
- Calcium metabolism, Carrier Proteins genetics, Cell Adhesion, Dictyostelium physiology, Protein Binding, Protozoan Proteins genetics, Actin Cytoskeleton metabolism, Carrier Proteins metabolism, Chemotaxis, Dictyostelium metabolism, Protozoan Proteins metabolism
- Abstract
Copines make up a family of calcium-dependent, phospholipid-binding proteins found in numerous eukaryotic organisms. Copine proteins consist of two C2 domains at the N-terminus followed by an A domain similar to the von Willebrand A domain found in integrins. We are studying copine protein function in the model organism, Dictyostelium discoideum , which has six copine genes, cpnA-cpnF . Previous research showed that cells lacking the cpnA gene exhibited a cytokinesis defect, a contractile vacuole defect, and developmental defects. To provide insight into the role of CpnA in these cellular processes, we used column chromatography and immunoprecipitation to isolate proteins that bind to CpnA. These proteins were identified by mass spectrometry. One of the proteins identified was actin. Purified CpnA was shown to bind to actin filaments in a calcium-dependent manner in vitro. cpnA
- cells exhibited defects in three actin-based processes: chemotaxis, cell polarity, and adhesion. These results suggest that CpnA plays a role in chemotaxis and adhesion and may do so by interacting with actin filaments.- Published
- 2019
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