Copine a interacts with actin filaments and plays a role in chemotaxis and adhesion

Matthew J. Buccilli, April N. Ilacqua, Mingxi Han, Andrew A. Banas, Elise M. Wight, Hanqian Mao, Samantha P. Perry, Tasha S. Salter, David R. Loiselle, Timothy A.J. Haystead, Cynthia K. Damer

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


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.

Original languageEnglish
Article number758
Issue number7
StatePublished - Jul 2019


  • Actin
  • Adhesion
  • CAMP
  • Calcium
  • Chemotaxis
  • Copine
  • Dictyostelium


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