2. Academic Validation
  3. EphA2 Interacts with Tim-4 through Association between Its FN3 Domain and the IgV Domain of Tim-4

EphA2 Interacts with Tim-4 through Association between Its FN3 Domain and the IgV Domain of Tim-4

  • Cells. 2021 May 22;10(6):1290. doi: 10.3390/cells10061290.
Byeongjin Moon 1 2,  Susumin Yang 1 2,  Kwangwoo Kim 1,  Juyeon Lee 1 2,  Dongtak Jeong 3,  Daeho Park 1 2
Affiliations

Affiliations

  • 1 School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
  • 2 Center for Cell Mechanobiology, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
  • 3 Department of Molecular and Life Science, College of Science and Convergence Technology, Hanyang University ERICA Campus, Ansan 15588, Korea.
PMID: 34067457 DOI: 10.3390/cells10061290
Abstract

Tim-4 promotes the engulfment of apoptotic cells or exogenous particles by securing them on phagocytes. It is unable to transduce signals by itself but helps Other engulfment receptors sense and internalize them. However, the identity of the engulfment receptors collaborating with Tim-4 is still incompletely understood. In this study, we searched for a candidate transmembrane protein with a FN3 domain, important for interaction with Tim-4, in silico and investigated whether it indeed interacts with Tim-4 and is involved in Tim-4-mediated phagocytosis. We found that EphA2 containing a FN3 domain in the extracellular region interacted with Tim-4, which was mediated by the IgV domain of Tim-4 and the FN3 domain of EphA2. Nevertheless, we found that EphA2 expression failed to alter Tim-4-mediated phagocytosis of apoptotic cells or polystyrene beads. Taken together, our findings suggest that EphA2, a new Tim-4 interacting protein, may intervene in a Tim-4-mediated cellular event even if it is not phagocytosis of endogenous or exogenous particles and vice versa.

Keywords

EphA2; FN3 domain; IgV domain; Tim-4; efferocytosis; interaction.

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