A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells

Hengwen Yang, Yu-Zen Chen, Yi Zhang, Xiaohui Wang, Xiang Zhao, James I. Godfroy, Qian Liang, Man Zhang, Tianying Zhang, Quan Yuan, Mary Ann Royal, Monica Driscoll, Ning-Shao Xia, Hang Yin and Ding Xue ()
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Hengwen Yang: Cellular and Developmental Biology, University of Colorado
Yu-Zen Chen: Cellular and Developmental Biology, University of Colorado
Yi Zhang: School of Life Sciences, Tsinghua University
Xiaohui Wang: University of Colorado
Xiang Zhao: School of Life Sciences, Tsinghua University
James I. Godfroy: University of Colorado
Qian Liang: School of Life Sciences, Tsinghua University
Man Zhang: School of Life Sciences, Tsinghua University
Tianying Zhang: National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University
Quan Yuan: National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University
Mary Ann Royal: Rutgers, The State University of New Jersey
Monica Driscoll: Rutgers, The State University of New Jersey
Ning-Shao Xia: National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University
Hang Yin: University of Colorado
Ding Xue: Cellular and Developmental Biology, University of Colorado

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The conserved phosphatidylserine receptor (PSR) was first identified as a receptor for phosphatidylserine, an ‘eat-me’ signal exposed by apoptotic cells. However, several studies suggest that PSR may also act as an arginine demethylase, a lysyl hydroxylase, or an RNA-binding protein through its N-terminal JmjC domain. How PSR might execute drastically different biochemical activities, and whether they are physiologically significant, remain unclear. Here we report that a lysine-rich motif in the extracellular domain of PSR-1, the Caenorhabditis elegans PSR, mediates specific phosphatidylserine binding in vitro and clearance of apoptotic cells in vivo. This motif also mediates phosphatidylserine-induced oligomerization of PSR-1, suggesting a mechanism by which PSR-1 activates phagocytosis. Mutations in the phosphatidylserine-binding motif, but not in its Fe(II) binding site critical for the JmjC activity, abolish PSR-1 phagocytic function. Moreover, PSR-1 enriches and clusters around apoptotic cells during apoptosis. These results establish that PSR-1 is a conserved, phosphatidylserine-recognizing phagocyte receptor.

Date: 2015
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DOI: 10.1038/ncomms6717

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