A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells
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 throug...
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pubmed-43064512015-07-07 A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells Yang, Hengwen Chen, Yu-Zen Zhang, Yi Wang, Xiaohui Zhao, Xiang Godfroy, James I. Liang, Qian Zhang, Man Zhang, Tianying Yuan, Quan Royal, Mary Ann Driscoll, Monica Xia, Ning-Shao Yin, Hang Xue, Ding Article 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. 2015-01-07 /pmc/articles/PMC4306451/ /pubmed/25564762 http://dx.doi.org/10.1038/ncomms6717 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
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Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Yang, Hengwen Chen, Yu-Zen Zhang, Yi Wang, Xiaohui Zhao, Xiang Godfroy, James I. Liang, Qian Zhang, Man Zhang, Tianying Yuan, Quan Royal, Mary Ann Driscoll, Monica Xia, Ning-Shao Yin, Hang Xue, Ding |
spellingShingle |
Yang, Hengwen Chen, Yu-Zen Zhang, Yi Wang, Xiaohui Zhao, Xiang Godfroy, James I. Liang, Qian Zhang, Man Zhang, Tianying Yuan, Quan Royal, Mary Ann Driscoll, Monica Xia, Ning-Shao Yin, Hang Xue, Ding A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
author_facet |
Yang, Hengwen Chen, Yu-Zen Zhang, Yi Wang, Xiaohui Zhao, Xiang Godfroy, James I. Liang, Qian Zhang, Man Zhang, Tianying Yuan, Quan Royal, Mary Ann Driscoll, Monica Xia, Ning-Shao Yin, Hang Xue, Ding |
author_sort |
Yang, Hengwen |
title |
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
title_short |
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
title_full |
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
title_fullStr |
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
title_full_unstemmed |
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells |
title_sort |
lysine-rich motif in the phosphatidylserine receptor psr-1 mediates recognition and removal of apoptotic cells |
description |
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. |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4306451/ |
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1613180743935066112 |