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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Main Authors: 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
Format: Online
Language:English
Published: 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4306451/
id pubmed-4306451
recordtype oai_dc
spelling 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
repository_type 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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