Adaptor protein GULP is involved in stabilin-1-mediated phagocytosis

Seung Yoon Park; Sang Yeob Kim; Kae Bok Kang; In San Kim

doi:10.1016/j.bbrc.2010.06.101

Adaptor protein GULP is involved in stabilin-1-mediated phagocytosis

Seung Yoon Park, Sang Yeob Kim, Kae Bok Kang, In San Kim

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

The clearance of apoptotic cells is critical during cellular homeostasis as well as inflammation resolution. Recently, we found that stabilin-1 is a phagocytic receptor that is involved in the clearance of apoptotic cells. However, the downstream signaling pathway of stabilin-1-mediated phagocytosis remains to be investigated. Here we identify that GULP is able to specifically interact with the NPxF/Y motif of stabilin-1 cytoplasmic region. The PTB domain of GULP is necessary for interaction with stabilin-1. GULP is enriched around PS-coated beads for phagocytosis and co-localized with stabilin-1. Downregulation of endogenous GULP expression decreased stabilin-1-mediated phagocytosis. Thus, these results indicate that GULP functions as an adaptor protein for stabilin-1-mediated phagocytosis.

Original language	English
Pages (from-to)	467-472
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	398
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2010.06.101
Publication status	Published - 2010 Jul
Externally published	Yes

Keywords

Aged RBC
GULP
Phagocytosis
Phosphatidylserine
Stabilin-1

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2010.06.101

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title = "Adaptor protein GULP is involved in stabilin-1-mediated phagocytosis",

abstract = "The clearance of apoptotic cells is critical during cellular homeostasis as well as inflammation resolution. Recently, we found that stabilin-1 is a phagocytic receptor that is involved in the clearance of apoptotic cells. However, the downstream signaling pathway of stabilin-1-mediated phagocytosis remains to be investigated. Here we identify that GULP is able to specifically interact with the NPxF/Y motif of stabilin-1 cytoplasmic region. The PTB domain of GULP is necessary for interaction with stabilin-1. GULP is enriched around PS-coated beads for phagocytosis and co-localized with stabilin-1. Downregulation of endogenous GULP expression decreased stabilin-1-mediated phagocytosis. Thus, these results indicate that GULP functions as an adaptor protein for stabilin-1-mediated phagocytosis.",

keywords = "Aged RBC, GULP, Phagocytosis, Phosphatidylserine, Stabilin-1",

author = "Park, {Seung Yoon} and Kim, {Sang Yeob} and Kang, {Kae Bok} and Kim, {In San}",

note = "Funding Information: This study was supported by Basic Science Research Program through the National Research Foundation of Korea funded by the Ministry of Education, Science and Technology ( R11-2008-044-03001-0 ); by National Research Foundation of Korea Grant funded by the Korean Government ( 2009-0068687 ); by WCU (World Class University) program through the Korea Science and Engineering Foundation funded by the Ministry of Education, Science and Technology ( R33-2008-000-10054-0 ); by the Grant no. RTI04-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy (MKE) ; and by the Brain Korea 21 Project .",

year = "2010",

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doi = "10.1016/j.bbrc.2010.06.101",

language = "English",

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pages = "467--472",

journal = "Biochemical and biophysical research communications",

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AU - Park, Seung Yoon

AU - Kim, Sang Yeob

AU - Kang, Kae Bok

AU - Kim, In San

N1 - Funding Information: This study was supported by Basic Science Research Program through the National Research Foundation of Korea funded by the Ministry of Education, Science and Technology ( R11-2008-044-03001-0 ); by National Research Foundation of Korea Grant funded by the Korean Government ( 2009-0068687 ); by WCU (World Class University) program through the Korea Science and Engineering Foundation funded by the Ministry of Education, Science and Technology ( R33-2008-000-10054-0 ); by the Grant no. RTI04-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy (MKE) ; and by the Brain Korea 21 Project .

PY - 2010/7

Y1 - 2010/7

N2 - The clearance of apoptotic cells is critical during cellular homeostasis as well as inflammation resolution. Recently, we found that stabilin-1 is a phagocytic receptor that is involved in the clearance of apoptotic cells. However, the downstream signaling pathway of stabilin-1-mediated phagocytosis remains to be investigated. Here we identify that GULP is able to specifically interact with the NPxF/Y motif of stabilin-1 cytoplasmic region. The PTB domain of GULP is necessary for interaction with stabilin-1. GULP is enriched around PS-coated beads for phagocytosis and co-localized with stabilin-1. Downregulation of endogenous GULP expression decreased stabilin-1-mediated phagocytosis. Thus, these results indicate that GULP functions as an adaptor protein for stabilin-1-mediated phagocytosis.

AB - The clearance of apoptotic cells is critical during cellular homeostasis as well as inflammation resolution. Recently, we found that stabilin-1 is a phagocytic receptor that is involved in the clearance of apoptotic cells. However, the downstream signaling pathway of stabilin-1-mediated phagocytosis remains to be investigated. Here we identify that GULP is able to specifically interact with the NPxF/Y motif of stabilin-1 cytoplasmic region. The PTB domain of GULP is necessary for interaction with stabilin-1. GULP is enriched around PS-coated beads for phagocytosis and co-localized with stabilin-1. Downregulation of endogenous GULP expression decreased stabilin-1-mediated phagocytosis. Thus, these results indicate that GULP functions as an adaptor protein for stabilin-1-mediated phagocytosis.

KW - Aged RBC

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KW - Phosphatidylserine

KW - Stabilin-1

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Adaptor protein GULP is involved in stabilin-1-mediated phagocytosis

Abstract

Keywords

ASJC Scopus subject areas

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