Thymosin β4 is involved in stabilin-2-mediated apoptotic cell engulfment

Sung Jin Lee, In Seop So, Seung Yoon Park, In-San Kim

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Stabilin-2 was recently identified as a novel receptor for membrane phosphatidylserine of apoptotic cells. To identify proteins that were candidates for stabilin-2 cytoplasmic domain binding, we screened a human spleen cDNA library using the yeast two-hybrid system. We found that thymosin β4 interacts with the stabilin-2 cytoplasmic domain and is co-localized with stabilin-2 at the phagocytic cup. Knockdown of thymosin β4 significantly decreased the phagocytic activity of stabilin-2, whereas overexpression of thymosin β4 increased this activity. Additionally, amino acids 2504-2514 of stabilin-2 cytoplasmic domain were found to be responsible for the interaction with thymosin β4. Taken together, these results suggest that thymosin β4 is a downstream molecule of stabilin-2 that plays a role in stabilin-2-mediated cell corpse clearance. Structured summary: MINT-6542321, MINT-6542357:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by anti tag coimmunoprecipitation (MI:0007)MINT-6542368:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by pull down (MI:0096)MINT-6542300:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P62328) by two hybrid (MI:0018).

Original languageEnglish
Pages (from-to)2161-2166
Number of pages6
JournalFEBS Letters
Volume582
Issue number15
DOIs
Publication statusPublished - 2008 Jun 25
Externally publishedYes

Fingerprint

Thymosin
Cells
Two-Hybrid System Techniques
Phosphatidylserines
Hybrid systems
Gene Library
Cadaver
Yeast
Spleen
Membranes
Amino Acids
Molecules
Proteins

Keywords

  • Phagocytosis
  • Stabilin-2
  • Thymosin β4
  • Yeast two-hybrid analysis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Thymosin β4 is involved in stabilin-2-mediated apoptotic cell engulfment. / Lee, Sung Jin; So, In Seop; Park, Seung Yoon; Kim, In-San.

In: FEBS Letters, Vol. 582, No. 15, 25.06.2008, p. 2161-2166.

Research output: Contribution to journalArticle

Lee, Sung Jin ; So, In Seop ; Park, Seung Yoon ; Kim, In-San. / Thymosin β4 is involved in stabilin-2-mediated apoptotic cell engulfment. In: FEBS Letters. 2008 ; Vol. 582, No. 15. pp. 2161-2166.
@article{6960fca7b4a04c4fb4ddf14a134f5db3,
title = "Thymosin β4 is involved in stabilin-2-mediated apoptotic cell engulfment",
abstract = "Stabilin-2 was recently identified as a novel receptor for membrane phosphatidylserine of apoptotic cells. To identify proteins that were candidates for stabilin-2 cytoplasmic domain binding, we screened a human spleen cDNA library using the yeast two-hybrid system. We found that thymosin β4 interacts with the stabilin-2 cytoplasmic domain and is co-localized with stabilin-2 at the phagocytic cup. Knockdown of thymosin β4 significantly decreased the phagocytic activity of stabilin-2, whereas overexpression of thymosin β4 increased this activity. Additionally, amino acids 2504-2514 of stabilin-2 cytoplasmic domain were found to be responsible for the interaction with thymosin β4. Taken together, these results suggest that thymosin β4 is a downstream molecule of stabilin-2 that plays a role in stabilin-2-mediated cell corpse clearance. Structured summary: MINT-6542321, MINT-6542357:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by anti tag coimmunoprecipitation (MI:0007)MINT-6542368:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by pull down (MI:0096)MINT-6542300:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P62328) by two hybrid (MI:0018).",
keywords = "Phagocytosis, Stabilin-2, Thymosin β4, Yeast two-hybrid analysis",
author = "Lee, {Sung Jin} and So, {In Seop} and Park, {Seung Yoon} and In-San Kim",
year = "2008",
month = "6",
day = "25",
doi = "10.1016/j.febslet.2008.03.058",
language = "English",
volume = "582",
pages = "2161--2166",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "15",

}

TY - JOUR

T1 - Thymosin β4 is involved in stabilin-2-mediated apoptotic cell engulfment

AU - Lee, Sung Jin

AU - So, In Seop

AU - Park, Seung Yoon

AU - Kim, In-San

PY - 2008/6/25

Y1 - 2008/6/25

N2 - Stabilin-2 was recently identified as a novel receptor for membrane phosphatidylserine of apoptotic cells. To identify proteins that were candidates for stabilin-2 cytoplasmic domain binding, we screened a human spleen cDNA library using the yeast two-hybrid system. We found that thymosin β4 interacts with the stabilin-2 cytoplasmic domain and is co-localized with stabilin-2 at the phagocytic cup. Knockdown of thymosin β4 significantly decreased the phagocytic activity of stabilin-2, whereas overexpression of thymosin β4 increased this activity. Additionally, amino acids 2504-2514 of stabilin-2 cytoplasmic domain were found to be responsible for the interaction with thymosin β4. Taken together, these results suggest that thymosin β4 is a downstream molecule of stabilin-2 that plays a role in stabilin-2-mediated cell corpse clearance. Structured summary: MINT-6542321, MINT-6542357:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by anti tag coimmunoprecipitation (MI:0007)MINT-6542368:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by pull down (MI:0096)MINT-6542300:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P62328) by two hybrid (MI:0018).

AB - Stabilin-2 was recently identified as a novel receptor for membrane phosphatidylserine of apoptotic cells. To identify proteins that were candidates for stabilin-2 cytoplasmic domain binding, we screened a human spleen cDNA library using the yeast two-hybrid system. We found that thymosin β4 interacts with the stabilin-2 cytoplasmic domain and is co-localized with stabilin-2 at the phagocytic cup. Knockdown of thymosin β4 significantly decreased the phagocytic activity of stabilin-2, whereas overexpression of thymosin β4 increased this activity. Additionally, amino acids 2504-2514 of stabilin-2 cytoplasmic domain were found to be responsible for the interaction with thymosin β4. Taken together, these results suggest that thymosin β4 is a downstream molecule of stabilin-2 that plays a role in stabilin-2-mediated cell corpse clearance. Structured summary: MINT-6542321, MINT-6542357:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by anti tag coimmunoprecipitation (MI:0007)MINT-6542368:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P20065) by pull down (MI:0096)MINT-6542300:Stab2-c (uniprotkb:Q8WWQ8) physically interacts (MI:0218) with tb4 (uniprotkb:P62328) by two hybrid (MI:0018).

KW - Phagocytosis

KW - Stabilin-2

KW - Thymosin β4

KW - Yeast two-hybrid analysis

UR - http://www.scopus.com/inward/record.url?scp=44749087582&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=44749087582&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2008.03.058

DO - 10.1016/j.febslet.2008.03.058

M3 - Article

C2 - 18519035

AN - SCOPUS:44749087582

VL - 582

SP - 2161

EP - 2166

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 15

ER -