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

Sung Jin Lee; In Seop So; Seung Yoon Park; In San Kim

doi:10.1016/j.febslet.2008.03.058

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 journal › Article › peer-review

39 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 language	English
Pages (from-to)	2161-2166
Number of pages	6
Journal	FEBS Letters
Volume	582
Issue number	15
DOIs	https://doi.org/10.1016/j.febslet.2008.03.058
Publication status	Published - 2008 Jun 25
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by Grant No. RTI04-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy, Advanced Medical Technology Cluster for Diagnosis and Prediction at Kyungpook National University; by a grant from the National R&D Program for Cancer Control, Ministry of Health & Welfare and Family Republic of Korea (0720550-2); and by the Brain Korea 21 Project.

Keywords

Phagocytosis
Stabilin-2
Thymosin β4
Yeast two-hybrid analysis

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2008.03.058

Cite this

@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 Kim, {In San}",

note = "Funding Information: This work was supported by Grant No. RTI04-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy, Advanced Medical Technology Cluster for Diagnosis and Prediction at Kyungpook National University; by a grant from the National R&D Program for Cancer Control, Ministry of Health & Welfare and Family Republic of Korea (0720550-2); and by the Brain Korea 21 Project. ",

year = "2008",

month = jun,

day = "25",

doi = "10.1016/j.febslet.2008.03.058",

language = "English",

volume = "582",

pages = "2161--2166",

journal = "FEBS Letters",

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publisher = "John Wiley and Sons Inc.",

number = "15",

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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

N1 - Funding Information: This work was supported by Grant No. RTI04-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy, Advanced Medical Technology Cluster for Diagnosis and Prediction at Kyungpook National University; by a grant from the National R&D Program for Cancer Control, Ministry of Health & Welfare and Family Republic of Korea (0720550-2); and by the Brain Korea 21 Project.

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

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DO - 10.1016/j.febslet.2008.03.058

M3 - Article

C2 - 18519035

AN - SCOPUS:44749087582

SN - 0014-5793

VL - 582

SP - 2161

EP - 2166

JO - FEBS Letters

JF - FEBS Letters

IS - 15

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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