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

28 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

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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