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LIM and SH3 protein-1 modulates CXCR2-mediated cell migration
Dayanidhi Raman1, Jiqing Sai, Nicole F Neel
1Department of Cancer Biology, Vanderbilt University School of Medicine, Nashville, Tennessee, United States of America.
Plos One
|April 27, 2010
Summary
LIM and SH3 protein 1 (LASP-1) is a key component of the CXCR2 chemosynapse, crucial for neutrophil migration. This interaction is vital for cell motility and focal adhesion turnover in CXCR2-mediated chemotaxis.
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- CXCR2 is a chemokine receptor critical for neutrophil, macrophage, and endothelial cell migration.
- It modulates angiogenesis, wound healing, inflammation, sepsis, and atherosclerosis.
- CXCR2's function relies on dynamic protein interactions forming the "CXCR2 chemosynapse".
Purpose of the Study:
- To identify novel proteins interacting with CXCR2.
- To elucidate the role of LASP-1 in CXCR2-mediated cell migration.
Main Methods:
- Proteomic analysis (co-immunoprecipitation) of dHL-60 cells.
- Site-directed and deletion mutagenesis.
- Dominant-negative and knockdown approaches.
Main Results:
- LASP-1 was identified as a novel CXCR2-binding protein.
- LASP-1 directly binds the C-terminal domain (CTD) of CXCR2, CXCR1, CXCR3, and CXCR4.
- The LKIL motif (Iso323-Leu324) on CXCR2-CTD is the LASP-1 binding site.
- Disruption of LASP-1/CXCR2 interaction inhibited chemotaxis and focal adhesion turnover, affecting Src, paxillin, PAK1, p130CAS, and ERK1/2 activation.
Conclusions:
- LASP-1 is a critical component of the "CXCR2 chemosynapse" essential for CXCR2-mediated chemotaxis.
- LASP-1 acts as a general mediator for CXC chemokine receptor-mediated chemotaxis.
- LASP-1 may link chemokine receptors to focal adhesions, regulating cell migration.
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