8vsd

Structural highlights

Function

LRC32_HUMAN Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:19750484, PubMed:19651619, PubMed:22278742). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:22278742). Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (PubMed:22278742). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:19651619). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (By similarity).[UniProtKB:G3XA59]^{[1] [2] [3]}

References

1. ↑ Tran DQ, Andersson J, Wang R, Ramsey H, Unutmaz D, Shevach EM. GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells. Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13445-50. doi:, 10.1073/pnas.0901944106. Epub 2009 Jul 27. PMID:19651619 doi:http://dx.doi.org/10.1073/pnas.0901944106
2. ↑ Stockis J, Colau D, Coulie PG, Lucas S. Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg. Eur J Immunol. 2009 Dec;39(12):3315-22. doi: 10.1002/eji.200939684. PMID:19750484 doi:http://dx.doi.org/10.1002/eji.200939684
3. ↑ Wang R, Zhu J, Dong X, Shi M, Lu C, Springer TA. GARP regulates the bioavailability and activation of TGFbeta. Mol Biol Cell. 2012 Mar;23(6):1129-39. doi: 10.1091/mbc.E11-12-1018. Epub 2012, Jan 25. PMID:22278742 doi:http://dx.doi.org/10.1091/mbc.E11-12-1018