Structural highlights
Function
[HRSL4_HUMAN] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphotidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. N- and O-acylation activity is hardly detectable.[1]
Publication Abstract from PubMed
H-REV107-like family proteins TIG3 and H-REV107 are class II tumor suppressors. Here we report that the C-terminal domains (CTDs) of TIG3 and H-REV107 can induce HeLa cell death independently. The N-terminal domain (NTD) of TIG3 enhances the cell death inducing ability of CTD, while NTD of H-REV107 plays an inhibitory role. The solution structure of TIG3 NTD is very similar to that of H-REV107 in overall fold. However, the CTD binding regions on NTD are different between TIG3 and H-REV107, which may explain their functional difference. As a result, the flexible main loop of H-REV107, but not that of TIG3, is critical for its NTD to modulate its CTD in inducing cell death.
Structural and functional characterization of tumor suppressors TIG3 and H-REV107.,Wei H, Wang L, Ren X, Yu W, Lin J, Jin C, Xia B FEBS Lett. 2015 May 8;589(11):1179-86. doi: 10.1016/j.febslet.2015.04.002. Epub, 2015 Apr 11. PMID:25871522[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001
- ↑ Wei H, Wang L, Ren X, Yu W, Lin J, Jin C, Xia B. Structural and functional characterization of tumor suppressors TIG3 and H-REV107. FEBS Lett. 2015 May 8;589(11):1179-86. doi: 10.1016/j.febslet.2015.04.002. Epub, 2015 Apr 11. PMID:25871522 doi:http://dx.doi.org/10.1016/j.febslet.2015.04.002
