과제정보
This research was funded by the National Research Foundation of Korea funded by the Korea government (MSIP) (2019R1A2C1006480, 2019R1I1A1A01057419, and 2019R1A4A1028802) and by GIST Research Institute (GRI) ARI grant in 2020.
참고문헌
- Boada-Romero, E., Martinez, J., Heckmann, B.L., and Green, D.R. (2020). The clearance of dead cells by efferocytosis. Nat. Rev. Mol. Cell Biol. 21, 398-414.
- Choi, Y., Shimogawa, H., Murakami, K., Ramdas, L., Zhang, W., Qin, J., and Uesugi, M. (2006). Chemical genetic identification of the IGF-linked pathway that is mediated by STAT6 and MFP2. Chem. Biol. 13, 241-249. https://doi.org/10.1016/j.chembiol.2005.12.011
- Clark, M.R. (2011). Flippin' lipids. Nat. Immunol. 12, 373-375. https://doi.org/10.1038/ni.2024
- Elliott, J.I., Surprenant, A., Marelli-Berg, F.M., Cooper, J.C., Cassady-Cain, R.L., Wooding, C., Linton, K., Alexander, D.R., and Higgins, C.F. (2005). Membrane phosphatidylserine distribution as a non-apoptotic signalling mechanism in lymphocytes. Nat. Cell Biol. 7, 808-816. https://doi.org/10.1038/ncb1279
- Fadok, V.A., Voelker, D.R., Campbell, P.A., Cohen, J.J., Bratton, D.L., and Henson, P.M. (1992). Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148, 2207-2216.
- Hanayama, R., Tanaka, M., Miwa, K., Shinohara, A., Iwamatsu, A., and Nagata, S. (2002). Identification of a factor that links apoptotic cells to phagocytes. Nature 417, 182-187. https://doi.org/10.1038/417182a
- Kay, J.G. and Grinstein, S. (2013). Phosphatidylserine-mediated cellular signaling. Adv. Exp. Med. Biol. 991, 177-193. https://doi.org/10.1007/978-94-007-6331-9_10
- Lee, J., Park, B., Moon, B., Park, J., Moon, H., Kim, K., Lee, S.A., Kim, D., Min, C., Lee, D.H., et al. (2019). A scaffold for signaling of Tim-4-mediated efferocytosis is formed by fibronectin. Cell Death Differ. 26, 1646-1655. https://doi.org/10.1038/s41418-018-0238-9
- Lemke, G. (2013). Biology of the TAM receptors. Cold Spring Harb. Perspect. Biol. 5, a009076. https://doi.org/10.1101/cshperspect.a009076
- Lentz, B.R. (2003). Exposure of platelet membrane phosphatidylserine regulates blood coagulation. Prog. Lipid Res. 42, 423-438. https://doi.org/10.1016/S0163-7827(03)00025-0
- Lomasney, J.W., Cheng, H.F., Roffler, S.R., and King, K. (1999). Activation of phospholipase C delta1 through C2 domain by a Ca(2+)-enzymephosphatidylserine ternary complex. J. Biol. Chem. 274, 21995-22001. https://doi.org/10.1074/jbc.274.31.21995
- Min, C., Park, J., Kim, G., Moon, H., Lee, S.A., Kim, D., Moon, B., Yang, S., Lee, J., Kim, K., et al. (2020). Tim-4 functions as a scavenger receptor for phagocytosis of exogenous particles. Cell Death Dis. 11, 561. https://doi.org/10.1038/s41419-020-02773-7
- Miyanishi, M., Tada, K., Koike, M., Uchiyama, Y., Kitamura, T., and Nagata, S. (2007). Identification of Tim4 as a phosphatidylserine receptor. Nature 450, 435-439. https://doi.org/10.1038/nature06307
- Moon, B., Lee, J., Lee, S.A., Min, C., Moon, H., Kim, D., Yang, S., Moon, H., Jeon, J., Joo, Y.E., et al. (2020a). Mertk interacts with Tim-4 to enhance Tim4-mediated efferocytosis. Cells 9, 1625. https://doi.org/10.3390/cells9071625
- Moon, H., Min, C., Kim, G., Kim, D., Kim, K., Lee, S.A., Moon, B., Yang, S., Lee, J., Yang, S.J., et al. (2020b). Crbn modulates calcium influx by regulating Orai1 during efferocytosis. Nat. Commun. 11, 5489. https://doi.org/10.1038/s41467-020-19272-0
- Nagata, S., Suzuki, J., Segawa, K., and Fujii, T. (2016). Exposure of phosphatidylserine on the cell surface. Cell Death Differ. 23, 952-961. https://doi.org/10.1038/cdd.2016.7
- Orr, J.W. and Newton, A.C. (1992). Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation. Biochemistry 31, 4667-4673. https://doi.org/10.1021/bi00134a019
- Otera, H., Setoguchi, K., Hamasaki, M., Kumashiro, T., Shimizu, N., and Fujiki, Y. (2002). Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22, 1639-1655. https://doi.org/10.1128/MCB.22.6.1639-1655.2002
- Otsuka, M., Kato, N., Ichimura, T., Abe, S., Tanaka, Y., Taniguchi, H., Hoshida, Y., Moriyama, M., Wang, Y., Shao, R.X., et al. (2005). Vitamin K2 binds 17beta-hydroxysteroid dehydrogenase 4 and modulates estrogen metabolism. Life Sci. 76, 2473-2482. https://doi.org/10.1016/j.lfs.2004.12.020
- Park, D., Han, C.Z., Elliott, M.R., Kinchen, J.M., Trampont, P.C., Das, S., Collins, S., Lysiak, J.J., Hoehn, K.L., and Ravichandran, K.S. (2011). Continued clearance of apoptotic cells critically depends on the phagocyte Ucp2 protein. Nature 477, 220-224. https://doi.org/10.1038/nature10340
- Park, D., Tosello-Trampont, A.C., Elliott, M.R., Lu, M., Haney, L.B., Ma, Z., Klibanov, A.L., Mandell, J.W., and Ravichandran, K.S. (2007). BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module. Nature 450, 430-434. https://doi.org/10.1038/nature06329
- Pierce, S.B., Walsh, T., Chisholm, K.M., Lee, M.K., Thornton, A.M., Fiumara, A., Opitz, J.M., Levy-Lahad, E., Klevit, R.E., and King, M.C. (2010). Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault Syndrome. Am. J. Hum. Genet. 87, 282-288. https://doi.org/10.1016/j.ajhg.2010.07.007
- Qadri, S.M., Bissinger, R., Solh, Z., and Oldenborg, P.A. (2017). Eryptosis in health and disease: a paradigm shift towards understanding the (patho) physiological implications of programmed cell death of erythrocytes. Blood Rev. 31, 349-361. https://doi.org/10.1016/j.blre.2017.06.001
- Ravichandran, K.S. and Lorenz, U. (2007). Engulfment of apoptotic cells: signals for a good meal. Nat. Rev. Immunol. 7, 964-974. https://doi.org/10.1038/nri2214
- Riedl, S., Rinner, B., Asslaber, M., Schaider, H., Walzer, S., Novak, A., Lohner, K., and Zweytick, D. (2011). In search of a novel target - phosphatidylserine exposed by non-apoptotic tumor cells and metastases of malignancies with poor treatment efficacy. Biochim. Biophys. Acta 1808, 2638-2645. https://doi.org/10.1016/j.bbamem.2011.07.026
- Rival, C.M., Xu, W., Shankman, L.S., Morioka, S., Arandjelovic, S., Lee, C.S., Wheeler, K.M., Smith, R.P., Haney, L.B., Isakson, B.E., et al. (2019). Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization. Nat. Commun. 10, 4456. https://doi.org/10.1038/s41467-019-12406-z
- Sakuragi, T., Kosako, H., and Nagata, S. (2019). Phosphorylation-mediated activation of mouse Xkr8 scramblase for phosphatidylserine exposure. Proc. Natl. Acad. Sci. U. S. A. 116, 2907-2912. https://doi.org/10.1073/pnas.1820499116
- Santiago, C., Ballesteros, A., Martinez-Munoz, L., Mellado, M., Kaplan, G.G., Freeman, G.J., and Casasnovas, J.M. (2007). Structures of T cell immunoglobulin mucin protein 4 show a metal-Ion-dependent ligand binding site where phosphatidylserine binds. Immunity 27, 941-951. https://doi.org/10.1016/j.immuni.2007.11.008
- Segawa, K., Kurata, S., Yanagihashi, Y., Brummelkamp, T.R., Matsuda, F., and Nagata, S. (2014). Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure. Science 344, 1164-1168. https://doi.org/10.1126/science.1252809
- Segawa, K. and Nagata, S. (2015). An apoptotic 'eat me' signal: phosphatidylserine exposure. Trends Cell Biol. 25, 639-650. https://doi.org/10.1016/j.tcb.2015.08.003
- Stace, C.L. and Ktistakis, N.T. (2006). Phosphatidic acid- and phosphatidylserine-binding proteins. Biochim. Biophys. Acta 1761, 913-926. https://doi.org/10.1016/j.bbalip.2006.03.006
- Swairjo, M.A., Concha, N.O., Kaetzel, M.A., Dedman, J.R., and Seaton, B.A. (1995). Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat. Struct. Biol. 2, 968-974. https://doi.org/10.1038/nsb1195-968
- van Meer, G., Voelker, D.R., and Feigenson, G.W. (2008). Membrane lipids: where they are and how they behave. Nat. Rev. Mol. Cell Biol. 9, 112-124. https://doi.org/10.1038/nrm2330
- Violante, S., Achetib, N., van Roermund, C.W.T., Hagen, J., Dodatko, T., Vaz, F.M., Waterham, H.R., Chen, H., Baes, M., Yu, C., et al. (2019). Peroxisomes can oxidize medium- and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4. FASEB J. 33, 4355-4364. https://doi.org/10.1096/fj.201801498r
- Voges, D., Berendes, R., Burger, A., Demange, P., Baumeister, W., and Huber, R. (1994). Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study. J. Mol. Biol. 238, 199-213. https://doi.org/10.1006/jmbi.1994.1281
- Wang, Y., Subramanian, M., Yurdagul, A., Jr., Barbosa-Lorenzi, V.C., Cai, B., de Juan-Sanz, J., Ryan, T.A., Nomura, M., Maxfield, F.R., and Tabas, I. (2017). Mitochondrial fission promotes the continued clearance of apoptotic cells by macrophages. Cell 171, 331-345.e22. https://doi.org/10.1016/j.cell.2017.08.041
- Yurdagul, A., Jr., Subramanian, M., Wang, X., Crown, S.B., Ilkayeva, O.R., Darville, L., Kolluru, G.K., Rymond, C.C., Gerlach, B.D., Zheng, Z., et al. (2020). Macrophage metabolism of apoptotic cell-derived arginine promotes continual efferocytosis and resolution of injury. Cell Metab. 31, 518-533.e10. https://doi.org/10.1016/j.cmet.2020.01.001
- Zhu, Z., Chen, J., Wang, G., Elsherbini, A., Zhong, L., Jiang, X., Qin, H., Tripathi, P., Zhi, W., Spassieva, S.D., et al. (2019). Ceramide regulates interaction of Hsd17b4 with Pex5 and function of peroxisomes. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864, 1514-1524. https://doi.org/10.1016/j.bbalip.2019.05.017
- Zwaal, R.F., Comfurius, P., and Bevers, E.M. (1998). Lipid-protein interactions in blood coagulation. Biochim. Biophys. Acta 1376, 433-453. https://doi.org/10.1016/S0304-4157(98)00018-5