Palmitoylation in apoptosis.
apoptosis
deacyltransferases
palmitoylation
palmitoyltransferases
protein modification
Journal
Journal of cellular physiology
ISSN: 1097-4652
Titre abrégé: J Cell Physiol
Pays: United States
ID NLM: 0050222
Informations de publication
Date de publication:
08 2023
08 2023
Historique:
revised:
26
04
2023
received:
29
01
2023
accepted:
08
05
2023
medline:
17
8
2023
pubmed:
1
6
2023
entrez:
1
6
2023
Statut:
ppublish
Résumé
Palmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates. S-palmitoylation, as the only reversible palmitoylation modification, is able to be deacylated by deacyltransferases. As an important mode of programmed cell death, apoptosis functions in the maintenance of organismal homeostasis as well as being associated with inflammatory and immune diseases. Recently, studies have found that palmitoylation and apoptosis have been demonstrated to be related in many human diseases. In this review, we will focus on the role of palmitoylation modifications in apoptosis.
Substances chimiques
Proteins
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1641-1650Informations de copyright
© 2023 Wiley Periodicals LLC.
Références
Adachi, N., Hess, D. T., Kaku, M., Ueda, C., Numa, C., & Saito, N. (2019). Differential s-palmitoylation of the human and rodent β3-adrenergic receptors. Journal of Biological Chemistry, 294(7), 2569-2578. https://doi.org/10.1074/jbc.RA118.004978
Adachi, N., Hess, D. T., McLaughlin, P., & Stamler, J. S. (2016). S-Palmitoylation of a novel site in the β2-Adrenergic receptor associated with a novel intracellular itinerary. Journal of Biological Chemistry, 291(38), 20232-20246. https://doi.org/10.1074/jbc.M116.725762
Akimzhanov, A. M., & Boehning, D. (2015). Rapid and transient palmitoylation of the tyrosine kinase Lck mediates Fas signaling. Proceedings of the National Academy of Sciences, 112(38), 11876-11880. https://doi.org/10.1073/pnas.1509929112
Ashkenazi, A., & Dixit, V. M. (1998). Death receptors: Signaling and modulation. Science, 281(5381), 1305-1308. https://doi.org/10.1126/science.281.5381.1305.
Bannan, B. A., Van Etten, J., Kohler, J. A., Tsoi, Y., Hansen, N. M., Sigmon, S., Fowler, E., Buff, H., Williams, T. S., Ault, J. G., Glaser, R. L., & Korey, C. A. (2008). The drosophila protein palmitoylome: Characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases. Fly, 2(4), 198-214. https://doi.org/10.4161/fly.6621
Beck, M. W., Kathayat, R. S., Cham, C. M., Chang, E. B., & Dickinson, B. C. (2017). Michael addition-based probes for ratiometric fluorescence imaging of protein s-depalmitoylases in live cells and tissues. Chemical Science, 8(11), 7588-7592. https://doi.org/10.1039/c7sc02805a
Bidère, N., Su, H. C., & Lenardo, M. J. (2006). Genetic disorders of programmed cell death in the immune system. Annual Review of Immunology, 24, 321-352. https://doi.org/10.1146/annurev.immunol.24.021605.090513
Boada-Romero, E., Martinez, J., Heckmann, B. L., & Green, D. R. (2020). The clearance of dead cells by efferocytosis. Nature Reviews Molecular Cell Biology, 21(7), 398-414. https://doi.org/10.1038/s41580-020-0232-1
Brozzi, F., Gerlo, S., Grieco, F. A., Juusola, M., Balhuizen, A., Lievens, S., Gysemans, C., Bugliani, M., Mathieu, C., Marchetti, P., Tavernier, J., & Eizirik, D. L. (2016). Ubiquitin D regulates IRE1α/c-Jun n-terminal kinase (JNK) protein-dependent apoptosis in pancreatic beta cells. Journal of Biological Chemistry, 291(23), 12040-12056. https://doi.org/10.1074/jbc.M115.704619
Cahuzac, N., Baum, W., Kirkin, V., Conchonaud, F., Wawrezinieck, L., Marguet, D., Janssen, O., Zörnig, M., & Hueber, A. O. (2006). Fas ligand is localized to membrane rafts, where it displays increased cell death-inducing activity. Blood, 107(6), 2384-2391. https://doi.org/10.1182/blood-2005-07-2883
Chakrabandhu, K., Hérincs, Z., Huault, S., Dost, B., Peng, L., Conchonaud, F., Marguet, D., He, H. T., & Hueber, A. O. (2007). Palmitoylation is required for efficient Fas cell death signaling. The EMBO Journal, 26(1), 209-220. https://doi.org/10.1038/sj.emboj.7601456
Chamberlain, L. H., & Shipston, M. J. (2015). The physiology of protein s-acylation. Physiological Reviews, 95(2), 341-376. https://doi.org/10.1152/physrev.00032.2014
Chen, B., Sun, Y., Niu, J., Jarugumilli, G. K., & Wu, X. (2018). Protein lipidation in cell signaling and diseases: Function, regulation, and therapeutic opportunities. Cell Chemical Biology, 25(7), 817-831. https://doi.org/10.1016/j.chembiol.2018.05.003
Chen, G., & Goeddel, D. V. (2002). TNF-R1 signaling: A beautiful pathway. Science, 296(5573), 1634-1635. https://doi.org/10.1126/science.1071924
Chen, X., Li, H., Fan, X., Zhao, C., Ye, K., Zhao, Z., Hu, L., Ma, H., Wang, H., & Fang, Z. (2020). Protein palmitoylation regulates cell survival by modulating XBP1 activity in glioblastoma multiforme. Molecular Therapy - Oncolytics, 17, 518-530. https://doi.org/10.1016/j.omto.2020.05.007
Cho, E., & Park, M. (2016). Palmitoylation in Alzheimer's disease and other neurodegenerative diseases. Pharmacological Research, 111, 133-151. https://doi.org/10.1016/j.phrs.2016.06.008
Cruz, A. C., Ramaswamy, M., Ouyang, C., Klebanoff, C. A., Sengupta, P., Yamamoto, T. N., Meylan, F., Thomas, S. K., Richoz, N., Eil, R., Price, S., Casellas, R., Rao, V. K., Lippincott-Schwartz, J., Restifo, N. P., & Siegel, R. M. (2016). Fas/CD95 prevents autoimmunity independently of lipid raft localization and efficient apoptosis induction. Nature Communications, 7, 13895. https://doi.org/10.1038/ncomms13895
Dowal, L., Yang, W., Freeman, M. R., Steen, H., & Flaumenhaft, R. (2011). Proteomic analysis of palmitoylated platelet proteins. Blood, 118(13), e62-e73. https://doi.org/10.1182/blood-2011-05-353078
Duncan, J. A., & Gilman, A. G. (2002). Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein α subunit deacylation in vivo. Journal of Biological Chemistry, 277(35), 31740-31752. https://doi.org/10.1074/jbc.M202505200
Edmonds, M. J., & Morgan, A. (2014). A systematic analysis of protein palmitoylation in Caenorhabditis elegans. BMC Genomics, 15, 841. https://doi.org/10.1186/1471-2164-15-841
Feig, C., Tchikov, V., Schütze, S., & Peter, M. E. (2007). Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. The EMBO Journal, 26(1), 221-231. https://doi.org/10.1038/sj.emboj.7601460
Flaumenhaft, R., Rozenvayn, N., Feng, D., & Dvorak, A. M. (2007). SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane. Blood, 110(5), 1492-1501. https://doi.org/10.1182/blood-2006-11-055772
Fröhlich, M., Dejanovic, B., Kashkar, H., Schwarz, G., & Nussberger, S. (2014). S-palmitoylation represents a novel mechanism regulating the mitochondrial targeting of BAX and initiation of apoptosis. Cell Death & Disease, 5, e1057. https://doi.org/10.1038/cddis.2014.17.
Galluzzo, P., Caiazza, F., Moreno, S., & Marino, M. (2007). Role of ERβ palmitoylation in the inhibition of human colon cancer cell proliferation. Endocrine-related Cancer, 14(1), 153-167. https://doi.org/10.1677/ERC-06-0020
Gardai, S. J., McPhillips, K. A., Frasch, S. C., Janssen, W. J., Starefeldt, A., Murphy-Ullrich, J. E., Bratton, D. L., Oldenborg, P. A., Michalak, M., & Henson, P. M. (2005). Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell, 123(2), 321-334. https://doi.org/10.1016/j.cell.2005.08.032
Goodwin, J. S., Drake, K. R., Rogers, C., Wright, L., Lippincott-Schwartz, J., Philips, M. R., & Kenworthy, A. K. (2005). Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway. Journal of Cell Biology, 170(2), 261-272. https://doi.org/10.1083/jcb.200502063
Gorleku, O. A., Barns, A. M., Prescott, G. R., Greaves, J., & Chamberlain, L. H. (2011). Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals. Journal of Biological Chemistry, 286(45), 39573-39584. https://doi.org/10.1074/jbc.M111.272369.
Gottlieb, C. D., & Linder, M. E. (2017). Structure and function of DHHC protein s-acyltransferases. Biochemical Society Transactions, 45(4), 923-928. https://doi.org/10.1042/BST20160304
Graham, R. K., Deng, Y., Slow, E. J., Haigh, B., Bissada, N., Lu, G., Pearson, J., Shehadeh, J., Bertram, L., Murphy, Z., Warby, S. C., Doty, C. N., Roy, S., Wellington, C. L., Leavitt, B. R., Raymond, L. A., Nicholson, D. W., & Hayden, M. R. (2006). Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell, 125(6), 1179-1191. https://doi.org/10.1016/j.cell.2006.04.026
Greaves, J., & Chamberlain, L. H. (2011). DHHC palmitoyl transferases: Substrate interactions and (patho)physiology. Trends in Biochemical Sciences, 36(5), 245-253. https://doi.org/10.1016/j.tibs.2011.01.003
Greaves, J., Munro, K. R., Davidson, S. C., Riviere, M., Wojno, J., Smith, T. K., Tomkinson, N. C. O., & Chamberlain, L. H. (2017). Molecular basis of fatty acid selectivity in the zDHHC family of S-acyltransferases revealed by click chemistry. Proceedings of the National Academy of Sciences, 114(8), E1365-E1374. https://doi.org/10.1073/pnas.1612254114
Guardiola-Serrano, F., Rossin, A., Cahuzac, N., Lückerath, K., Melzer, I., Mailfert, S., Marguet, D., Zörnig, M., & Hueber, A. O. (2010). Palmitoylation of human FasL modulates its cell death-inducing function. Cell Death & Disease, 1, e88. https://doi.org/10.1038/cddis.2010.62
Hanawa-Suetsugu, K., Kukimoto-Niino, M., Mishima-Tsumagari, C., Akasaka, R., Ohsawa, N., Sekine, S., Ito, T., Tochio, N., Koshiba, S., Kigawa, T., Terada, T., Shirouzu, M., Nishikimi, A., Uruno, T., Katakai, T., Kinashi, T., Kohda, D., Fukui, Y., & Yokoyama, S. (2012). Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms. Proceedings of the National Academy of Sciences, 109(9), 3305-3310. https://doi.org/10.1073/pnas.1113512109.
Huang, K., Yanai, A., Kang, R., Arstikaitis, P., Singaraja, R. R., Metzler, M., Mullard, A., Haigh, B., Gauthier-Campbell, C., Gutekunst, C. A., Hayden, M. R., & El-Husseini, A. (2004). Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron, 44(6), 977-986. https://doi.org/10.1016/j.neuron.2004.11.027
Huynh, K. K., Eskelinen, E. L., Scott, C. C., Malevanets, A., Saftig, P., & Grinstein, S. (2007). LAMP proteins are required for fusion of lysosomes with phagosomes. The EMBO Journal, 26(2), 313-324. https://doi.org/10.1038/sj.emboj.7601511
Jin, J., Zhi, X., Wang, X., & Meng, D. (2021). Protein palmitoylation and its pathophysiological relevance. Journal of Cellular Physiology, 236(5), 3220-3233. https://doi.org/10.1002/jcp.30122
Kanda, S., Yanagitani, K., Yokota, Y., Esaki, Y., & Kohno, K. (2016). Autonomous translational pausing is required for XBP1u mRNA recruitment to the ER via the SRP pathway. Proceedings of the National Academy of Sciences, 113(40), E5886-E5895. https://doi.org/10.1073/pnas.1604435113
Kawano, M., & Nagata, S. (2018). Efferocytosis and autoimmune disease. International Immunology, 30(12), 551-558. https://doi.org/10.1093/intimm/dxy055
Kischkel, F. C., Hellbardt, S., Behrmann, I., Germer, M., Pawlita, M., Krammer, P. H., & Peter, M. E. (1995). Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. The EMBO Journal, 14(22), 5579-5588. https://doi.org/10.1002/j.1460-2075.1995.tb00245.x
Kleuss, C. (2003). Galpha(s) is palmitoylated at the N-terminal glycine. The EMBO Journal, 22(4), 826-832. https://doi.org/10.1093/emboj/cdg095
Klíma, M., Zájedová, J., Doubravská, L., & Anděra, L. (2009). Functional analysis of the posttranslational modifications of the death receptor 6. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1793(10), 1579-1587. https://doi.org/10.1016/j.bbamcr.2009.07.008
Kuida, K., Haydar, T. F., Kuan, C. Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S. S., Rakic, P., & Flavell, R. A. (1998). Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell, 94(3), 325-337. https://doi.org/10.1016/s0092-8674(00)81476-2
Lai, T. Y., Cao, J., Ou-Yang, P., Tsai, C. Y., Lin, C. W., Chen, C. C., Tsai, M. K., & Lee, C. Y. (2022). Different methods of detaching adherent cells and their effects on the cell surface expression of Fas receptor and Fas ligand. Scientific Reports, 12(1), 5713. https://doi.org/10.1038/s41598-022-09605-y
Lauber, K., Bohn, E., Kröber, S. M., Xiao, Y., Blumenthal, S. G., Lindemann, R. K., Marini, P., Wiedig, C., Zobywalski, A., Baksh, S., Xu, Y., Autenrieth, I. B., Schulze-Osthoff, K., Belka, C., Stuhler, G., & Wesselborg, S. (2003). Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal. Cell, 113(6), 717-730. https://doi.org/10.1016/s0092-8674(03)00422-7
Li, P., Jing, H., Wang, Y., Yuan, L., Xiao, H., & Zheng, Q. (2021). SUMO modification in apoptosis. Journal of Molecular Histology, 52(1), 1-10. https://doi.org/10.1007/s10735-020-09924-2
Lin, D. T. S., & Conibear, E. (2015). ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization. eLife, 4, e11306. https://doi.org/10.7554/eLife.11306
Linder, M. E., & Deschenes, R. J. (2007). Palmitoylation: Policing protein stability and traffic. Nature Reviews Molecular Cell Biology, 8(1), 74-84. https://doi.org/10.1038/nrm2084
Man, S. M., & Kanneganti, T. D. (2016). Converging roles of caspases in inflammasome activation, cell death and innate immunity. Nature Reviews Immunology, 16(1), 7-21. https://doi.org/10.1038/nri.2015.7
Martin, B. R., Wang, C., Adibekian, A., Tully, S. E., & Cravatt, B. F. (2011). Global profiling of dynamic protein palmitoylation. Nature Methods, 9(1), 84-89. https://doi.org/10.1038/nmeth.1769
Mérino, D., Lalaoui, N., Morizot, A., Schneider, P., Solary, E., & Micheau, O. (2006). Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2. Molecular and Cellular Biology, 26(19), 7046-7055. https://doi.org/10.1128/MCB.00520-06
Milligan, G., Parenti, M., & Magee, A. I. (1995). The dynamic role of palmitoylation in signal transduction. Trends in Biochemical Sciences, 20(5), 181-186. https://doi.org/10.1016/s0968-0004(00)89004-0.
Morioka, S., Maueröder, C., & Ravichandran, K. S. (2019). Living on the edge: Efferocytosis at the interface of homeostasis and pathology. Immunity, 50(5), 1149-1162. https://doi.org/10.1016/j.immuni.2019.04.018
Nagata, S. (2005). DNA degradation in development and programmed cell death. Annual Review of Immunology, 23, 853-875. https://doi.org/10.1146/annurev.immunol.23.021704.115811
Nagata, S. (2018). Apoptosis and clearance of apoptotic cells. Annual Review of Immunology, 36, 489-517. https://doi.org/10.1146/annurev-immunol-042617-053010
Nagata, S., Hanayama, R., & Kawane, K. (2010). Autoimmunity and the clearance of dead cells. Cell, 140(5), 619-630. https://doi.org/10.1016/j.cell.2010.02.014
Newton, K., Wickliffe, K. E., Maltzman, A., Dugger, D. L., Reja, R., Zhang, Y., Roose-Girma, M., Modrusan, Z., Sagolla, M. S., Webster, J. D., & Dixit, V. M. (2019). Activity of caspase-8 determines plasticity between cell death pathways. Nature, 575(7784), 679-682. https://doi.org/10.1038/s41586-019-1752-8
Palacios, E. H., & Weiss, A. (2004). Function of the Src-family kinases, Lck and fyn, in T-cell development and activation. Oncogene, 23(48), 7990-8000. https://doi.org/10.1038/sj.onc.1208074
Pepinsky, R. B., Zeng, C., Wen, D., Rayhorn, P., Baker, D. P., Williams, K. P., Bixler, S. A., Ambrose, C. M., Garber, E. A., Miatkowski, K., Taylor, F. R., Wang, E. A., & Galdes, A. (1998). Identification of a palmitic acid-modified form of human sonic hedgehog. Journal of Biological Chemistry, 273(22), 14037-14045. https://doi.org/10.1074/jbc.273.22.14037
Peter, M. E., & Krammer, P. H. (2003). The CD95(APO-1/Fas) DISC and beyond. Cell Death & Differentiation, 10(1), 26-35. https://doi.org/10.1038/sj.cdd.4401186
Poggi, M., Kara, I., Brunel, J. M., Landrier, J. F., Govers, R., Bonardo, B., Fluhrer, R., Haass, C., Alessi, M. C., & Peiretti, F. (2013). Palmitoylation of TNF alpha is involved in the regulation of TNF receptor 1 signalling. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1833(3), 602-612. https://doi.org/10.1016/j.bbamcr.2012.11.009
Reddien, P. W., Cameron, S., & Horvitz, H. R. (2001). Phagocytosis promotes programmed cell death in C. elegans. Nature, 412(6843), 198-202. https://doi.org/10.1038/35084096
Rink, J., Ghigo, E., Kalaidzidis, Y., & Zerial, M. (2005). Rab conversion as a mechanism of progression from early to late endosomes. Cell, 122(5), 735-749. https://doi.org/10.1016/j.cell.2005.06.043
Rocks, O., Gerauer, M., Vartak, N., Koch, S., Huang, Z. P., Pechlivanis, M., Kuhlmann, J., Brunsveld, L., Chandra, A., Ellinger, B., Waldmann, H., & Bastiaens, P. I. H. (2010). The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins. Cell, 141(3), 458-471. https://doi.org/10.1016/j.cell.2010.04.007
Rongvaux, A., Jackson, R., Harman, C. C. D., Li, T., West, A. P., de Zoete, M. R., Wu, Y., Yordy, B., Lakhani, S. A., Kuan, C. Y., Taniguchi, T., Shadel, G. S., Chen, Z. J., Iwasaki, A., & Flavell, R. A. (2014). Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA. Cell, 159(7), 1563-1577. https://doi.org/10.1016/j.cell.2014.11.037
Rossin, A., Derouet, M., Abdel-Sater, F., & Hueber, A. O. (2009). Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling. Biochemical Journal, 419(1), 185-194. https://doi.org/10.1042/BJ20081212
Rossin, A., Durivault, J., Chakhtoura-Feghali, T., Lounnas, N., Gagnoux-Palacios, L., & Hueber, A. O. (2015). Fas palmitoylation by the palmitoyl acyltransferase DHHC7 regulates Fas stability. Cell Death & Differentiation, 22(4), 643-653. https://doi.org/10.1038/cdd.2014.153
Salaun, C., Greaves, J., & Chamberlain, L. H. (2010). The intracellular dynamic of protein palmitoylation. Journal of Cell Biology, 191(7), 1229-1238. https://doi.org/10.1083/jcb.201008160
Siegel, R. M., Ka-Ming chan, F., Chun, H. J., & Lenardo, M. J. (2000). The multifaceted role of fas signaling in immune cell homeostasis and autoimmunity. Nature Immunology, 1(6), 469-474. https://doi.org/10.1038/82712
Silke, J., & Meier, P. (2013). Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation. Cold Spring Harbor Perspectives in Biology, 5(2), a008730. https://doi.org/10.1101/cshperspect.a008730)
Skotte, N. H., Sanders, S. S., Singaraja, R. R., Ehrnhoefer, D. E., Vaid, K., Qiu, X., Kannan, S., Verma, C., & Hayden, M. R. (2017). Palmitoylation of caspase-6 by HIP14 regulates its activation. Cell Death & Differentiation, 24(3), 433-444. https://doi.org/10.1038/cdd.2016.139
Tait, J. F., & Smith, C. (1999). Phosphatidylserine receptors: Role of CD36 in binding of anionic phospholipid vesicles to monocytic cells. Journal of Biological Chemistry, 274(5), 3048-3054. https://doi.org/10.1074/jbc.274.5.3048
Takada, R., Satomi, Y., Kurata, T., Ueno, N., Norioka, S., Kondoh, H., Takao, T., & Takada, S. (2006). Monounsaturated fatty acid modification of Wnt protein: Its role in Wnt secretion. Developmental Cell, 11(6), 791-801. https://doi.org/10.1016/j.devcel.2006.10.003
Tan, S., Liu, X., Chen, L., Wu, X., Tao, L., Pan, X., Tan, S., Liu, H., Jiang, J., & Wu, B. (2021). Fas/FasL mediates NF-κBp65/PUMA-modulated hepatocytes apoptosis via autophagy to drive liver fibrosis. Cell Death & Disease, 12(5), 474. https://doi.org/10.1038/s41419-021-03749-x
Truman, L. A., Ford, C. A., Pasikowska, M., Pound, J. D., Wilkinson, S. J., Dumitriu, I. E., Melville, L., Melrose, L. A., Ogden, C. A., Nibbs, R., Graham, G., Combadiere, C., & Gregory, C. D. (2008). CX3CL1/fractalkine is released from apoptotic lymphocytes to stimulate macrophage chemotaxis. Blood, 112(13), 5026-5036. https://doi.org/10.1182/blood-2008-06-162404
Utsumi, T., Takeshige, T., Tanaka, K., Takami, K., Kira, Y., Klostergaard, J., & Ishisaka, R. (2001). Transmembrane TNF (pro-TNF) is palmitoylated. FEBS Letters, 500(1-2), 1-6. https://doi.org/10.1016/s0014-5793(01)02576-5
Wang, J., Hao, J. W., Wang, X., Guo, H., Sun, H. H., Lai, X. Y., Liu, L. Y., Zhu, M., Wang, H. Y., Li, Y. F., Yu, L. Y., Xie, C., Wang, H. R., Mo, W., Zhou, H. M., Chen, S., Liang, G., & Zhao, T. J. (2019). DHHC4 and DHHC5 facilitate fatty acid uptake by palmitoylating and targeting CD36 to the plasma membrane. Cell Reports, 26(1), 209-221. https://doi.org/10.1016/j.celrep.2018.12.022
Wang, S., & El-Deiry, W. S. (2003). TRAIL and apoptosis induction by TNF-family death receptors. Oncogene, 22(53), 8628-8633. https://doi.org/10.1038/sj.onc.1207232
Wang, X., & Yang, C. (2016). Programmed cell death and clearance of cell corpses in Caenorhabditis elegans. Cellular and Molecular Life Sciences, 73(11-12), 2221-2236. https://doi.org/10.1007/s00018-016-2196-z
Won, S. J., Cheung See Kit, M., & Martin, B. R. (2018). Protein depalmitoylases. Critical Reviews in Biochemistry and Molecular Biology, 53(1), 83-98. https://doi.org/10.1080/10409238.2017.1409191
Yang, J., Brown, M. S., Liang, G., Grishin, N. V., & Goldstein, J. L. (2008). Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. Cell, 132(3), 387-396. https://doi.org/10.1016/j.cell.2008.01.017
Youle, R. J., & Strasser, A. (2008). The BCL-2 protein family: Opposing activities that mediate cell death. Nature Reviews Molecular Cell Biology, 9(1), 47-59. https://doi.org/10.1038/nrm2308
Yuan, L., Li, P., Jing, H., Zheng, Q., & Xiao, H. (2022). trim-21 promotes proteasomal degradation of CED-1 for apoptotic cell clearance in C. elegans. eLife, 11. https://doi.org/10.7554/eLife.76436
Yuan, L., Li, P., Zheng, Q., Wang, H., & Xiao, H. (2022). The ubiquitin-proteasome system in apoptosis and apoptotic cell clearance. Frontiers in Cell and Developmental Biology, 10, 914288. https://doi.org/10.3389/fcell.2022.914288
Yurchak, L. K., & Sefton, B. M. (1995). Palmitoylation of either Cys-3 or Cys-5 is required for the biological activity of the Lck tyrosine protein kinase. Molecular and Cellular Biology, 15(12), 6914-6922. https://doi.org/10.1128/MCB.15.12.6914
Zheng, Q., Gao, N., Sun, Q., Li, X., Wang, Y., & Xiao, H. (2021). bfc, a novel serpent co-factor for the expression of croquemort, regulates efferocytosis in Drosophila melanogaster. PLoS Genetics, 17(12), e1009947. https://doi.org/10.1371/journal.pgen.1009947
Zheng, Q., Ma, A., Yuan, L., Gao, N., Feng, Q., Franc, N. C., & Xiao, H. (2017). Apoptotic cell clearance in Drosophila melanogaster. Frontiers in immunology, 8, 1881. https://doi.org/10.3389/fimmu.2017.01881
Zingler, P., Särchen, V., Glatter, T., Caning, L., Saggau, C., Kathayat, R. S., Dickinson, B. C., Adam, D., Schneider-Brachert, W., Schütze, S., & Fritsch, J. (2019). Palmitoylation is required for TNF-R1 signaling. Cell Communication and Signaling, 17(1), 90. https://doi.org/10.1186/s12964-019-0405-8