References
- Akassoglou, K., Malester, B., Xu, J., Tessarollo, L., Rosenbluth, J., and Chao, M.V. (2004). Brain-specific deletion of neuropathy target esterase/swisscheese results in neurodegeneration. Proc. Natl. Acad. Sci. U. S. A. 101, 5075-5080. https://doi.org/10.1073/pnas.0401030101
- Atkins, J. and Glynn, P. (2000). Membrane association of and critical residues in the catalytic domain of human neuropathy target esterase. J. Biol. Chem. 275, 24477-24483. https://doi.org/10.1074/jbc.M002921200
- Barneda, D. and Christian, M. (2017). Lipid droplet growth: regulation of a dynamic organelle. Curr. Opin. Cell Biol. 47, 9-15. https://doi.org/10.1016/j.ceb.2017.02.002
- Brasaemle, D.L. and Wolins, N.E. (2016). Isolation of lipid droplets from cells by density gradient centrifugation. Curr. Protoc. Cell Biol. 72, 3.15.1-3.15.13.
- Chang, P.A., Wang, Z.X., Long, D.X., Qin, W.Z., Wei, C.Y., and Wu, Y.J. (2012). Identification of two novel splicing variants of murine NTE-related esterase. Gene 497, 164-171. https://doi.org/10.1016/j.gene.2012.01.064
- Claros, M.G. and von Heijne, G. (1994). TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10, 685-686.
- Eilers, M., Shekar, S.C., Shieh, T., Smith, S.O., and Fleming, P.J. (2000). Internal packing of helical membrane proteins. Proc. Natl. Acad. Sci. U. S. A. 97, 5796-5801. https://doi.org/10.1073/pnas.97.11.5796
- Farese, R.V., Jr. and Walther, T.C. (2009). Lipid droplets finally get a little R-E-S-P-E-C-T. Cell 139, 855-860. https://doi.org/10.1016/j.cell.2009.11.005
- Fujimoto, T., Ohsaki, Y., Cheng, J., Suzuki, M., and Shinohara, Y. (2008). Lipid droplets: a classic organelle with new outfits. Histochem. Cell Biol. 130, 263-279. https://doi.org/10.1007/s00418-008-0449-0
- Fujimoto, T. and Parton, R.G. (2011). Not just fat: the structure and function of the lipid droplet. Cold Spring Harb. Perspect. Biol. 3, a004838. https://doi.org/10.1101/cshperspect.a004838
- Heier, C., Kien, B., Huang, F., Eichmann T.O., Xie, H., Zechner, R., and Chang, P.A. (2017). The phospholipase PNPLA7 functions as a lysophosphatidylcholine hydrolase and interacts with lipid droplets through its catalytic domain. J. Biol. Chem. 292, 19087-19098. https://doi.org/10.1074/jbc.M117.792978
- Hirokawa, T., Boon-Chieng, S., and Mitaku, S. (1998). SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14, 378-379. https://doi.org/10.1093/bioinformatics/14.4.378
- Hofmann, K. and Stoffel, W. (1993). TMbase - a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374, 166.
- Hristova, K., Wimley, W.C., Mishra, V.K., Anantharamiah, G.M., Segrest, J.P., and White, S.H. (2009). An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method. J. Mol. Biol. 290, 99-117. https://doi.org/10.1006/jmbi.1999.2840
- Huang, F.F., Chang, P.A., Sun, L.X., Qin, W.Z., Han, L.P., and Chen, R. (2016). The destruction box is involved in the degradation of the NTE family proteins by the proteasome. Mol. Biol. Rep. 43, 1285-1292. https://doi.org/10.1007/s11033-016-4063-2
- Kassan, A., Herms, A., Fernandez-Vidal, A., Bosch, M., Schieber, N.L., Reddy, B.J., Fajardo, A., Gelabert-Baldrich, M., Tebar, F., Enrich, C., et al. (2013). Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains. J. Cell Biol. 203, 985-1001. https://doi.org/10.1083/jcb.201305142
-
Kien, B., Grond, S., Haemmerle, G., Lass, A., Eichmann, T.O., and Radner, F.P.W. (2018). ABHD5 stimulates PNPLA1-mediated
${\omega}$ -O-acylceramide biosynthesis essential for a functional skin permeability barrier. J. Lipid Res. 59, 2360-2367. https://doi.org/10.1194/jlr.M089771 - Kienesberger, P.C., Lass, A., Preiss-Landl, K., Wolinski, H., Kohlwein, S.D., Zimmermann, R., and Zechner, R. (2008). Identification of an insulin-regulated lysophospholipase with homology to neuropathy target esterase. J. Biol. Chem. 283, 5908-5917. https://doi.org/10.1074/jbc.M709598200
- Kienesberger, P.C., Oberer, M., Lass, A., and Zechner, R. (2009). Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J. Lipid Res. 50 Suppl, S63-S68. https://doi.org/10.1194/jlr.R800082-JLR200
- Kory, N., Farese, R.V., Jr., and Walther, T.C. (2016). Targeting fat: mechanisms of protein localization to lipid droplets. Trends Cell Biol. 26, 535-546. https://doi.org/10.1016/j.tcb.2016.02.007
- Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E.L. (2001). Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580. https://doi.org/10.1006/jmbi.2000.4315
- Li, Y., Dinsdale, D., and Glynn, P. (2003). Protein domains, catalytic activity, and subcellular distribution of neuropathy target esterase in Mammalian cells. J. Biol. Chem. 278, 8820-8825. https://doi.org/10.1074/jbc.M210743200
- Lush, M.J., Li, Y., Read, D.J., Willis, A.C., and Glynn, P. (1998). Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man. Biochem. J. 332(Pt 1), 1-4. https://doi.org/10.1042/bj3320001
- Murugesan, S., Goldberg, E.B., Dou, E., and Brown, W.J. (2013). Identification of diverse lipid droplet targeting motifs in the PNPLA family of triglyceride lipases. PLoS One 8, e64950. https://doi.org/10.1371/journal.pone.0064950
-
Ohno, Y., Nara, A., Nakamichi, S., and Kihara, A. (2018). Molecular mechanism of the ichthyosis pathology of Chanarin-Dorfman syndrome: Stimulation of PNPLA1-catalyzed
${\omega}$ -O-acylceramide production by ABHD5. J. Dermatol. Sci. 92, 245-253. https://doi.org/10.1016/j.jdermsci.2018.11.005 - Ostermeyer, A.G., Ramcharan, L.T., Zeng, Y., Lublin, D.M., and Brown, D.A. (2004). Role of the hydrophobic domain in targeting caveolin-1 to lipid droplets. J. Cell Biol. 164, 69-78. https://doi.org/10.1083/jcb.200303037
- Papadopoulos, C., Orso, G., Mancuso, G., Herholz, M., Gumeni, S., Tadepalle, N., Jungst, C., Tzschichholz, A., Schauss, A., Honing, S., et al. (2015). Spastin binds to lipid droplets and affects lipid metabolism. PLoS Genet. 11, e1005149. https://doi.org/10.1371/journal.pgen.1005149
- Pichery, M., Huchenq, A., Sandhoff, R., Severino-Freire, M., Zaafouri, S., Opalka, L., Levade, T., Soldan, V., Bertrand-Michel, J., Lhuillier, E., et al. (2017). PNPLA1 defects in patients with autosomal recessive congenital ichthyosis and KO mice sustain PNPLA1 irreplaceable function in epidermal omega-O-acylceramide synthesis and skin permeability barrier. Hum. Mol. Genet. 26, 1787-1800. https://doi.org/10.1093/hmg/ddx079
- Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E., and Casida, J.E. (2003). Evidence that mouse brain neuropathy target esterase is a lysophospholipase. Proc. Natl. Acad. Sci. U. S. A. 100, 7983-7987. https://doi.org/10.1073/pnas.1232473100
- Read, D.J., Li, Y., Chao, M.V., Cavanagh, J.B., and Glynn, P. (2009). Neuropathy target esterase is required for adult vertebrate axon maintenance. J. Neurosci. 29, 11594-11600. https://doi.org/10.1523/JNEUROSCI.3007-09.2009
- Reue, K. (2011). Lipid droplet storage and metabolism: from yeast to man. J. Lipid Res. 52, 1865-1868. https://doi.org/10.1194/jlr.E020602
- Seelig, J. (2004). Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 1666, 40-50. https://doi.org/10.1016/j.bbamem.2004.08.004
- Sztalryd, C. and Brasaemle, D.L. (2017). The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1862, 1221-1232. https://doi.org/10.1016/j.bbalip.2017.07.009
- Tusnady, G.E. and Simon, I. (2001). The HMMTOP transmembrane topology prediction server. Bioinformatics 17, 849-850. https://doi.org/10.1093/bioinformatics/17.9.849
- Tzen, J.T., Lie, G.C., and Huang, A.H. (1992). Characterization of the charged components and their topology on the surface of plant seed oil bodies. J. Biol. Chem. 267, 15626-15634. https://doi.org/10.1016/S0021-9258(19)49582-3
- van Tienhoven, M., Atkins, J., Li, Y., and Glynn, P. (2002). Human neuropathy target esterase catalyzes hydrolysis of membrane lipids. J. Biol. Chem. 277, 20942-20948. https://doi.org/10.1074/jbc.M200330200
- Wijeyesakere, S.J., Richardson, R.J., and Stuckey, J.A. (2007). Modeling the tertiary structure of the patatin domain of neuropathy target esterase. Protein J. 26, 165-172. https://doi.org/10.1007/s10930-006-9058-8
- Wilson, P.A., Gardner, S.D., Lambie, N.M., Commans, S.A., and Crowther, D.J. (2006). Characterization of the human patatin-like phospholipase family. J. Lipid Res. 47, 1940-1949. https://doi.org/10.1194/jlr.M600185-JLR200
- Zaccheo, O., Dinsdale, D., Meacock, P.A., and Glynn, P. (2004). Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells. J. Biol. Chem. 279, 24024-24033. https://doi.org/10.1074/jbc.M400830200
- Zhang, C. and Liu, P. (2019). The new face of the lipid droplet: lipid droplet proteins. Proteomics 19, e1700223. https://doi.org/10.1002/pmic.201700223
Cited by
- Consensus module analysis of abdominal fat deposition across multiple broiler lines vol.22, pp.1, 2020, https://doi.org/10.1186/s12864-021-07423-6