Alberts, S.M., Sonntag, C., Schafer, A., and Wolf, D.H. (2009). Ubx4 modulates Cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulum. J. Biol. Chem. 284, 16082–16089.Google Scholar
Alexandru, G., Graumann, J., Smith, G.T., Kolawa, N.J., Fang, R., and Deshaies, R.J. (2008). UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134, 804–816.Google Scholar
Auld, K.L. and Silver, P.A. (2006). Transcriptional regulation by the proteasome as a mechanism for cellular protein homeostasis. Cell Cycle 5, 1503–1505.CrossrefPubMedGoogle Scholar
Bernales, S., McDonald, K.L., and Walter, P. (2006a). Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4, e423.CrossrefGoogle Scholar
Bernales, S., Papa, F.R., and Walter, P. (2006b). Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22, 487–508.PubMedCrossrefGoogle Scholar
Bernales, S., Schuck, S., and Walter, P. (2007). ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3, 285–287.PubMedGoogle Scholar
Bhattacharya, S., Shcherbik, N., Vasilescu, J., Smith, J.C., Figeys, D., and Haines, D.S. (2009). Identification of lysines within membrane-anchored Mga2p120 that are targets of Rsp5p ubiquitination and mediate mobilization of tethered Mga2p90. J. Mol. Biol. 385, 718–725.Google Scholar
Bigay, J. and Antonny, B. (2012). Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity. Dev. Cell 23, 886–895.CrossrefPubMedGoogle Scholar
Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002). Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615–621.CrossrefGoogle Scholar
Bretscher, M.S. and Munro, S. (1993). Cholesterol and the Golgi apparatus. Science 261, 1280–1281.Google Scholar
Brown, M.S. and Goldstein, J.L. (2009). Cholesterol feedback: from Schoenheimer’s bottle to Scap’s MELADL. J. Lipid Res. 50, S15–S27.Google Scholar
Buchberger, A., Howard, M.J., Proctor, M., and Bycroft, M. (2001). The UBX domain: a widespread ubiquitin-like module. J. Mol. Biol. 307, 17–24.Google Scholar
Carvalho, P., Goder, V., and Rapoport, T.A. (2006). Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126, 361–373.Google Scholar
Chellappa, R., Kandasamy, P., Oh, C.S., Jiang, Y., Vemula, M., and Martin, C.E. (2001). The membrane proteins, Spt23p and Mga2p, play distinct roles in the activation of Saccharomyces cerevisiae OLE1 gene expression. Fatty acid-mediated regulation of Mga2p activity is independent of its proteolytic processing into a soluble transcription activator. J. Biol. Chem. 276, 43548–43556.Google Scholar
Coskun, U., Grzybek, M., Drechsel, D., and Simons, K. (2011). Regulation of human EGF receptor by lipids. Proc. Natl. Acad. Sci. USA 108, 9044–9048.Google Scholar
Cox, J.S., Shamu, C.E., and Walter, P. (1993). Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197–1206.Google Scholar
Dowhan, W. and Bogdanov, M. (2009). Lipid-dependent membrane protein topogenesis. Annu. Rev. Biochem. 78, 515–540.CrossrefPubMedGoogle Scholar
Ejsing, C.S., Sampaio, J.L., Surendranath, V., Duchoslav, E., Ekroos, K., Klemm, R.W., Simons, K., and Shevchenko, A. (2009). Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry. Proc. Natl. Acad. Sci. USA 106, 2136–2141.CrossrefGoogle Scholar
Elbaz, Y. and Schuldiner, M. (2011). Staying in touch: the molecular era of organelle contact sites. Trends Biochem. Sci. 36, 616–623.CrossrefPubMedGoogle Scholar
English, A.R. and Voeltz, G.K. (2013). Endoplasmic reticulum structure and interconnections with other organelles. Cold Spring Harb. Perspect. Biol. 5, a013227.Google Scholar
Ernst, R., Mueller, B., Ploegh, H.L., and Schlieker, C. (2009). The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell 36, 28–38.Google Scholar
Ernst, R., Claessen, J.H., Mueller, B., Sanyal, S., Spooner, E., van der Veen, A.G., Kirak, O., Schlieker, C.D., Weihofen, W.A., and Ploegh, H.L. (2011). Enzymatic blockade of the ubiquitin-proteasome pathway. PLoS Biol. 8, e1000605.CrossrefGoogle Scholar
Fei, W., Wang, H., Fu, X., Bielby, C., and Yang, H. (2009). Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae. Biochem. J. 424, 61–67.CrossrefGoogle Scholar
Foresti, O., Ruggiano, A., Hannibal-Bach, H.K., Ejsing, C.S., and Carvalho, P. (2013). Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4. eLife 2, e00953.Google Scholar
Fu, S., Yang, L., Li, P., Hofmann, O., Dicker, L., Hide, W., Lin, X., Watkins, S.M., Ivanov, A.R., and Hotamisligil, G.S. (2011). Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity. Nature 473, 528–531.Google Scholar
Goldstein, J.L., DeBose-Boyd, R.A., and Brown, M.S. (2006). Protein sensors for membrane sterols. Cell 124, 35–46.CrossrefPubMedGoogle Scholar
Grillitsch, K., Connerth, M., Kofeler, H., Arrey, T.N., Rietschel, B., Wagner, B., Karas, M., and Daum, G. (2011). Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: lipidome meets proteome. Biochim. Biophys. Acta 1811, 1165–1176.Google Scholar
Hammond, G.R., Fischer, M.J., Anderson, K.E., Holdich, J., Koteci, A., Balla, T., and Irvine, R.F. (2012). PI4P and PI(4,5)P2 are essential but independent lipid determinants of membrane identity. Science 337, 727–730.Google Scholar
Hampton, R.Y., Gardner, R.G., and Rine, J. (1996). Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029–2044.Google Scholar
Han, X. and Gross, R.W. (2005). Shotgun lipidomics: electrospray ionization mass spectrometric analysis and quantitation of cellular lipidomes directly from crude extracts of biological samples. Mass Spectrom. Rev. 24, 367–412.CrossrefGoogle Scholar
Han, S., Lone, M.A., Schneiter, R., and Chang, A. (2010). Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control. Proc. Natl. Acad. Sci. USA 107, 5851–5856.CrossrefGoogle Scholar
Henry, S.A., Kohlwein, S.D., and Carman, G.M. (2012). Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae. Genetics 190, 317–349.Google Scholar
Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H.D., and Jentsch, S. (2000). Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577–586.Google Scholar
Jacquier, N., Choudhary, V., Mari, M., Toulmay, A., Reggiori, F., and Schneiter, R. (2011). Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Sci. 124, 2424–2437.CrossrefGoogle Scholar
Jonikas, M.C., Collins, S.R., Denic, V., Oh, E., Quan, E.M., Schmid, V., Weibezahn, J., Schwappach, B., Walter, P., Weissman, J.S., et al. (2009). Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323, 1693–1697.Google Scholar
Kaiser, H.J., Orlowski, A., Rog, T., Nyholm, T.K., Chai, W., Feizi, T., Lingwood, D., Vattulainen, I., and Simons, K. (2011). Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching. Proc. Natl. Acad. Sci. USA 108, 16628–16633.CrossrefGoogle Scholar
Kandasamy, P., Vemula, M., Oh, C.S., Chellappa, R., and Martin, C.E. (2004). Regulation of unsaturated fatty acid biosynthesis in Saccharomyces: the endoplasmic reticulum membrane protein, Mga2p, a transcription activator of the OLE1 gene, regulates the stability of the OLE1 mRNA through exosome-mediated mechanisms. J. Biol. Chem. 279, 36586–36592.Google Scholar
Kim, H., Zhang, H., Meng, D., Russell, G., Lee, J.N., and Ye, J. (2013). UAS domain of Ubxd8 and FAF1 polymerizes upon interaction with long-chain unsaturated fatty acids. J. Lipid Res. 54, 2144–2152.CrossrefGoogle Scholar
Klemm, R.W., Ejsing, C.S., Surma, M.A., Kaiser, H.J., Gerl, M.J., Sampaio, J.L., de Robillard, Q., Ferguson, C., Proszynski, T.J., Shevchenko, A., et al. (2009). Segregation of sphingolipids and sterols during formation of secretory vesicles at the trans-Golgi network. J. Cell Biol. 185, 601–612.Google Scholar
Klemm, E.J., Spooner, E., and Ploegh, H.L. (2011). Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control. J. Biol. Chem. 286, 37602–37614.CrossrefGoogle Scholar
Klose, C., Surma, M.A., and Simons, K. (2013). Organellar lipidomics – background and perspectives. Curr. Opin. Cell Biol. 25, 406–413.PubMedCrossrefGoogle Scholar
Kohlwein, S.D., Veenhuis, M., and van der Klei, I.J. (2013). Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fat – store ’em up or burn ’em down. Genetics 193, 1–50.Google Scholar
Kolawa, N.J., Sweredoski, M.J., Graham, R.L.J., Oania, R., Hess, S., and Deshaies, R.J. (2013). Perturbations to the ubiquitin conjugate proteome in yeast Δubx mutants identify Ubx2 as a regulator of membrane lipid composition. Mol. Cell Proteomics 12, 2791–2803.PubMedCrossrefGoogle Scholar
Korennykh, A. and Walter, P. (2012). Structural basis of the unfolded protein response. Annu. Rev. Cell Dev. Biol. 28, 251–277.CrossrefPubMedGoogle Scholar
Krumpe, K., Frumkin, I., Herzig, Y., Rimon, N., Ozbalci, C., Brugger, B., Rapaport, D., and Schuldiner, M. (2012). Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes. Mol. Biol. Cell 23, 3927–3935.CrossrefPubMedGoogle Scholar
Lajoie, P., Moir, R.D., Willis, I.M., and Snapp, E.L. (2012). Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells. Mol. Biol. Cell 23, 955–964.CrossrefGoogle Scholar
Lee, J.N., Zhang, X., Feramisco, J.D., Gong, Y., and Ye, J. (2008). Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step. J. Biol. Chem. 283, 33772–33783.Google Scholar
Lee, J.N., Kim, H., Yao, H., Chen, Y., Weng, K., and Ye, J. (2010). Identification of Ubxd8 protein as a sensor for unsaturated fatty acids and regulator of triglyceride synthesis. Proc. Natl. Acad. Sci. USA 107, 21424–21429.CrossrefGoogle Scholar
Lin, J.H., Walter, P., and Yen, T.S. (2008). Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 3, 399–425.CrossrefPubMedGoogle Scholar
Listenberger, L.L., Han, X., Lewis, S.E., Cases, S., Farese, R.V., Jr., Ory, D.S., and Schaffer, J.E. (2003). Triglyceride accumulation protects against fatty acid-induced lipotoxicity. Proc. Natl. Acad. Sci. USA 100, 3077–3082.CrossrefGoogle Scholar
Loewen, C.J., Gaspar, M.L., Jesch, S.A., Delon, C., Ktistakis, N.T., Henry, S.A., and Levine, T.P. (2004). Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science 304, 1644–1647.Google Scholar
Martin, C.E., Oh, C.S., and Jiang, Y. (2007). Regulation of long chain unsaturated fatty acid synthesis in yeast. Biochim. Biophys. Acta 1771, 271–285.Google Scholar
Meusser, B., Hirsch, C., Jarosch, E., and Sommer, T. (2005). ERAD: the long road to destruction. Nat. Cell Biol. 7, 766–772.CrossrefGoogle Scholar
Meyer, H., Bug, M., and Bremer, S. (2012). Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117–123.PubMedGoogle Scholar
Mitra, K., Ubarretxena-Belandia, I., Taguchi, T., Warren, G., and Engelman, D.M. (2004). Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc. Natl. Acad. Sci. USA 101, 4083–4088.CrossrefGoogle Scholar
Mueller, B., Klemm, E.J., Spooner, E., Claessen, J.H., and Ploegh, H.L. (2008). SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Natl. Acad. Sci. USA 105, 12325–12330.Google Scholar
Needham, P.G. and Brodsky, J.L. (2013). How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochim. Biophys. Acta 1833, 2447–2457.Google Scholar
Neuber, O., Jarosch, E., Volkwein, C., Walter, J., and Sommer, T. (2005). Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat. Cell Biol. 7, 993–998.CrossrefGoogle Scholar
Nilsson, I., Ohvo-Rekila, H., Slotte, J.P., Johnson, A.E., and von Heijne, G. (2001). Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols. J. Biol. Chem. 276, 41748–41754.Google Scholar
Olzmann, J.A. and Kopito, R.R. (2011). Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation. J. Biol. Chem. 286, 27872–27874.CrossrefGoogle Scholar
Olzmann, J.A., Richter, C.M., and Kopito, R.R. (2013). Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. USA 110, 1345–1350.Google Scholar
Park, E. and Rapoport, T.A. (2012). Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu. Rev. Biophys. 41, 21–40.CrossrefGoogle Scholar
Petschnigg, J., Wolinski, H., Kolb, D., Zellnig, G., Kurat, C.F., Natter, K., and Kohlwein, S.D. (2009). Good fat, essential cellular requirements for triacylglycerol synthesis to maintain membrane homeostasis in yeast. J. Biol. Chem. 284, 30981–30993.Google Scholar
Piehler, J., Thomas, C., Garcia, K.C., and Schreiber, G. (2012). Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation. Immunol. Rev. 250, 317–334.Google Scholar
Ploegh, H.L. (2007). A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 448, 435–438.Google Scholar
Promlek, T., Ishiwata-Kimata, Y., Shido, M., Sakuramoto, M., Kohno, K., and Kimata, Y. (2011). Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol. Biol. Cell 22, 3520–3532.CrossrefGoogle Scholar
Radhakrishnan, A., Goldstein, J.L., McDonald, J.G., and Brown, M.S. (2008). Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance. Cell Metab. 8, 512–521.PubMedCrossrefGoogle Scholar
Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., and Jentsch, S. (2001). Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107, 667–677.CrossrefGoogle Scholar
Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005). A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73–84.Google Scholar
Rodriguez-Boulan, E. and Powell, S.K. (1992). Polarity of epithelial and neuronal cells. Annu. Rev. Cell Biol. 8, 395–427.Google Scholar
Sampaio, J.L., Gerl, M.J., Klose, C., Ejsing, C.S., Beug, H., Simons, K., and Shevchenko, A. (2011). Membrane lipidome of an epithelial cell line. Proc. Natl. Acad. Sci. USA 108, 1903–1907.CrossrefGoogle Scholar
Schaffer, J.E. (2003). Lipotoxicity: when tissues overeat. Curr. Opin. Lipidol. 14, 281–287.PubMedCrossrefGoogle Scholar
Schuberth, C. and Buchberger, A. (2005). Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat. Cell Biol. 7, 999–1006.CrossrefGoogle Scholar
Schuck, S., Prinz, W.A., Thorn, K.S., Voss, C., and Walter, P. (2009). Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell Biol. 187, 525–536.Google Scholar
Schuldiner, M., Collins, S.R., Thompson, N.J., Denic, V., Bhamidipati, A., Punna, T., Ihmels, J., Andrews, B., Boone, C., Greenblatt, J.F., et al. (2005). Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123, 507–519.Google Scholar
Sharpe, H.J., Stevens, T.J., and Munro, S. (2010). A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142, 158–169.Google Scholar
Shcherbik, N. and Haines, D.S. (2007). Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol. Cell 25, 385–397.Google Scholar
Shcherbik, N., Zoladek, T., Nickels, J.T., and Haines, D.S. (2003). Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr. Biol. 13, 1227–1233.CrossrefGoogle Scholar
Shevchenko, A. and Simons, K. (2010). Lipidomics: coming to grips with lipid diversity. Nature Rev. Mol. Cell Biol. 11, 593–598.CrossrefGoogle Scholar
Shuai, K. and Liu, B. (2003). Regulation of JAK-STAT signalling in the immune system. Nat. Rev. Immunol. 3, 900–911.PubMedCrossrefGoogle Scholar
Simons, K. and Gerl, M.J. (2010). Revitalizing membrane rafts: new tools and insights. Nature Rev. Mol. Cell Biol. 11, 688–699.CrossrefGoogle Scholar
Spandl, J., Lohmann, D., Kuerschner, L., Moessinger, C., and Thiele, C. (2011). Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region. J. Biol. Chem. 286, 5599–5606.Google Scholar
Stolz, A., Hilt, W., Buchberger, A., and Wolf, D.H. (2011). Cdc48: a power machine in protein degradation. Trends Biochem. Sci. 36, 515–523.CrossrefGoogle Scholar
Stukey, J.E., McDonough, V.M., and Martin, C.E. (1990). The OLE1 gene of Saccharomyces cerevisiae encodes the Δ9 fatty acid desaturase and can be functionally replaced by the rat stearoyl-CoA desaturase gene. J. Biol. Chem. 265, 20144–20149.Google Scholar
Surma, M.A., Klose, C., Peng, D., Shales, M., Mrejen, C., Stefanko, A., Braberg, H., Gordon, D.E., Vorkel, D., Ejsing, C.S., et al. (2013). A lipid E-MAP identifies Ubx2 as a critical regulator of lipid saturation and lipid bilayer stress. Mol. Cell 51, 519–530.CrossrefGoogle Scholar
Thibault, G., Shui, G., Kim, W., McAlister, G.C., Ismail, N., Gygi, S.P., Wenk, M.R., and Ng, D.T. (2012). The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network. Mol. Cell 48, 16–27.CrossrefPubMedGoogle Scholar
Thomas, C., Moraga, I., Levin, D., Krutzik, P.O., Podoplelova, Y., Trejo, A., Lee, C., Yarden, G., Vleck, S.E., Glenn, J.S., et al. (2011). Structural linkage between ligand discrimination and receptor activation by type I interferons. Cell 146, 621–632.Google Scholar
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.CrossrefGoogle Scholar
Varshavsky, A. (1997). The ubiquitin system. Trends Biochem. Sci. 22, 383–387.CrossrefPubMedGoogle Scholar
Volmer, R., van der Ploeg, K., and Ron, D. (2013). Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc. Natl. Acad. Sci. USA 110, 4628–4633.Google Scholar
von Heijne, G. (1989). Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341, 456–458.Google Scholar
Walter, P. and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081–1086.Google Scholar
Wang, C.W. and Lee, S.C. (2012). The ubiquitin-like (UBX)-domain-containing protein Ubx2/Ubxd8 regulates lipid droplet homeostasis. J. Cell Sci. 125, 2930–2939.CrossrefGoogle Scholar
Wenk, M.R. (2005). The emerging field of lipidomics. Nat. Rev. Drug Discov. 4, 594–610.PubMedCrossrefGoogle Scholar
Werstuck, G.H., Lentz, S.R., Dayal, S., Hossain, G.S., Sood, S.K., Shi, Y.Y., Zhou, J., Maeda, N., Krisans, S.K., Malinow, M.R., et al. (2001). Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J. Clin. Invest. 107, 1263–1273.CrossrefGoogle Scholar
Xu, G., Sztalryd, C., Lu, X., Tansey, J.T., Gan, J., Dorward, H., Kimmel, A.R., and Londos, C. (2005). Post-translational regulation of adipose differentiation-related protein by the ubiquitin/proteasome pathway. J. Biol. Chem. 280, 42841–42847.Google Scholar
Yamamoto, K., Takahara, K., Oyadomari, S., Okada, T., Sato, T., Harada, A., and Mori, K. (2010). Induction of liver steatosis and lipid droplet formation in ATF6α-knockout mice burdened with pharmacological endoplasmic reticulum stress. Mol. Biol. Cell 21, 2975–2986.Google Scholar
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