Protein acyl thioesterases (Review)

References

• Smotrys JE, Linder ME. Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem 2004; 73: 559–587
   PubMed Web of Science ®Google Scholar
• Resh MD. Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci STKE 2006; 2006: 1–12
   Google Scholar
• Resh MD. Trafficking and signaling by fatty-acylated and prenylated proteins. Nat Chem Biol 2006; 2: 584–590
   PubMed Web of Science ®Google Scholar
• Pepinsky RB, Zeng C, Wen D, Rayhorn P, Baker DP, Williams KP, Bixler SA, Ambrose CM, Garber EA, Miatkowski K, Taylor FR, Wang EA, Galdes A. Identification of a palmitic acid-modified form of human Sonic hedgehog. J Biol Chem 1998; 273: 14037–14045
   PubMed Web of Science ®Google Scholar
• Kleuss C, Krause E. α(s) is palmitoylated at the N-terminal glycine. EMBO J 2003; 22: 826–832
   PubMed Web of Science ®Google Scholar
• Wolven A, Okamura H, Rosenblatt Y, Resh MD. Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association. Mol Biol Cell 1997; 8: 1159–1173
   PubMed Web of Science ®Google Scholar
• Magee AI, Gutierrez L, McKay IA, Marshall CJ, Hall A. Dynamic fatty acylation of p21N-ras. EMBO J 1987; 6: 3353–3357
   PubMed Web of Science ®Google Scholar
• Baker TL, Zheng H, Walker J, Coloff JL, Buss JE. Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-Ras. J Biol Chem 2003; 278: 19292–19300
   PubMed Web of Science ®Google Scholar
• El-Husseini AE-D, Schnell E, Dakoji S, Sweeney N, Zhou Q, Prange O, Gauthier-Campbell C, Aguilera-Moreno A, Nicoll RA, Bredt DS. Synaptic strength regulated by palmitate cycling on PSD-95. Cell 2002; 108: 849–863
   PubMed Web of Science ®Google Scholar
• Yeh DC, Duncan JA, Yamashita S, Michel T. Depalmitoylation of endothelial nitric-oxide synthase by acyl-protein thioesterase 1 is potentiated by Ca(2 + )-calmodulin. J Biol Chem 1999; 274: 33148–33154
   PubMed Web of Science ®Google Scholar
• Hawtin SR, Tobin AB, Patel S, Wheatley M. Palmitoylation of the vasopressin V1a receptor reveals different conformational requirements for signaling, agonist-induced receptor phosphorylation, and sequestration. J Biol Chem 2001; 276: 38139–38146
   PubMedGoogle Scholar
• Ponimaskin EG, Schmidt MF, Heine M, Bickmeyer U, Richter DW. 5-Hydroxytryptamine 4(a) receptor expressed in Sf9 cells is palmitoylated in an agonist-dependent manner. Biochem J 2001; 353: 627–634
   PubMed Web of Science ®Google Scholar
• Hayashi MK, Haga T. Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail. Arch Biochem Biophys 1997; 340: 376–382
   PubMed Web of Science ®Google Scholar
• Kennedy ME, Limbird LE. Palmitoylation of the α 2A-adrenergic receptor. J Biol Chem 1994; 269: 31915–31922
   PubMed Web of Science ®Google Scholar
• Loisel TP, Adam L, Hebert TE, Bouvier M. Agonist stimulation increases the turnover rate of beta 2AR-bound palmitate and promotes receptor depalmitoylation. Biochemistry 1996; 35: 15923–15932
   Google Scholar
• Petaja-Repo UE, Hogue M, Leskela TT, Markkanen PMH, Tuusa JT, Bouvier M. Distinct subcellular localization for constitutive and agonist-modulated palmitoylation of the human δ opioid receptor. J Biol Chem 2006; 281: 15780–15789
   PubMedGoogle Scholar
• Moffett S, Rousseau G, Lagacé M, Michel Bouvier. The palmitoylation state of the β2-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and β-adrenergic receptor kinase involved in its phosphorylation and desensitization. J Neurochem 2001; 76: 269–279
   PubMed Web of Science ®Google Scholar
• Soskic V, Nyakatura E, Roos M, Muller-Esterl W, Godovac-Zimmermann J. Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells. J Biol Chem 1999; 274: 8539–8545
   PubMedGoogle Scholar
• Ponimaskin E, Dumuis A, Gaven F, Barthet G, Heine M, Glebov K, Richter DW, Oppermann M. Palmitoylation of the 5-Hydroxytryptamine4a receptor regulates receptor phosphorylation, desensitization, and β-arrestin-mediated endocytosis. Mol Pharmacol 2005; 67: 1434–1443
   PubMed Web of Science ®Google Scholar
• Mumby SM, Kleuss C, Gilman AG. Receptor regulation of G-protein palmitoylation. Proc Natl Acad Sci USA 1994; 91: 2800–2804
   PubMed Web of Science ®Google Scholar
• Degtyarev MY, Spiegel AM, Jones TL. Increased palmitoylation of the Gs protein α subunit after activation by the beta-adrenergic receptor or cholera toxin. J Biol Chem 1993; 268: 23769–23772
   PubMedGoogle Scholar
• Gurdal H, Seasholtz TM, Wang HY, Brown RD, Johnson MD, Friedman E. Role of G α q or G α o proteins in α 1-adrenoceptor subtype-mediated responses in Fischer 344 rat aorta. Mol Pharmacol 1997; 52: 1064–1070
   PubMedGoogle Scholar
• Bhamre S, Wang HY, Friedman E. Serotonin-mediated palmitoylation and depalmitoylation of G alpha proteins in rat brain cortical membranes. J Pharmacol Exp Ther 1998; 286: 1482–1489
   PubMed Web of Science ®Google Scholar
• Chen CA, Manning DR. Regulation of gα i palmitoylation by activation of the 5-hydroxytryptamine-1A receptor. J Biol Chem 2000; 275: 23516–23522
   PubMed Web of Science ®Google Scholar
• Duncan JA, Gilman AG. A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein α subunits and p21RAS. J Biol Chem 1998; 273: 15830–15837
   PubMed Web of Science ®Google Scholar
• Duncan JA, Gilman AG. Autoacylation of G protein α subunits. J Biol Chem 1996; 271: 23594–23600
   PubMed Web of Science ®Google Scholar
• Veit M, Sachs K, Heckelmann M, Maretzki D, Hofmann KP, Schmidt MFG. Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation. Biochim Biophys Acta 1998; 1394: 90–98
   PubMedGoogle Scholar
• Veit M. Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin. Biochem J 2000; 345: 145–151
   PubMedGoogle Scholar
• Corvi MM, Soltys C-LM, Berthiaume LG. Regulation of mitochondrial carbamoyl-phosphate synthetase 1 activity by active site fatty acylation. J Biol Chem 2001; 276: 45704–45712
   PubMed Web of Science ®Google Scholar
• Kümmel D, Heinemann U, Veit M. Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability. Proc Natl Acad Sci USA 2006; 103: 12701–12706
   PubMed Web of Science ®Google Scholar
• Bélanger C, Ansanay H, Qanbar R, Bouvier M. Primary sequence requirements for S-acylation of β2-adrenergic receptor peptides. FEBS Lett 2001; 499: 59–64
   PubMedGoogle Scholar
• Bañó MC, Jackson CS, Magee AI. Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo. Biochem J 1998; 330: 23–731
   Google Scholar
• Lobo S, Greentree WK, Linder ME, Deschenes RJ. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J Biol Chem. 2002; 277: 41268–41273
   PubMed Web of Science ®Google Scholar
• Roth AF, Feng Y, Chen L, Davis NG. The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J Cell Biol 2002; 159: 23–28
   PubMed Web of Science ®Google Scholar
• Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR III, Davis NG. Global analysis of protein palmitoylation in yeast. Cell :1003 2006; 125: 1013
   Google Scholar
• Fukata M, Fukata Y, Adesnik H, Nicoll RA, Bredt DS. Identification of PSD-95 palmitoylating enzymes. Neuron 2004; 44: 987–996
   PubMed Web of Science ®Google Scholar
• Mitchell DA, Vasudevan A, Linder ME, Deschenes RJ. Protein palmitoylation by a family of DHHC protein S-acyltransferases. J Lipid Res 2006; 47: 1118–1127
   PubMed Web of Science ®Google Scholar
• Tsutsumi R, Fukata Y, Fukata M. Discovery of protein-palmitoylating enzymes. Pflugers Arch 2008; 456: 1199–1206
   PubMed Web of Science ®Google Scholar
• Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME. DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J Biol Chem 2005; 280: 31141–31148
   PubMed Web of Science ®Google Scholar
• Fernandez-Hernando C, Fukata M, Bernatchez PN, Fukata Y, Lin MI, Bredt DS, Sessa WC. Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase. J Cell Biol 2006; 174: 369–377
   PubMed Web of Science ®Google Scholar
• Huang K, Yanai A, Kang R, Arstikaitis P, Singaraja RR, Metzler M, Mullard A, Haigh B, Gauthier-Campbell C, Gutekunst CA, Hayden MR, El-Husseini A. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 2004; 44: 977–986
   PubMed Web of Science ®Google Scholar
• Yanai A, Huang K, Kang R, Singaraja RR, Arstikaitis P, Gan L, Orban PC, Mullard A, Cowan CM, Raymond LA, Drisdel RC, Green WN, Ravikumar B, Rubinsztein DC, El-Husseini A, Hayden MR. Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat Neurosci 2006; 9: 824–831
   PubMed Web of Science ®Google Scholar
• Keller CA, Yuan X, Panzanelli P, Martin ML, Alldred M, Sassoe-Pognetto M, Luscher B. The γ2 subunit of GABA(A) receptors is a substrate for palmitoylation by GODZ. J Neurosci 2004; 24: 5881–5891
   PubMed Web of Science ®Google Scholar
• Miura GI, Treisman JE. Lipid modification of secreted signaling proteins. Cell Cycle 2006; 5: 1184–1188
   PubMed Web of Science ®Google Scholar
• Hofmann K. A superfamily of membrane-bound O-acyltransferases with implications for Wnt signaling. Trends Biochem Sci 2000; 25: 111–112
   PubMed Web of Science ®Google Scholar
• Buglino JA, Resh MD. What is a palmitoylacyltransferase with specificity for N-palmitoylation of Sonic Hedgehog. J Biol Chem 2008; 283: 22076–22088
   PubMed Web of Science ®Google Scholar
• Miura GI, Buglino J, Alvarado D, Lemmon MA, Resh MD, Treisman JE. Palmitoylation of the EGFR ligand Spitz by Rasp increases Spitz activity by restricting its diffusion. Dev Cell 2006; 10: 167–176
   PubMedGoogle Scholar
• Zhai L, Chaturvedi D, Cumberledge S. Drosophila Wnt-1 undergoes a hydrophobic modification and is targeted to lipid rafts, a process that requires porcupine. J Biol Chem 2004; 279: 33220–33227
   PubMed Web of Science ®Google Scholar
• Yang J, Brown MS, Liang G, Grishin NV, Goldstein JL. Identification of the acyltransferase that octanoylates Ghrelin, an appetite-stimulating peptide hormone. Cell. 2008; 132: 387–396
   PubMed Web of Science ®Google Scholar
• Veit M. The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues. Biochem J 2004; 384: 233–237
   PubMedGoogle Scholar
• Dietrich LE, Gurezka R, Veit M, Ungermann C. The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion. EMBO J 2004; 23: 45–53
   PubMed Web of Science ®Google Scholar
• Smotrys JE, Schoenfish MJ, Stutz MA, Linder ME. The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p. J Cell Biol 2005; 170: 1091–1099
   PubMed Web of Science ®Google Scholar
• Meiringer CTA, Auffarth K, Hou H, Ungermann C. Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway. Traffic 2008; 9: 1510–1521
   PubMed Web of Science ®Google Scholar
• Sugimoto H, Hayashi H, Yamashita S. Purification, cDNA cloning, and regulation of lysophospholipase from rat liver. J Biol Chem 1996; 271: 7705–7711
   PubMed Web of Science ®Google Scholar
• Toyoda T, Sugimoto H, Yamashita S. Sequence, expression in Escherichia coli, and characterization of lysophospholipase II. Biochim Biophys Acta 1999; 1437: 182–193
   PubMed Web of Science ®Google Scholar
• Duncan JA, Gilman AG. Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein α subunit deacylation in vivo. J Biol Chem 2002; 277: 31740–31752
   PubMed Web of Science ®Google Scholar
• Flaumenhaft R, Rozenvayn N, Feng D, Dvorak AM. SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane. Blood 2007; 110: 1492–1501
   PubMed Web of Science ®Google Scholar
• Veit M, Schmidt MFG. Enzymatic depalmitoylation of viral glycoproteins with acyl-protein thioesterase 1 in vitro. Virology 2001; 288: 89–95
   PubMed Web of Science ®Google Scholar
• Sim DS, Dilks JR, Flaumenhaft R. Platelets possess and require an active protein palmitoylation pathway for agonist-mediated activation and in vivo thrombus formation. Arterioscler Thromb Vasc Biol 2007; 27: 1478–1485
   PubMed Web of Science ®Google Scholar
• Makita N, Sato J, Rondard P, Fukamachi H, Yuasa Y, Aldred MA, Hashimoto M, Fujita T, Iiri T. Human Gsα mutant causes pseudohypoparathyroidism type Ia/neonatal diarrhea, a potential cell-specific role of the palmitoylation cycle. Proc Natl Acad Sci USA 2007; 104: 17424–17429
   PubMedGoogle Scholar
• Robinson LJ, Michel T. Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting. Proc Natl Acad Sci USA 1995; 92: 11776–11780
   PubMed Web of Science ®Google Scholar
• Degtyarev M, Spiegel A, Jones T. Palmitoylation of a G protein α i subunit requires membrane localization not myristoylation. J Biol Chem 1994; 269: 30898–30903
   PubMedGoogle Scholar
• Hancock JF, Magee AI, Childs JE, Marshall CJ. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 1989; 57: 1167–1177
   PubMed Web of Science ®Google Scholar
• Pallavi B, Nagaraj R. Palmitoylated peptides from the cysteine-rich domain of SNAP-23 cause membrane fusion depending on peptide length, position of cysteines, and extent of palmitoylation. J Biol Chem 2003; 278: 12737–12744
   PubMedGoogle Scholar
• Vogel K, Roche PA. SNAP-23 and SNAP-25 are palmitoylated in vivo. Biochem Biophys Res Commun 1999; 258: 407–410
   PubMedGoogle Scholar
• Rose JK, Adams GA, Gallione CJ. The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition. Proc Natl Acad Sci USA 1984; 81: 2050–2054
   PubMed Web of Science ®Google Scholar
• Veit M, Kretzschmar E, Kuroda K, Garten W, Schmidt MF, Klenk HD, Rott R. Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J Virol 1991; 65: 2491–2500
   PubMed Web of Science ®Google Scholar
• Dietzen DJ, Hastings WR, Lublin DM. Caveolin is palmitoylated on multiple cysteine residues. J Biol Chem 1995; 270: 6838–6842
   PubMed Web of Science ®Google Scholar
• Veit M, Reverey H, Schmidt MF. Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins. Biochem J 1996; 318: 163–172
   PubMedGoogle Scholar
• Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS. Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure 2000; 8: 1137–1146
   PubMed Web of Science ®Google Scholar
• Biel M, Deck P, Giannis A, Waldmann H. Synthesis and evaluation of acyl protein thioesterase 1 (APT1) inhibitors. Chemistry 2006; 12: 4121–4143
   PubMedGoogle Scholar
• Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CCA, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RIS, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MRJ, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ESI, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NSW, McLaren S, Milne S, Mistry S, Moore MJF, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR. The DNA sequence and biological annotation of human chromosome 1. Nature 2006; 441: 315–321
   PubMed Web of Science ®Google Scholar
• Camp L, Hofmann S. Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. J Biol Chem 1993; 268: 22566–22574
   PubMed Web of Science ®Google Scholar
• Camp L, Verkruyse L, Afendis S, Slaughter C, Hofmann S. Molecular cloning and expression of palmitoyl-protein thioesterase. J Biol Chem 1994; 269: 23212–23219
   PubMedGoogle Scholar
• Verkruyse LA, Hofmann SL. Lysosomal targeting of palmitoyl-protein thioesterase. J Biol Chem 1996; 271: 15831–15836
   PubMed Web of Science ®Google Scholar
• Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature 1995; 376: 584–587
   PubMed Web of Science ®Google Scholar
• Lu JY, Verkruyse LA, Hofmann SL. Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc Natl Acad Sci USA 1996; 93: 10046–10050
   PubMed Web of Science ®Google Scholar
• Hellsten E, Vesa J, Olkkonen VM, Jalanko A, Peltonen L. Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis. Embo J 1996; 15: 5240–5245
   PubMed Web of Science ®Google Scholar
• Zhang Z, Lee Y-C, Kim S-J, Choi MS, Tsai P-C, Xu Y, Xiao Y-J, Zhang P, Heffer A, Mukherjee AB. Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in INCL. Hum Mol Genet 2006; 15: 337–346
   PubMed Web of Science ®Google Scholar
• Kim S-J, Zhang Z, Hitomi E, Lee Y-C, Mukherjee AB. Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL. Hum Mol Genet 2006; 15: 1826–1834
   PubMed Web of Science ®Google Scholar
• Kim S-J, Zhang Z, Lee Y-C, Mukherjee AB. Palmitoyl-protein thioesterase-1 deficiency leads to the activation of caspase-9 and contributes to rapid neurodegeneration in INCL. Hum Mol Genet 2006; 15: 1580–1586
   PubMed Web of Science ®Google Scholar
• Cho S, Dawson G. Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells. J Neurochem 2000; 74: 1478–1488
   PubMed Web of Science ®Google Scholar
• Cho S, Dawson PE, Dawson G. Antisense palmitoyl protein thioesterase 1 (PPT1) treatment inhibits PPT1 activity and increases cell death in LA-N-5 neuroblastoma cells. J Neurosci Res 2000; 62: 234–240
   PubMed Web of Science ®Google Scholar
• Bellizzi JJ 3rd, Widom J, Kemp C, Lu JY, Das AK, Hofmann SL, Clardy J. The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. Proc Natl Acad Sci USA 2000; 97: 4573–4578
   PubMed Web of Science ®Google Scholar
• Soyombo AA, Hofmann SL. Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity. J Biol Chem 1997; 272: 27456–27463
   PubMed Web of Science ®Google Scholar
• Calero G, Gupta P, Nonato MC, Tandel S, Biehl ER, Hofmann SL, Clardy J. The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2. J Biol Chem 2003; 278: 37957–37964
   PubMed Web of Science ®Google Scholar
• Gupta P, Soyombo AA, Atashband A, Wisniewski KE, Shelton JM, Richardson JA, Hammer RE, Hofmann SL. Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in knockout mice. Proc Natl Acad Sci USA 2001; 98: 13566–13571
   PubMed Web of Science ®Google Scholar
• Bannan BA, Van Etten J, Kohler JA, Tsoi Y, Hansen NM, Sigmon S, Fowler E, Buff H, Williams TS, Ault JG, Glaser RL, Korey CA. The Drosophila protein palmitoylome: characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases. Fly (Austin) 2008; 2: 1–17
   PubMedGoogle Scholar
• MacDonald ME, Ambrose CM, Duyao MP, Myers RH, Lin C, Srinidhi L, Barnes G, Taylor SA, James M, Groot N, MacFarlane H, Jenkins B, Anderson MA, Wexler NS, Gusella JF, Bates GP, Baxendale S, Hummerich H, Kirby S, North M, Youngman S, Mott R, Zehetner G, Sedlacek Z, Poustka A, Frischauf A-M, Lehrach H, Buckler AJ, Church D, Doucette-Stamm L, O'Donovan MC, Riba-Ramirez L, Shah M, Stanton VP, Strobel SA, Draths KM, Wales JL, Dervan P, Housman DE, Altherr M, Shiang R, Thompson L, Fielder T, Wasmuth JJ, Tagle D, Valdes J, Elmer L, Allard M, Castilla L, Swaroop M, Blanchard K, Collins FS, Snell R, Holloway T, Gillespie K, Datson N, Shaw D, Harper PS. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993; 72: 971–983
   PubMed Web of Science ®Google Scholar
• Karnoub AE, Weinberg RA. Ras oncogenes: split personalities. Nat Rev Mol Cell Biol 2008; 9: 517–531
   PubMed Web of Science ®Google Scholar
• Sousa SF, Fernandes PA, Ramos MJ. Farnesyltransferase inhibitors: a detailed chemical view on an elusive biological problem. Curr Med Chem 2008; 15: 1478–1492
   PubMed Web of Science ®Google Scholar
• Caron JM, Herwood M. Vinblastine, a chemotherapeutic drug, inhibits palmitoylation of tubulin in human leukemic lymphocytes. Chemotherapy 2007; 53: 51–58
   PubMedGoogle Scholar
• Wolff J, Zambito A, Britto P, Knipling L. Autopalmitoylation of tubulin. Protein Sci 2000; 9: 1357–1364
   PubMedGoogle Scholar
• Cantrell DA, Smith KA. The interleukin-2 T-cell system: a new cell growth model. Science 1984; 224: 1312–1316
   PubMed Web of Science ®Google Scholar