메뉴 건너뛰기




Volumn 180, Issue , 2014, Pages 44-52

Mechanistic effects of protein palmitoylation and the cellular consequences thereof

Author keywords

Acyl protein thioesterases; Acyl biotin exchange; DHHC enzymes; Palmitoylation; Radiolabeling

Indexed keywords

CYTOSOLIC ACYL PROTEIN THIOESTERASE; DHHC ENZYME; FAT; GLUCOSE; PROTEIN DEPALMITOYLATION INHIBITOR; PROTEIN INHIBITOR; PROTEIN PALMITOYLATION INHIBITOR; SUGAR; THIOL ESTER HYDROLASE; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84897987131     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2014.02.001     Document Type: Review
Times cited : (44)

References (126)
  • 1
    • 78649437379 scopus 로고    scopus 로고
    • Glucose stimulation of protein acylation in the pancreatic beta-cell
    • M. Abdel-Ghany, G.W. Sharp, and S.G. Straub Glucose stimulation of protein acylation in the pancreatic beta-cell Life Sci. 87 2010 667 671
    • (2010) Life Sci. , vol.87 , pp. 667-671
    • Abdel-Ghany, M.1    Sharp, G.W.2    Straub, S.G.3
  • 2
    • 44449107477 scopus 로고    scopus 로고
    • Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum
    • L. Abrami, B. Kunz, I. Iacovache, and F.G. van der Goot Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum Proc. Natl. Acad. Sci. U.S.A. 105 2008 5384 5389
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5384-5389
    • Abrami, L.1    Kunz, B.2    Iacovache, I.3    Van Der Goot, F.G.4
  • 3
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • L. Abrami, S.H. Leppla, and F.G. van der Goot Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis J. Cell. Biol. 172 2006 309 320
    • (2006) J. Cell. Biol. , vol.172 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    Van Der Goot, F.G.3
  • 6
    • 0025149021 scopus 로고
    • Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid
    • E. Alvarez, N. Girones, and R.J. Davis Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid J. Biol. Chem. 265 1990 16644 16655
    • (1990) J. Biol. Chem. , vol.265 , pp. 16644-16655
    • Alvarez, E.1    Girones, N.2    Davis, R.J.3
  • 9
    • 84880474167 scopus 로고    scopus 로고
    • Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid rafts
    • R. Bhattacharyya, C. Barren, and D.M. Kovacs Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid rafts J. Neurosci. 33 2013 11169 11183
    • (2013) J. Neurosci. , vol.33 , pp. 11169-11183
    • Bhattacharyya, R.1    Barren, C.2    Kovacs, D.M.3
  • 11
    • 84878758131 scopus 로고    scopus 로고
    • What does S-palmitoylation do to membrane proteins?
    • S. Blaskovic, M. Blanc, and F.G. van der Goot What does S-palmitoylation do to membrane proteins? FEBS J. 280 2013 2766 2774
    • (2013) FEBS J. , vol.280 , pp. 2766-2774
    • Blaskovic, S.1    Blanc, M.2    Van Der Goot, F.G.3
  • 12
    • 0000643086 scopus 로고    scopus 로고
    • Kinetics and mechanisms of reactions of thiol, thiono, and dithio analogues of carboxylic esters with nucleophiles
    • E.A. Castro Kinetics and mechanisms of reactions of thiol, thiono, and dithio analogues of carboxylic esters with nucleophiles Chem. Rev. 99 1999 3505 3524
    • (1999) Chem. Rev. , vol.99 , pp. 3505-3524
    • Castro, E.A.1
  • 13
    • 84887033963 scopus 로고    scopus 로고
    • MicroRNA-134 activity in somatostatin interneurons regulates H-Ras localization by repressing the palmitoylation enzyme, DHHC9
    • U.S.A
    • Chai, S., Cambronne, X.A., Eichhorn, S.W., Goodman, R.H., 2013. MicroRNA-134 activity in somatostatin interneurons regulates H-Ras localization by repressing the palmitoylation enzyme, DHHC9. Proc. Natl. Acad. Sci. U.S.A.
    • (2013) Proc. Natl. Acad. Sci
    • Chai, S.1    Cambronne, X.A.2    Eichhorn, S.W.3    Goodman, R.H.4
  • 14
    • 0142039784 scopus 로고    scopus 로고
    • Palmitoylation of the V2 vasopressin receptor carboxyl tail enhances beta-arrestin recruitment leading to efficient receptor endocytosis and ERK1/2 activation
    • P.G. Charest, and M. Bouvier Palmitoylation of the V2 vasopressin receptor carboxyl tail enhances beta-arrestin recruitment leading to efficient receptor endocytosis and ERK1/2 activation J. Biol. Chem. 278 2003 41541 41551
    • (2003) J. Biol. Chem. , vol.278 , pp. 41541-41551
    • Charest, P.G.1    Bouvier, M.2
  • 16
    • 78649734941 scopus 로고    scopus 로고
    • Palmitoylation and depalmitoylation dynamics at a glance
    • E. Conibear, and N.G. Davis Palmitoylation and depalmitoylation dynamics at a glance J. Cell. Sci. 123 2010 4007 4010
    • (2010) J. Cell. Sci. , vol.123 , pp. 4007-4010
    • Conibear, E.1    Davis, N.G.2
  • 18
    • 77951729960 scopus 로고    scopus 로고
    • Palmitoylation of oncogenic NRAS is essential for leukemogenesis
    • B. Cuiffo, and R. Ren Palmitoylation of oncogenic NRAS is essential for leukemogenesis Blood 115 2010 3598 3605
    • (2010) Blood , vol.115 , pp. 3598-3605
    • Cuiffo, B.1    Ren, R.2
  • 19
    • 0035501459 scopus 로고    scopus 로고
    • Cellular pharmacology of cerulenin analogs that inhibit protein palmitoylation
    • M.L. De Vos, D.S. Lawrence, and C.D. Smith Cellular pharmacology of cerulenin analogs that inhibit protein palmitoylation Biochem. Pharmacol. 62 2001 985 995
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 985-995
    • De Vos, M.L.1    Lawrence, D.S.2    Smith, C.D.3
  • 20
    • 0027504955 scopus 로고
    • Novel use of an iodo-myristyl-coa analog identifies a semialdehyde dehydrogenase in bovine liver
    • I. Deichaite, L. Berthiaume, S.M. Peseckis, W.F. Patton, and M.D. Resh Novel use of an iodo-myristyl-coa analog identifies a semialdehyde dehydrogenase in bovine liver J. Biol. Chem. 268 1993 13738 13747
    • (1993) J. Biol. Chem. , vol.268 , pp. 13738-13747
    • Deichaite, I.1    Berthiaume, L.2    Peseckis, S.M.3    Patton, W.F.4    Resh, M.D.5
  • 22
    • 0034435875 scopus 로고    scopus 로고
    • Crystal structure of the human acyl protein thioesterase i from a single X-ray data set to 1.5 A
    • Y. Devedjiev, Z. Dauter, S.R. Kuznetsov, T.L. Jones, and Z.S. Derewenda Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A Structure 8 2000 1137 1146
    • (2000) Structure , vol.8 , pp. 1137-1146
    • Devedjiev, Y.1    Dauter, Z.2    Kuznetsov, S.R.3    Jones, T.L.4    Derewenda, Z.S.5
  • 23
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • D.J. Dietzen, W.R. Hastings, and D.M. Lublin Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae J. Biol. Chem. 270 1995 6838 6842
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 24
    • 77950199320 scopus 로고    scopus 로고
    • DHHC20: A human palmitoyl acyltransferase that causes cellular transformation
    • J.M. Draper, and C.D. Smith DHHC20: a human palmitoyl acyltransferase that causes cellular transformation Mol. Membr. Biol. 27 2010 123 136
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 123-136
    • Draper, J.M.1    Smith, C.D.2
  • 25
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • R.C. Drisdel, and W.N. Green Labeling and quantifying sites of protein palmitoylation Biotechniques 36 2004 276 285
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 27
    • 0032546946 scopus 로고    scopus 로고
    • A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS)
    • J.A. Duncan, and A.G. Gilman A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS) J. Biol. Chem. 273 1998 15830 15837
    • (1998) J. Biol. Chem. , vol.273 , pp. 15830-15837
    • Duncan, J.A.1    Gilman, A.G.2
  • 29
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • A.E. El-Husseini, S.E. Craven, D.M. Chetkovich, B.L. Firestein, E. Schnell, C. Aoki, and D.S. Bredt Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering J. Cell. Biol. 148 2000 159 172
    • (2000) J. Cell. Biol. , vol.148 , pp. 159-172
    • El-Husseini, A.E.1    Craven, S.E.2    Chetkovich, D.M.3    Firestein, B.L.4    Schnell, E.5    Aoki, C.6    Bredt, D.S.7
  • 31
    • 26844473519 scopus 로고    scopus 로고
    • Lipid-modified proteins as biomarkers for cardiovascular disease: A review
    • N. Ferri, R. Paoletti, and A. Corsini Lipid-modified proteins as biomarkers for cardiovascular disease: a review Biomarkers 10 2005 219 237
    • (2005) Biomarkers , vol.10 , pp. 219-237
    • Ferri, N.1    Paoletti, R.2    Corsini, A.3
  • 34
    • 79953132315 scopus 로고    scopus 로고
    • Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation
    • J.D. Foster, and R.A. Vaughan Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation J. Biol. Chem. 286 2011 5175 5186
    • (2011) J. Biol. Chem. , vol.286 , pp. 5175-5186
    • Foster, J.D.1    Vaughan, R.A.2
  • 38
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Y. Fukata, and M. Fukata Protein palmitoylation in neuronal development and synaptic plasticity Nat. Rev. Neurosci. 11 2010 161 175
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 39
    • 33748958810 scopus 로고    scopus 로고
    • Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells
    • Y. Fukata, T. Iwanaga, and M. Fukata Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells Methods 40 2006 177 182
    • (2006) Methods , vol.40 , pp. 177-182
    • Fukata, Y.1    Iwanaga, T.2    Fukata, M.3
  • 40
    • 84890978108 scopus 로고    scopus 로고
    • Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine
    • X. Gao, and R.N. Hannoush Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine Nat. Chem. Biol. 10 2014 61 68
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 61-68
    • Gao, X.1    Hannoush, R.N.2
  • 42
    • 64249172320 scopus 로고    scopus 로고
    • A novel motif at the C-terminus of palmitoyltransferases is essential for Swf1 and Pfa3 function in vivo
    • A. Gonzalez Montoro, R. Quiroga, H.J. Maccioni, and J. Valdez Taubas A novel motif at the C-terminus of palmitoyltransferases is essential for Swf1 and Pfa3 function in vivo Biochem. J. 419 2009 301 308
    • (2009) Biochem. J. , vol.419 , pp. 301-308
    • Gonzalez Montoro, A.1    Quiroga, R.2    Maccioni, H.J.3    Valdez Taubas, J.4
  • 43
    • 84883354970 scopus 로고    scopus 로고
    • Zinc co-ordination by the DHHC cysteine-rich domain of the palmitoyltransferase Swf1
    • A. Gonzalez Montoro, R. Quiroga, and J. Valdez Taubas Zinc co-ordination by the DHHC cysteine-rich domain of the palmitoyltransferase Swf1 Biochem. J. 454 2013 427 435
    • (2013) Biochem. J. , vol.454 , pp. 427-435
    • Gonzalez Montoro, A.1    Quiroga, R.2    Valdez Taubas, J.3
  • 44
    • 80655128141 scopus 로고    scopus 로고
    • Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals
    • O.A. Gorleku, A.M. Barns, G.R. Prescott, J. Greaves, and L.H. Chamberlain Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals J. Biol. Chem. 286 2011 39573 39584
    • (2011) J. Biol. Chem. , vol.286 , pp. 39573-39584
    • Gorleku, O.A.1    Barns, A.M.2    Prescott, G.R.3    Greaves, J.4    Chamberlain, L.H.5
  • 45
    • 69249216587 scopus 로고    scopus 로고
    • Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence
    • M.L. Grantham, W.H. Wu, E.N. Lalime, M.E. Lorenzo, S.L. Klein, and A. Pekosz Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence J. Virol. 83 2009 8655 8661
    • (2009) J. Virol. , vol.83 , pp. 8655-8661
    • Grantham, M.L.1    Wu, W.H.2    Lalime, E.N.3    Lorenzo, M.E.4    Klein, S.L.5    Pekosz, A.6
  • 46
    • 79955649200 scopus 로고    scopus 로고
    • DHHC palmitoyl transferases: Substrate interactions and (patho)physiology
    • J. Greaves, and L.H. Chamberlain DHHC palmitoyl transferases: substrate interactions and (patho)physiology Trends Biochem. Sci. 36 2011 245 253
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 245-253
    • Greaves, J.1    Chamberlain, L.H.2
  • 47
    • 79953143263 scopus 로고    scopus 로고
    • Differential palmitoylation regulates intracellular patterning of SNAP25
    • J. Greaves, and L.H. Chamberlain Differential palmitoylation regulates intracellular patterning of SNAP25 J. Cell. Sci. 124 2011 1351 1360
    • (2011) J. Cell. Sci. , vol.124 , pp. 1351-1360
    • Greaves, J.1    Chamberlain, L.H.2
  • 48
    • 77955293805 scopus 로고    scopus 로고
    • Palmitoylation of the SNAP25 protein family: Specificity and regulation by DHHC palmitoyl transferases
    • J. Greaves, O.A. Gorleku, C. Salaun, and L.H. Chamberlain Palmitoylation of the SNAP25 protein family: specificity and regulation by DHHC palmitoyl transferases J. Biol. Chem. 285 2010 24629 24638
    • (2010) J. Biol. Chem. , vol.285 , pp. 24629-24638
    • Greaves, J.1    Gorleku, O.A.2    Salaun, C.3    Chamberlain, L.H.4
  • 49
    • 65649108966 scopus 로고    scopus 로고
    • The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases
    • J. Greaves, G.R. Prescott, Y. Fukata, M. Fukata, C. Salaun, and L.H. Chamberlain The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases Mol. Biol. Cell 20 2009 1845 1854
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1845-1854
    • Greaves, J.1    Prescott, G.R.2    Fukata, Y.3    Fukata, M.4    Salaun, C.5    Chamberlain, L.H.6
  • 50
    • 84876936164 scopus 로고    scopus 로고
    • Characterization of palmitoylation of ATP binding cassette transporter G1: Effect on protein trafficking and function
    • H.M. Gu, G. Li, X. Gao, L.G. Berthiaume, and D.W. Zhang Characterization of palmitoylation of ATP binding cassette transporter G1: effect on protein trafficking and function Biochim. Biophys. Acta 1831 2013 1067 1078
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 1067-1078
    • Gu, H.M.1    Li, G.2    Gao, X.3    Berthiaume, L.G.4    Zhang, D.W.5
  • 51
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 52
    • 80052372651 scopus 로고    scopus 로고
    • Neurotensin receptor-1 inducible palmitoylation is required for efficient receptor-mediated mitogenic-signaling within structured membrane microdomains
    • Y. Heakal, M.P. Woll, T. Fox, K. Seaton, R. Levenson, and M. Kester Neurotensin receptor-1 inducible palmitoylation is required for efficient receptor-mediated mitogenic-signaling within structured membrane microdomains Cancer Biol. Ther. 12 2011 427 435
    • (2011) Cancer Biol. Ther. , vol.12 , pp. 427-435
    • Heakal, Y.1    Woll, M.P.2    Fox, T.3    Seaton, K.4    Levenson, R.5    Kester, M.6
  • 54
    • 84888372471 scopus 로고    scopus 로고
    • Massive endocytosis triggered by surface membrane palmitoylation under mitochondrial control in BHK fibroblasts
    • D.W. Hilgemann, M. Fine, M.E. Linder, B.C. Jennings, and M.J. Lin Massive endocytosis triggered by surface membrane palmitoylation under mitochondrial control in BHK fibroblasts eLife 2 2013
    • (2013) ELife , vol.2
    • Hilgemann, D.W.1    Fine, M.2    Linder, M.E.3    Jennings, B.C.4    Lin, M.J.5
  • 56
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • J. Huotari, and A. Helenius Endosome maturation EMBO J. 30 2011 3481 3500
    • (2011) EMBO J. , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 58
    • 84857737571 scopus 로고    scopus 로고
    • DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities
    • B.C. Jennings, and M.E. Linder DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities J. Biol. Chem. 287 2012 7236 7245
    • (2012) J. Biol. Chem. , vol.287 , pp. 7236-7245
    • Jennings, B.C.1    Linder, M.E.2
  • 59
    • 64749106134 scopus 로고    scopus 로고
    • 2-Bromopalmitate and 2-(2-hydroxy-5-nitro-benzylidene)-benzo[b]thiophen- 3-one inhibit DHHC-mediated palmitoylation in vitro
    • B.C. Jennings, M.J. Nadolski, Y. Ling, M.B. Baker, M.L. Harrison, R.J. Deschenes, and M.E. Linder 2-Bromopalmitate and 2-(2-hydroxy-5-nitro- benzylidene)-benzo[b]thiophen-3-one inhibit DHHC-mediated palmitoylation in vitro J. Lipid Res. 50 2009 233 242
    • (2009) J. Lipid Res. , vol.50 , pp. 233-242
    • Jennings, B.C.1    Nadolski, M.J.2    Ling, Y.3    Baker, M.B.4    Harrison, M.L.5    Deschenes, R.J.6    Linder, M.E.7
  • 61
    • 84887563272 scopus 로고    scopus 로고
    • DJ-1 Associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes
    • K.S. Kim, J.S. Kim, J.Y. Park, Y.H. Suh, I. Jou, E.H. Joe, and S.M. Park DJ-1 Associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes Hum. Mol. Genet. 2013
    • (2013) Hum. Mol. Genet.
    • Kim, K.S.1    Kim, J.S.2    Park, J.Y.3    Suh, Y.H.4    Jou, I.5    Joe, E.H.6    Park, S.M.7
  • 62
    • 84875972777 scopus 로고    scopus 로고
    • Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene H-ras product and growth-associated protein-43
    • E. Kong, S. Peng, G. Chandra, C. Sarkar, Z. Zhang, M.B. Bagh, and A.B. Mukherjee Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene H-ras product and growth-associated protein-43 J. Biol. Chem. 288 2013 9112 9125
    • (2013) J. Biol. Chem. , vol.288 , pp. 9112-9125
    • Kong, E.1    Peng, S.2    Chandra, G.3    Sarkar, C.4    Zhang, Z.5    Bagh, M.B.6    Mukherjee, A.B.7
  • 63
    • 79951576355 scopus 로고    scopus 로고
    • The role of palmitoylation in directing dopamine D1 receptor internalization through selective endocytic routes
    • M.M. Kong, V. Verma, B.F. O'Dowd, and S.R. George The role of palmitoylation in directing dopamine D1 receptor internalization through selective endocytic routes Biochem. Biophys. Res. Commun. 405 2011 445 449
    • (2011) Biochem. Biophys. Res. Commun. , vol.405 , pp. 445-449
    • Kong, M.M.1    Verma, V.2    O'Dowd, B.F.3    George, S.R.4
  • 64
    • 84880482155 scopus 로고    scopus 로고
    • Lectin-like oxidized LDL receptor-1 is palmitoylated and internalizes ligands via caveolae/raft-dependent endocytosis
    • M. Kumano-Kuramochi, Q. Xie, S. Kajiwara, S. Komba, T. Minowa, and S. Machida Lectin-like oxidized LDL receptor-1 is palmitoylated and internalizes ligands via caveolae/raft-dependent endocytosis Biochem. Biophys. Res. Commun. 434 2013 594 599
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 594-599
    • Kumano-Kuramochi, M.1    Xie, Q.2    Kajiwara, S.3    Komba, S.4    Minowa, T.5    Machida, S.6
  • 65
    • 84860320810 scopus 로고    scopus 로고
    • Palmitoylation regulates 17beta-estradiol-induced estrogen receptor-alpha degradation and transcriptional activity
    • P. La Rosa, V. Pesiri, G. Leclercq, M. Marino, and F. Acconcia Palmitoylation regulates 17beta-estradiol-induced estrogen receptor-alpha degradation and transcriptional activity Mol. Endocrinol. 26 2012 762 774
    • (2012) Mol. Endocrinol. , vol.26 , pp. 762-774
    • La Rosa, P.1    Pesiri, V.2    Leclercq, G.3    Marino, M.4    Acconcia, F.5
  • 66
    • 84881230382 scopus 로고    scopus 로고
    • Oligomerization of DHHC protein s-acyltransferases
    • Lai, J., Linder, M.E., 2013. Oligomerization of DHHC Protein S-Acyltransferases. J. Biol. Chem.
    • (2013) J. Biol. Chem
    • Lai, J.1    Linder, M.E.2
  • 70
    • 84888320142 scopus 로고    scopus 로고
    • Massive palmitoylation-dependent endocytosis during reoxygenation of anoxic cardiac muscle
    • M.J. Lin, M. Fine, J.Y. Lu, S.L. Hofmann, G. Frazier, and D.W. Hilgemann Massive palmitoylation-dependent endocytosis during reoxygenation of anoxic cardiac muscle eLife 2013 2
    • (2013) ELife , pp. 2
    • Lin, M.J.1    Fine, M.2    Lu, J.Y.3    Hofmann, S.L.4    Frazier, G.5    Hilgemann, D.W.6
  • 71
    • 84878564038 scopus 로고    scopus 로고
    • Membrane-bound RLCKs LIP1 and LIP2 are essential male factors controlling male-female attraction in Arabidopsis
    • J. Liu, S. Zhong, X. Guo, L. Hao, X. Wei, Q. Huang, Y. Hou, J. Shi, C. Wang, H. Gu, and L.J. Qu Membrane-bound RLCKs LIP1 and LIP2 are essential male factors controlling male-female attraction in Arabidopsis Curr. Biol. 23 2013 993 998
    • (2013) Curr. Biol. , vol.23 , pp. 993-998
    • Liu, J.1    Zhong, S.2    Guo, X.3    Hao, L.4    Wei, X.5    Huang, Q.6    Hou, Y.7    Shi, J.8    Wang, C.9    Gu, H.10    Qu, L.J.11
  • 72
    • 84864978744 scopus 로고    scopus 로고
    • Palmitoylation regulates intracellular trafficking of beta2 adrenergic receptor/arrestin/phosphodiesterase 4D complexes in cardiomyocytes
    • R. Liu, D. Wang, Q. Shi, Q. Fu, S. Hizon, and Y.K. Xiang Palmitoylation regulates intracellular trafficking of beta2 adrenergic receptor/arrestin/ phosphodiesterase 4D complexes in cardiomyocytes PLoS One 7 2012 e42658
    • (2012) PLoS One , vol.7 , pp. 42658
    • Liu, R.1    Wang, D.2    Shi, Q.3    Fu, Q.4    Hizon, S.5    Xiang, Y.K.6
  • 73
    • 0024261849 scopus 로고
    • Fatty acid acylation at the single cysteine residue in the cytoplasmic domain of the glycoprotein of vesicular-stomatitis virus
    • D. Mack, and J. Kruppa Fatty acid acylation at the single cysteine residue in the cytoplasmic domain of the glycoprotein of vesicular-stomatitis virus Biochem. J. 256 1988 1021 1027
    • (1988) Biochem. J. , vol.256 , pp. 1021-1027
    • Mack, D.1    Kruppa, J.2
  • 76
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • B.R. Martin, and B.F. Cravatt Large-scale profiling of protein palmitoylation in mammalian cells Nat. Meth. 6 2009 135 138
    • (2009) Nat. Meth. , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 80
    • 84867267220 scopus 로고    scopus 로고
    • The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate
    • D.A. Mitchell, L.D. Hamel, K. Ishizuka, G. Mitchell, L.M. Schaefer, and R.J. Deschenes The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate J. Biol. Chem. 287 2012 34337 34348
    • (2012) J. Biol. Chem. , vol.287 , pp. 34337-34348
    • Mitchell, D.A.1    Hamel, L.D.2    Ishizuka, K.3    Mitchell, G.4    Schaefer, L.M.5    Deschenes, R.J.6
  • 82
    • 84870478193 scopus 로고    scopus 로고
    • Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
    • Y. Ohno, A. Kashio, R. Ogata, A. Ishitomi, Y. Yamazaki, and A. Kihara Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system Mol. Biol. Cell. 23 2012 4543 4551
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 4543-4551
    • Ohno, Y.1    Kashio, A.2    Ogata, R.3    Ishitomi, A.4    Yamazaki, Y.5    Kihara, A.6
  • 83
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • Y. Ohno, A. Kihara, T. Sano, and Y. Igarashi Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins Biochim. Biophys. Acta 1761 2006 474 483
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 84
    • 84880770109 scopus 로고    scopus 로고
    • The LIM domain only 4 protein is a metabolic responsive inhibitor of protein tyrosine phosphatase 1B that controls hypothalamic leptin signaling
    • N.R. Pandey, X. Zhou, Z. Qin, T. Zaman, M. Gomez-Smith, K. Keyhanian, H. Anisman, J.M. Brunel, A.F. Stewart, and H.H. Chen The LIM domain only 4 protein is a metabolic responsive inhibitor of protein tyrosine phosphatase 1B that controls hypothalamic leptin signaling J. Neurosci. 33 2013 12647 12655
    • (2013) J. Neurosci. , vol.33 , pp. 12647-12655
    • Pandey, N.R.1    Zhou, X.2    Qin, Z.3    Zaman, T.4    Gomez-Smith, M.5    Keyhanian, K.6    Anisman, H.7    Brunel, J.M.8    Stewart, A.F.9    Chen, H.H.10
  • 85
    • 0028123665 scopus 로고
    • Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension
    • S.I. Patterson, and J.H. Skene Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension J. Cell. Biol. 124 1994 521 536
    • (1994) J. Cell. Biol. , vol.124 , pp. 521-536
    • Patterson, S.I.1    Skene, J.H.2
  • 86
    • 84884855140 scopus 로고    scopus 로고
    • 2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities
    • M.P. Pedro, A.A. Vilcaes, V.M. Tomatis, R.G. Oliveira, G.A. Gomez, and J.L. Daniotti 2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities PLoS One 8 2013 e75232
    • (2013) PLoS One , vol.8 , pp. 75232
    • Pedro, M.P.1    Vilcaes, A.A.2    Tomatis, V.M.3    Oliveira, R.G.4    Gomez, G.A.5    Daniotti, J.L.6
  • 88
    • 0033012819 scopus 로고    scopus 로고
    • The DHHC domain: A new highly conserved cysteine-rich motif
    • T. Putilina, P. Wong, and S. Gentleman The DHHC domain: a new highly conserved cysteine-rich motif Mol. Cell. Biochem. 195 1999 219 226
    • (1999) Mol. Cell. Biochem. , vol.195 , pp. 219-226
    • Putilina, T.1    Wong, P.2    Gentleman, S.3
  • 89
    • 84877799575 scopus 로고    scopus 로고
    • Proteomic analysis of protein palmitoylation in adipocytes
    • W. Ren, U.S. Jhala, and K. Du Proteomic analysis of protein palmitoylation in adipocytes Adipocyte 2 2013 17 28
    • (2013) Adipocyte , vol.2 , pp. 17-28
    • Ren, W.1    Jhala, U.S.2    Du, K.3
  • 90
    • 84886914670 scopus 로고    scopus 로고
    • DHHC17 Palmitoylates ClipR-59 and Modulates ClipR-59 association with the plasma membrane
    • W. Ren, Y. Sun, and K. Du DHHC17 Palmitoylates ClipR-59 and Modulates ClipR-59 association with the plasma membrane Mol. Cell. Biol. 33 2013 4255 4265
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 4255-4265
    • Ren, W.1    Sun, Y.2    Du, K.3
  • 91
    • 62749084512 scopus 로고    scopus 로고
    • Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling
    • 182 p following 192
    • A. Rossin, M. Derouet, F. Abdel-Sater, and A.O. Hueber Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling Biochem. J. 419 2009 185 192 182 p following 192
    • (2009) Biochem. J. , vol.419 , pp. 185-192
    • Rossin, A.1    Derouet, M.2    Abdel-Sater, F.3    Hueber, A.O.4
  • 94
    • 78650718836 scopus 로고    scopus 로고
    • The intracellular dynamic of protein palmitoylation
    • C. Salaun, J. Greaves, and L.H. Chamberlain The intracellular dynamic of protein palmitoylation J. Cell. Biol. 191 2010 1229 1238
    • (2010) J. Cell. Biol. , vol.191 , pp. 1229-1238
    • Salaun, C.1    Greaves, J.2    Chamberlain, L.H.3
  • 99
    • 70350448399 scopus 로고    scopus 로고
    • Distinct domains within PSD-95 mediate synaptic incorporation, stabilization, and activity-dependent trafficking
    • J.F. Sturgill, P. Steiner, B.L. Czervionke, and B.L. Sabatini Distinct domains within PSD-95 mediate synaptic incorporation, stabilization, and activity-dependent trafficking J. Neurosci. 29 2009 12845 12854
    • (2009) J. Neurosci. , vol.29 , pp. 12845-12854
    • Sturgill, J.F.1    Steiner, P.2    Czervionke, B.L.3    Sabatini, B.L.4
  • 102
    • 84885385698 scopus 로고    scopus 로고
    • Smarter neuronal signaling complexes from existing components: How regulatory modifications were acquired during animal evolution: Evolution of palmitoylation-dependent regulation of AMPA-type ionotropic glutamate receptors
    • G.M. Thomas, and T. Hayashi Smarter neuronal signaling complexes from existing components: How regulatory modifications were acquired during animal evolution: Evolution of palmitoylation-dependent regulation of AMPA-type ionotropic glutamate receptors Bioessays 35 2013 929 939
    • (2013) Bioessays , vol.35 , pp. 929-939
    • Thomas, G.M.1    Hayashi, T.2
  • 103
    • 84863012668 scopus 로고    scopus 로고
    • Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking
    • G.M. Thomas, T. Hayashi, S.L. Chiu, C.M. Chen, and R.L. Huganir Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking Neuron 73 2012 482 496
    • (2012) Neuron , vol.73 , pp. 482-496
    • Thomas, G.M.1    Hayashi, T.2    Chiu, S.L.3    Chen, C.M.4    Huganir, R.L.5
  • 104
    • 84884547415 scopus 로고    scopus 로고
    • DHHC8-Dependent PICK1 palmitoylation is required for induction of cerebellar long-term synaptic depression
    • G.M. Thomas, T. Hayashi, R.L. Huganir, and D.J. Linden DHHC8-Dependent PICK1 palmitoylation is required for induction of cerebellar long-term synaptic depression J. Neurosci. 33 2013 15401 15407
    • (2013) J. Neurosci. , vol.33 , pp. 15401-15407
    • Thomas, G.M.1    Hayashi, T.2    Huganir, R.L.3    Linden, D.J.4
  • 105
    • 77954900572 scopus 로고    scopus 로고
    • Multiple palmitoyltransferases are required for palmitoylation-dependent regulation of large conductance calcium- and voltage-activated potassium channels
    • L. Tian, H. McClafferty, O. Jeffries, and M.J. Shipston Multiple palmitoyltransferases are required for palmitoylation-dependent regulation of large conductance calcium- and voltage-activated potassium channels J. Biol. Chem. 285 2010 23954 23962
    • (2010) J. Biol. Chem. , vol.285 , pp. 23954-23962
    • Tian, L.1    McClafferty, H.2    Jeffries, O.3    Shipston, M.J.4
  • 106
    • 78649789580 scopus 로고    scopus 로고
    • Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43
    • V.M. Tomatis, A. Trenchi, G.A. Gomez, and J.L. Daniotti Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43 PLoS One 5 2010 e15045
    • (2010) PLoS One , vol.5 , pp. 15045
    • Tomatis, V.M.1    Trenchi, A.2    Gomez, G.A.3    Daniotti, J.L.4
  • 107
    • 50049114778 scopus 로고    scopus 로고
    • Discovery of protein-palmitoylating enzymes
    • R. Tsutsumi, Y. Fukata, and M. Fukata Discovery of protein-palmitoylating enzymes Pflugers Arch. 456 2008 1199 1206
    • (2008) Pflugers Arch. , vol.456 , pp. 1199-1206
    • Tsutsumi, R.1    Fukata, Y.2    Fukata, M.3
  • 111
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: Purification and identification
    • J. Wan, A.F. Roth, A.O. Bailey, and N.G. Davis Palmitoylated proteins: purification and identification Nat. Protoc. 2 2007 1573 1584
    • (2007) Nat. Protoc. , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 112
    • 84888156005 scopus 로고    scopus 로고
    • SCG10 promotes non-amyloidogenic processing of amyloid precursor protein by facilitating its trafficking to the cell surface
    • Wang, J., Shan, C., Cao, W., Zhang, C., Teng, J., Chen, J., 2013. SCG10 promotes non-amyloidogenic processing of amyloid precursor protein by facilitating its trafficking to the cell surface. Hum. Mol. Genet.
    • (2013) Hum. Mol. Genet
    • Wang, J.1    Shan, C.2    Cao, W.3    Zhang, C.4    Teng, J.5    Chen, J.6
  • 113
    • 0028250743 scopus 로고
    • Fluorography of polyacrylamide gels containing tritium
    • J.H. Waterborg, and H.R. Matthews Fluorography of polyacrylamide gels containing tritium Methods Mol. Biol. 32 1994 163 167
    • (1994) Methods Mol. Biol. , vol.32 , pp. 163-167
    • Waterborg, J.H.1    Matthews, H.R.2
  • 114
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • Y. Webb, L. Hermida-Matsumoto, and M.D. Resh Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids J. Biol. Chem. 275 2000 261 270
    • (2000) J. Biol. Chem. , vol.275 , pp. 261-270
    • Webb, Y.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 115
    • 0028173706 scopus 로고
    • Activation and depalmitoylation of Gs alpha
    • P.B. Wedegaertner, and H.R. Bourne Activation and depalmitoylation of Gs alpha Cell 77 1994 1063 1070
    • (1994) Cell , vol.77 , pp. 1063-1070
    • Wedegaertner, P.B.1    Bourne, H.R.2
  • 117
    • 84863011676 scopus 로고    scopus 로고
    • Inhibiting the palmitoylation/depalmitoylation cycle selectively reduces the growth of hematopoietic cells expressing oncogenic Nras
    • J. Xu, C. Hedberg, F.J. Dekker, Q. Li, K.M. Haigis, E. Hwang, H. Waldmann, and K. Shannon Inhibiting the palmitoylation/depalmitoylation cycle selectively reduces the growth of hematopoietic cells expressing oncogenic Nras Blood 119 2012 1032 1035
    • (2012) Blood , vol.119 , pp. 1032-1035
    • Xu, J.1    Hedberg, C.2    Dekker, F.J.3    Li, Q.4    Haigis, K.M.5    Hwang, E.6    Waldmann, H.7    Shannon, K.8
  • 120
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • W. Yang, D. Di Vizio, M. Kirchner, H. Steen, and M.R. Freeman Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes Mol. Cell. Proteomics 9 2010 54 70
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 121
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • X. Yang, O.V. Kovalenko, W. Tang, C. Claas, C.S. Stipp, and M.E. Hemler Palmitoylation supports assembly and function of integrin-tetraspanin complexes J. Cell. Biol. 167 2004 1231 1240
    • (2004) J. Cell. Biol. , vol.167 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 124
    • 84880959257 scopus 로고    scopus 로고
    • Quantitative control of protein s-palmitoylation regulates meiotic entry in fission yeast
    • M.M. Zhang, P.Y. Wu, F.D. Kelly, P. Nurse, and H.C. Hang Quantitative control of protein s-palmitoylation regulates meiotic entry in fission yeast PLoS Biol. 11 2013 e1001597
    • (2013) PLoS Biol. , vol.11 , pp. 1001597
    • Zhang, M.M.1    Wu, P.Y.2    Kelly, F.D.3    Nurse, P.4    Hang, H.C.5
  • 125
    • 0034002307 scopus 로고    scopus 로고
    • Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides
    • Y. Zhao, J.B. McCabe, J. Vance, and L.G. Berthiaume Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides Mol. Biol. Cell. 11 2000 721 734
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 721-734
    • Zhao, Y.1    McCabe, J.B.2    Vance, J.3    Berthiaume, L.G.4
  • 126
    • 5644243063 scopus 로고    scopus 로고
    • The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility- and invasiveness-inhibitory activity
    • B. Zhou, L. Liu, M. Reddivari, and X.A. Zhang The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility- and invasiveness-inhibitory activity Cancer Res. 64 2004 7455 7463
    • (2004) Cancer Res. , vol.64 , pp. 7455-7463
    • Zhou, B.1    Liu, L.2    Reddivari, M.3    Zhang, X.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.