Timing of palmitoylation of influenza virus hemagglutinin

Veit, Michael; Schmidt, Michael F. G.

doi:10.1016/0014-5793(93)80812-9

Cited by 51 publications

(37 citation statements)

References 31 publications

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“…However, such a non-enzymatic reaction would not show any preference for the attachment of a particular fatty acid to a certain site but should rather reflect the concentration of individual acylCoAs at the intracellular site of acylation, the membranes of the late endoplasmic reticulum or early Golgi (19). Although very little is known about the distribution of acyl-CoAs in cellular membranes, there is no indication that the concentrations of Pal-CoA and Stear-CoA grossly differ in the endoplasmic reticulum/Golgi because both are also used for the synthesis of phospholipids that contain palmitate and stearate as the major type of fatty acids.…”

Section: Discussionmentioning

confidence: 99%

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Site-specific S-Acylation of Influenza Virus Hemagglutinin

Brett

Kordyukova

Serebryakova

et al. 2014

Journal of Biological Chemistry

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Background: S-Acylation of hemagglutinin with stearate and palmitate is essential for influenza virus replication. Results: Mass spectrometry showed that shifting a cysteine from the transmembrane region to a cytoplasmic position eliminates attachment of stearate. Conclusion:The location of the acylation site is the decisive factor for site-specific acylation. Significance: Similar differential acylation might occur in cellular transmembrane proteins.

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Section: Discussionmentioning

confidence: 99%

“…Most of the DHHC proteins are located in the endoplasmic reticulum or Golgi region where acylation of HA takes place (19). Alternatively, S-acylation of at least some proteins can occur by a non-enzymatic or autocatalytic mechanism (20,21).…”

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confidence: 99%

Site-specific S-Acylation of Influenza Virus Hemagglutinin

Brett

Kordyukova

Serebryakova

et al. 2014

Journal of Biological Chemistry

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“…The enzymes responsible for the acylation of viral glycoproteins have not been identified, but DHHC-CRD proteins are likely candidates since they were shown to palmitoylate cellular proteins (3). DHHC-CRD proteins are polytopic membrane proteins present at diverse intracellular locations, including the endoplasmic reticulum and the Golgi apparatus, the intracellular site where acylation of HA occurs (18). Since the DHHC-CRD family contains 23 members, it is likely that individual enzymes differ in their acyl-coenzyme A and substrate specificities.…”

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confidence: 99%

S Acylation of the Hemagglutinin of Influenza Viruses: Mass Spectrometry Reveals Site-Specific Attachment of Stearic Acid to a Transmembrane Cysteine

Kordyukova

Serebryakova

Baratova

et al. 2008

J Virol

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S acylation of cysteines located in the transmembrane and/or cytoplasmic region of influenza virus hemagglutinins (HA) contributes to the membrane fusion and assembly of virions. Our results from using mass spectrometry (MS) show that influenza B virus HA possessing two cytoplasmic cysteines contains palmitate, whereas HA-esterase-fusion glycoprotein of influenza C virus having one transmembrane cysteine is stearoylated. HAs of influenza A virus having one transmembrane and two cytoplasmic cysteines contain both palmitate and stearate. MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA.

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“…The palmitoylation of proteins known to be modified early in the secretory pathway is unaffected by BFA treatment (30)(31)(32). Similarly, syntaxin 8 might be modified in the ER or Golgi.…”

Section: Discussionmentioning

confidence: 99%

“…Viral glycoproteins and caveolin are examples of proteins that are stably palmitoylated, and no palmitate incorporation is detected in the absence of new protein synthesis (32,34). In contrast, many signaling proteins cycle between membrane compartments using an acylation/deacylation cycle that occurs on the time course of minutes (26).…”

Section: Discussionmentioning

confidence: 99%

Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8

Linder

2009

Journal of Lipid Research

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Palmitoylation is a posttranslational modification that regulates protein trafficking and stability. In this study we investigated whether the endosomal soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins syntaxin 7 and syntaxin 8 are modified with palmitate. Using metabolic labeling and sitedirected mutagenesis, we show that human syntaxins 7 and 8 are modified with palmitate through a thioester linkage. Palmitoylation is dependent upon cysteine 239 of human syntaxin 7 and cysteine 214 of syntaxin 8, residues that are located on the cytoplasmic face of the transmembrane domain (TMD). Palmitoylation of syntaxin 8 is minimally affected by the Golgi-disturbing agent brefeldin A (BFA), whereas BFA dramatically inhibits palmitoylation of syntaxin7. The differential effect of BFA suggests that palmitoylation of syntaxins 7 and 8 occurs in distinct subcellular compartments. Palmitoylation does not affect the rate of protein turnover of syntaxins 7 and 8 nor does it influence the steady-state localization of syntaxin 8 in late endosomes. Syntaxin 7 actively cycles between endosomes and the plasma membrane. Palmitoylation-defective syntaxin 7 is selectively retained on the plasma membrane, suggesting that palmitoylation is important for intercompartmental transport of syntaxin 7.-He, Y., and M. E. Linder. Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8. J. Lipid Res. 2009. 50: 398-404. Supplementary key words protein trafficking • fatty acylation • brefeldin A Palmitoylation refers to the posttranslational addition of palmitate to cysteine residues in proteins (1-3). Two features of palmitoylation distinguish it from other covalent lipid modifications that occur in the cytoplasm or on the cytoplasmic face of membranes. First, palmitoylation is reversible. Palmitate is added to proteins through a reversible thioester linkage, whereas myristate and prenyl groups are attached through stable amide and thioether linkages, respectively. Second, palmitoylation is a modification of both integral and peripheral membrane proteins, whereas Nmyristoylation and prenylation almost exclusively are modifications of proteins peripherally associated with membranes.A key function for lipid attachment to otherwise soluble proteins is to promote their interactions with membranes. Integral membrane proteins are permanently inserted into membranes by virtue of their transmembrane domains (TMDs). For many receptors and ion channels, palmitoylation of cytoplasmic tails creates additional sites of protein-membrane attachment (3). In other integral membrane proteins, however, the site of palmitoylation is often at one or more cysteine residues near the interface of the cytoplasm and the membrane. The functional consequences of palmitoylating integral membrane proteins are unclear; although evidence is emerging that palmitoylation may impact protein stability (4, 5).Several members of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) fami...

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Timing of palmitoylation of influenza virus hemagglutinin

Cited by 51 publications

References 31 publications

Site-specific S-Acylation of Influenza Virus Hemagglutinin

Site-specific S-Acylation of Influenza Virus Hemagglutinin

S Acylation of the Hemagglutinin of Influenza Viruses: Mass Spectrometry Reveals Site-Specific Attachment of Stearic Acid to a Transmembrane Cysteine

Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8

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