Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S]
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. Usin...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2009-03-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S002222752030883X |
| _version_ | 1819077249919352832 |
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| author | Yuhong He Maurine E. Linder |
| author_facet | Yuhong He Maurine E. Linder |
| author_sort | Yuhong He |
| collection | DOAJ |
| description | 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 site-directed 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. |
| first_indexed | 2024-12-21T18:54:12Z |
| format | Article |
| id | doaj.art-bc0ddddb71f54ec08f445e217538fb75 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-21T18:54:12Z |
| publishDate | 2009-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-bc0ddddb71f54ec08f445e217538fb752022-12-21T18:53:40ZengElsevierJournal of Lipid Research0022-22752009-03-01503398404Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S]Yuhong He0Maurine E. Linder1Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110Palmitoylation 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 site-directed 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.http://www.sciencedirect.com/science/article/pii/S002222752030883Xprotein traffickingfatty acylationbrefeldin A |
| spellingShingle | Yuhong He Maurine E. Linder Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] Journal of Lipid Research protein trafficking fatty acylation brefeldin A |
| title | Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] |
| title_full | Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] |
| title_fullStr | Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] |
| title_full_unstemmed | Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] |
| title_short | Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8*[S] |
| title_sort | differential palmitoylation of the endosomal snares syntaxin 7 and syntaxin 8 s |
| topic | protein trafficking fatty acylation brefeldin A |
| url | http://www.sciencedirect.com/science/article/pii/S002222752030883X |
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