|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2009-2-17
|
|
pubmed:abstractText |
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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-10329400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-10564279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-10713171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-10888671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-10982406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-11101518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-11278313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-11786915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-12114505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15044687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15133481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-1555237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15603740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15705808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15893389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-15973437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16401723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16595649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16751107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16818716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16912714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-16959963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-17077383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-17183362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-17242068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-1740466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-18032660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-18378904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-18701706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-3322807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-6324873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-7597066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-7651165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-7835332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-8262238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-8641455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-9349529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-9487128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18980942-9891088
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0022-2275
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
50
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
398-404
|
|
pubmed:dateRevised |
2010-9-21
|
|
pubmed:meshHeading |
pubmed-meshheading:18980942-Brefeldin A,
pubmed-meshheading:18980942-Cell Membrane,
pubmed-meshheading:18980942-DNA, Complementary,
pubmed-meshheading:18980942-Endosomes,
pubmed-meshheading:18980942-Green Fluorescent Proteins,
pubmed-meshheading:18980942-Half-Life,
pubmed-meshheading:18980942-HeLa Cells,
pubmed-meshheading:18980942-Humans,
pubmed-meshheading:18980942-Lipoylation,
pubmed-meshheading:18980942-Microscopy, Confocal,
pubmed-meshheading:18980942-Multiprotein Complexes,
pubmed-meshheading:18980942-Mutagenesis, Site-Directed,
pubmed-meshheading:18980942-Qa-SNARE Proteins,
pubmed-meshheading:18980942-Recombinant Fusion Proteins,
pubmed-meshheading:18980942-Transfection
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8.
|
|
pubmed:affiliation |
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
