| pubmed-article:19170188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C0027836 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C0300824 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C1419206 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C1420271 | lld:lifeskim |
| pubmed-article:19170188 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:19170188 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:19170188 | pubmed:dateCreated | 2009-10-12 | lld:pubmed |
| pubmed-article:19170188 | pubmed:abstractText | During myelin formation, vast amounts of specialized membrane proteins and lipids are trafficked toward the growing sheath in cell surface-directed transport vesicles. Soluble N-ethylmaleimide-sensitive factor (NSF) attachment proteins (SNAPs) are important components of molecular complexes required for membrane fusion. We have analyzed the expression profile and molecular interactions of SNAP-29 in the nervous system. In addition to its known enrichment in neuronal synapses, SNAP-29 is abundant in oligodendrocytes during myelination and in noncompact myelin of the peripheral nervous system. By yeast two-hybrid screen and coimmunoprecipitation, we found that the GTPases Rab3A, Rab24, and septin 4 bind to the N-terminal domain of SNAP-29. The interaction with Rab24 or septin 4 was GTP independent. In contrast, interaction between SNAP-29 and Rab3A was GTP dependent, and colocalization was extensive both in synapses and in myelinating glia. In HEK293 cells, cytoplasmic SNAP-29 pools were redistributed upon coexpression with Rab3A, and surface-directed trafficking of myelin proteolipid protein was enhanced by overexpression of SNAP-29 and Rab3A. Interestingly, the abundance of SNAP-29 in sciatic nerves was increased during remyelination and in a rat model of Charcot-Marie-Tooth disease, two pathological situations with increased myelin membrane biogenesis. We suggest that Rab3A may regulate SNAP-29-mediated membrane fusion during myelination. | lld:pubmed |
| pubmed-article:19170188 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19170188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19170188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19170188 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:19170188 | pubmed:issn | 1097-4547 | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:NaveKlaus-Arm... | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:SeredaMichael... | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:BrinkmannBast... | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:SchardtAnkeA | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:WernerHauke... | lld:pubmed |
| pubmed-article:19170188 | pubmed:author | pubmed-author:MitkovskiMiso... | lld:pubmed |
| pubmed-article:19170188 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19170188 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:19170188 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:19170188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19170188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19170188 | pubmed:pagination | 3465-79 | lld:pubmed |
| pubmed-article:19170188 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:19170188 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19170188 | pubmed:articleTitle | The SNARE protein SNAP-29 interacts with the GTPase Rab3A: Implications for membrane trafficking in myelinating glia. | lld:pubmed |
| pubmed-article:19170188 | pubmed:affiliation | Department of Neurogenetics, Max-Planck-Institute of Experimental Medicine, Göttingen, Germany. | lld:pubmed |
| pubmed-article:19170188 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19170188 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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