The SNARE Protein SNAP-29 Interacts With the GTPase Rab3A: Implications for Membrane Trafficking in Myelinating Glia
2009 | journal article. A publication with affiliation to the University of Göttingen.
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The SNARE Protein SNAP-29 Interacts With the GTPase Rab3A: Implications for Membrane Trafficking in Myelinating Glia
Schardt, A.; Brinkmann, B. G.; Mitkovski, M.; Sereda, M. W.; Werner, H. B. & Nave, K.-A. (2009)
Journal of Neuroscience Research, 87(15) pp. 3465-3479. DOI: https://doi.org/10.1002/jnr.22005
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- Authors
- Schardt, Anke; Brinkmann, Bastian G.; Mitkovski, Miso; Sereda, Michael W.; Werner, Hauke B.; Nave, Klaus-Armin
- Abstract
- 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. (C) 2009 Wiley-Liss, Inc.
- Issue Date
- 2009
- Status
- published
- Publisher
- Wiley-blackwell
- Journal
- Journal of Neuroscience Research
- ISSN
- 0360-4012
- Sponsor
- DFG [SFB 523]; BMBF (Leukonet)