The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana
- 26 April 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (13) , 2842-2846
- https://doi.org/10.1016/j.febslet.2005.04.022
Abstract
SNAREs (soluble N-ethyl-maleimide sensitive factor attachment protein receptors) which locate on the specific organelle membrane assure the correct vesicular transport by mediating specific membrane fusions. SNAREs are referred to as R- or Q-SNAREs on the basis of the amino acid sequence similarities and specific conserved residues. All of the Arabidopsis R-SNAREs have a N-terminal domain, called the longin domain (LD). In this study, we investigated the vacuolar targeting mechanism of Arabidopsis R-SNAREs. The vacuolar localized AtVAMP711 was used as the mother protein of GFP-tagged chimeric proteins joined to several domains such as the LD, the SNARE motif (SNM) and the transmembrane domain (TMD) of other organelle-localized R-SNAREs. The results showed that, whereas the TMD is not relevant for the vacuolar targeting, a complete LD is essential for the vacuolar and subcellular targeting.Keywords
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