The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana |
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Authors: | Uemura Tomohiro Sato Masa H Takeyasu Kunio |
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Affiliation: | Graduate School of Biostudies, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Japan. tuemura@biol.s.u-tokyo.ac.jp |
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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. |
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Keywords: | SNAREs, soluble N-ethyl-maleimide sensitive factor attachment protein receptors LD, longin domain SNM, SNARE motif TMD, transmembrane region PM, plasma membrane TGN, trans-Golgi network GFP, green fluorescent protein |
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