The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana.
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.
Uemura
Tomohiro
T
Graduate School of Biostudies, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Japan. tuemura@biol.s.u-tokyo.ac.jp
Sato
Masa H
MH
Takeyasu
Kunio
K
D017360:Arabidopsis / Q000378:metabolism*; D018613:Microscopy, Confocal; D050600:SNARE Proteins; D013347:Subcellular Fractions / Q000378:metabolism*; D033921:Vesicular Transport Proteins / Q000737:chemistry / Q000378:metabolism*
D050600:SNARE Proteins; D033921:Vesicular Transport Proteins