Abstract
Secretory Carrier Membrane Proteins (SCAMPs) are ubiquitous components of recycling vesicles that shuttle between the plasma membrane, endosomes, and trans-Golgi complex in mammalian cells. SCAMPs are consisted with a cytoplasmic N-terminal domain with NPF repeats, four central transmembrane regions, and a cytoplasmic tail. We obtained tobacco homolog cDNA for SCAMP (NtSCAMP) from EST collection of tobacco culture BY-2 cells. Using this clone and antibodies against encoding protein, we have been analyzing about localization and the function of SCAMP in plant cells. We investigated the localization of NtSCANP with YFP fusion (NtSCAMP-YFP) in BY-2 cells by video and laser scanning fluorescent microscopy. SCAMP-YFP was localized in plasma membrane, and endosome, which is a FM4-64 positive compartment. In dividing cells, it was detected predominantly on phragmoplast. By immunocytochemical analyses using anti-NtSCAMP antibody, NtSCAMP were localized along divided plate.
