Internalized and newly synthesized Arabidopsis PIN-FORMED2 pass through brefeldin A compartments: a new insight into intracellular dynamics of the protein by using the photoconvertible fluorescence protein Dendra2 as a tag.
jan.jasik@rec.uniba.sk.
Ján
J
Jásik
a Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Köln, Germany.
Elmon
E
Schmelzer
D017360:Arabidopsis / Q000187:drug effects / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000096:biosynthesis*; D020126:Brefeldin A / Q000494:pharmacology*; D002451:Cell Compartmentation / Q000187:drug effects*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D004705:Endocytosis / Q000187:drug effects; D005453:Fluorescence; D042541:Intracellular Space / Q000187:drug effects / Q000378:metabolism*; D008164:Luminescent Proteins / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D029681:Arabidopsis Proteins; D020126:Brefeldin A; D008164:Luminescent Proteins; D011993:Recombinant Fusion Proteins; C583169:Dendra2 protein, Dendronephthya; C117013:AT5G57090 protein, Arabidopsis