Rab-A1c GTPase Defines a Population of the Trans-Golgi Network that Is Sensitive to Endosidin1 during Cytokinesis in Arabidopsis

• Published in: Molecular plant Vol. 6; no. 3; pp. 847 - 859
• Main Authors: Qi, Xingyun, Zheng, Huanquan
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01-05-2013
• Subjects: Androstadienes - pharmacology; Arabidopsis - cytology; Arabidopsis - drug effects; Arabidopsis - enzymology; Arabidopsis Proteins - metabolism; cytokinesis; Cytokinesis - drug effects; ES1; Glucuronidase - metabolism; Green Fluorescent Proteins - metabolism; Limonins - pharmacology; Meristem - drug effects; Meristem - growth & development; Meristem - metabolism; Mutation - genetics; Promoter Regions, Genetic - genetics; Protein Transport - drug effects; rab GTP-Binding Proteins - metabolism; Rab-A; Subcellular Fractions - drug effects; Subcellular Fractions - metabolism; TGN; trans-Golgi Network - drug effects; trans-Golgi Network - metabolism; Vacuolar Proton-Translocating ATPases - metabolism; Vacuoles - drug effects; Vacuoles - metabolism; ES1; TGN; Rab-A; cytokinesis
• ISSN: 1674-2052; 1752-9867
• DOI: 10.1093/mp/sss116

In plant cells, Rab-A proteins have been implicated to play important roles in membrane trafficking from the trans-Golgi network (TGN) to the plasma membrane/cell wall and to the newly formed cell plate in cytokinesis. But how different Rab-A proteins may work in the TGN is not well studied. We show here that RAB-A1c defines a population of TGN that is partially overlapped with the VHA-a1 marked-TGN. Interestingly, the morphology of RAB-A1c defined-TGN is sensitive to endosidin 1 (ES1), but not to wortmannin. In mitotic cells, RAB-A1c is relocated to the cell plate. We revealed that this process could be interrupted by ES1, but not by wortmannin. In addition, root growth and cytokinesis in root mitotic cells of rab-a1a/b/c triple mutant seedlings are hypersensitive to lower concentrations of ES1. ES1 is known to selectively block the transport of several plasma membrane auxin transporters, including PIN2 and AUX1 at the TGN. Together with the known facts that members of Rab-A1 proteins are involved in auxin-mediated responses in root growth and that mutations in TRAPPII, a protein complex that acts upstream of RAB-A1c, also selectively impair the transport of PIN2 and AUX1 at the TGN, we propose that the Rab-A1-mediated trafficking pathways around the TGN, but not Rab-A1s directly, are the target of ES1.