Conserved Arabidopsis ECHIDNA protein mediates trans-Golgi-network trafficking and cell elongation


Gendre, Delphine, Oh, Jaesung, Boutte, Yuhann, Best, Jacob G., Samuels, Lacey, Nilsson, Robert, Uemura, Tomohiro, Marchant, Alan, Bennett, Malcolm J., Grebe, Markus and Bhalerao, Rishikesh P. (2011) Conserved Arabidopsis ECHIDNA protein mediates trans-Golgi-network trafficking and cell elongation. Proceedings of the National Academy of Sciences, 108, (19), 8048-8053. (doi:10.1073/pnas.1018371108). (PMID:21512130).

Download

Full text not available from this repository.

Description/Abstract

Multiple steps of plant growth and development rely on rapid cell elongation during which secretory and endocytic trafficking via the trans-Golgi network (TGN) plays a central role. Here, we identify the ECHIDNA (ECH) protein from Arabidopsis thaliana as a TGN-localized component crucial for TGN function. ECH partially complements loss of budding yeast TVP23 function and a Populus ECH complements the Arabidopsis ech mutant, suggesting functional conservation of the genes. Compared with wild-type, the Arabidopsis ech mutant exhibits severely perturbed cell elongation as well as defects in TGN structure and function, manifested by the reduced association between Golgi bodies and TGN as well as mislocalization of several TGN-localized proteins including vacuolar H+-ATPase subunit a1 (VHA-a1). Strikingly, ech is defective in secretory trafficking, whereas endocytosis appears unaffected in the mutant. Some aspects of the ech mutant phenotype can be phenocopied by treatment with a specific inhibitor of vacuolar H+-ATPases, concanamycin A, indicating that mislocalization of VHA-a1 may account for part of the defects in ech. Hence, ECH is an evolutionarily conserved component of the TGN with a central role in TGN structure and function.

Item Type: Article
ISSNs: 0027-8424 (print)
1091-6490 (electronic)
Related URLs:
Keywords: secretory pathway, dwarf mutant, vacuolar defect
Subjects: Q Science > QH Natural history > QH301 Biology
R Medicine > R Medicine (General)
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 184787
Date Deposited: 09 May 2011 09:27
Last Modified: 27 Mar 2014 19:39
URI: http://eprints.soton.ac.uk/id/eprint/184787

Actions (login required)

View Item View Item