English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Assembly and Sorting of the Tonoplast Potassium Channel AtTPK1 and Its Turnover by Internalization into the Vacuole

Maitrejean, M., Wudick, M. M., Voelker, C., Prinsi, B., Mueller-Roeber, B., Czempinski, K., et al. (2011). Assembly and Sorting of the Tonoplast Potassium Channel AtTPK1 and Its Turnover by Internalization into the Vacuole. Plant Physiology, 156(4), 1783-1796. doi:10.1104/pp.111.177816.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2161-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2162-B
Genre: Journal Article

Files

show Files
hide Files
:
Maitrejean-2011-Assembly and Sorting.pdf (Any fulltext), 2MB
Name:
Maitrejean-2011-Assembly and Sorting.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Maitrejean, M.1, Author
Wudick, M. M.1, Author
Voelker, C.1, Author
Prinsi, B.1, Author
Mueller-Roeber, B.2, Author              
Czempinski, K.2, Author              
Pedrazzini, E.1, Author
Vitale, A.1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Plant Signalling, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753311              

Content

show
hide
Free keywords: green fluorescent protein plant k+ channels endoplasmic-reticulum arabidopsis-thaliana plasma-membrane secretory pathway quality-control h+-atpase domain cells
 Abstract: The assembly, sorting signals, and turnover of the tonoplast potassium channel AtTPK1 of Arabidopsis (Arabidopsis thaliana) were studied. We used transgenic Arabidopsis expressing a TPK1-green fluorescent protein (GFP) fusion or protoplasts transiently transformed with chimeric constructs based on domain exchange between TPK1 and TPK4, the only TPK family member not located at the tonoplast. The results show that TPK1-GFP is a dimer and that the newly synthesized polypeptides transiently interact with a thus-far unidentified 20-kD polypeptide. A subset of the TPK1-TPK4 chimeras were unable to assemble correctly and these remained located in the endoplasmic reticulum where they interacted with the binding protein chaperone. Therefore, TPK1 must assemble correctly to pass endoplasmic reticulum quality control. Substitution of the cytosolic C terminus of TPK4 with the corresponding domain of TPK1 was sufficient to allow tonoplast delivery, indicating that this domain contains tonoplast sorting information. Pulse-chase labeling indicated that TPK1-GFP has a half-life of at least 24 h. Turnover of the fusion protein involves internalization into the vacuole where the GFP domain is released. This indicates a possible mechanism for the turnover of tonoplast proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2011-06-222011
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: ISI:000293568800011
DOI: 10.1104/pp.111.177816
ISSN: 0032-0889
URI: ://000293568800011 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3149923/pdf/1783.pdf?tool=pmcentrez
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Plant Physiology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 156 (4) Sequence Number: - Start / End Page: 1783 - 1796 Identifier: -