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- Publisher
- Springer Journals
- Copyright
- Copyright © 2002 by Springer-Verlag
- Subject
- Life Sciences; Plant Sciences; Agriculture; Ecology; Forestry
- ISSN
- 0032-0935
- eISSN
- 1432-2048
- DOI
- 10.1007/s00425-002-0915-1
- pmid
- 12430022
- Publisher site
- See Article on Publisher Site
Abstract
The plant plasma membrane H+-ATPase contains a C-terminal autoinhibitory domain whose displacement from the catalytic site is caused by binding of regulatory 14-3-3 proteins. Members of the highly conserved 14-3-3 family bind their individual target proteins in a sequence-specific and phosphorylation-dependent manner within a central groove, the latter characterized by the presence of highly invariant residues. However, an atypical binding site for 14-3-3s within the H+-ATPase has been identified that does not resemble any other 14-3-3 binding motif. Combination of site-directed mutagenesis with glutathione S-transferase pull-down assays points to the importance of the central 14-3-3 groove for the interaction with the apparently unique site of the H+-ATPase. Furthermore, a 14-3-3 dimer is essential for binding such unusual motif.
Journal
Planta – Springer Journals
Published: Nov 12, 2002