Regulatory 14-3-3 proteins bind the atypical motif within the C terminus of the plant plasma membrane H+-ATPase via their typical amphipathic groove

Regulatory 14-3-3 proteins bind the atypical motif within the C terminus of the plant plasma... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Planta Springer Journals

Regulatory 14-3-3 proteins bind the atypical motif within the C terminus of the plant plasma membrane H+-ATPase via their typical amphipathic groove

Planta, Volume 216 (1) – Nov 12, 2002

Loading next page...
 
/lp/springer-journals/regulatory-14-3-3-proteins-bind-the-atypical-motif-within-the-c-IxCSFcjkJO
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
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

PlantaSpringer Journals

Published: Nov 12, 2002

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create folders to
organize your research

Export folders, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off