Linked Life Data

18182027

Source:http://linkedlifedata.com/resource/pubmed/id/18182027

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-3-20
pubmed:abstractText
Ethylene is an important hormone in plant growth, development and responses to environmental stimuli. The ethylene-signaling pathway is initiated by the induction of ethylene biosynthesis, which is under tight regulation at both transcriptional and post-transcriptional levels by exogenous and endogenous cues. 1-Aminocyclopropane-1-carboxylic acid synthase (ACS) is the rate-limiting enzyme that catalyzes the committing step of ethylene biosynthesis. Recently, we found that ACS2 and ACS6, two isoforms of the Arabidopsis ACS family, are substrates of a stress-responsive mitogen-activated protein kinase (MAPK) cascade. Phosphorylation of ACS2/ACS6 by MPK6 leads to the accumulation of ACS proteins and the induction of ethylene. In this report, we demonstrate that unphosphorylated ACS6 protein is rapidly degraded by the 26S proteasome pathway. The degradation machinery targets the C-terminal non-catalytic domain of ACS6, which is sufficient to confer instability to green fluorescent protein and luciferase reporters. Phosphorylation of ACS6 introduces negative charges to the C-terminus of ACS6, which reduces the turnover of ACS6 by the degradation machinery. Consistent with this, other nearby conserved negatively charged amino acid residues are essential for ACS6 stability regulation. Protein degradation and phosphorylation are two important post-translational modifications of proteins. This research reveals an intricate interplay between these two important processes in controlling the levels of cellular ACS activity, and thus ethylene biosynthesis. The post-translational nature of both processes ensures a rapid response of ethylene induction, which is detectable within minutes after plants are exposed to stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1365-313X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-40
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
MAPK phosphorylation-induced stabilization of ACS6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26S proteasome pathway.
pubmed:affiliation
Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.