Publication Information
Whiteman et al., 2008
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Abstract
Proteomics. 2008 Sep;8(17):3536-47. doi: 10.1002/pmic.200701104.
Identification of novel proteins and phosphorylation sites in a tonoplast
enriched membrane fraction of Arabidopsis thaliana.
Whiteman SA(1), Serazetdinova L, Jones AM, Sanders D, Rathjen J, Peck SC,
Maathuis FJ.
Author information:
(1)Department of Biology Area 9, University of York, York, UK.
Plant vacuoles play essential roles in many physiological processes,
particularly in mineral nutrition, turgor provision and cellular signalling. The
vacuolar membrane, the tonoplast, contains many membrane transporters that are
critical in the execution of these processes. However, although increasing
knowledge is available about the identity of proteins involved in these
processes very little is known about the regulation of tonoplast transporters.
By studying the phosphoproteome of tonoplast-enriched membranes, we identified
66 phosphorylation sites on 58 membrane proteins. Amongst these, 31 sites were
identified in 28 membrane transporters of various families including tonoplast
anion transporters of the CLC family, potassium transporters of the KUP family,
tonoplast sugar transporters and ABC transporters. In a number of cases, the
detected sites were well conserved across isoforms of one family pointing to
common mechanisms of regulation. In other cases, isoform-unique sites were
present, suggesting regulatory mechanisms tailored to the function of individual
proteins. These results provide the basis for future studies to elucidate the
mechanistic regulation of tonoplast membrane transporters.
DOI: 10.1002/pmic.200701104
PMID: 18686298 [Indexed for MEDLINE]
