Phosphorylation regulated ion‐binding is a property shared by the acidic subclass dehydrins

By M. Alsheikh, J. Svensson, S. Randall. 2005

117 citations recorded by the source corpus.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/23d5fb1f9d7d28e93766fea4e6304b05ea26f07f

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Citations in the corpus

LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana (2008, background): “They have also been subdivided into an acidic group containing COR47 (#4), ERD10 (#5), ERD14 (#10), #14, #44, and #45, and a basic/neutral group containing #8, XERO2 (#33), XERO1 (#34), and RAB18 (#51) [ 53 ].”
The continuing conundrum of the LEA proteins (2007, background): “Three acidic Group 2b proteins, ERD10, COR47 and ERD14, have also been shown to exhibit phosphorylation-dependent Ca2+ binding (Alsheikh et al. 2003, 2005).”
The Enigmatic LEA Proteins and Other Hydrophilins1[W] (2008, background): “Moreover, acidic dehydrins such as a vacuole-associated dehydrin from celery (Apium graveolens; VCaB45) and Arabidopsis ERD14 possess calcium-binding properties, which seem to be positively modulated by phosphorylation (Heyen et al., 2002; Alsheikh et al., 2003, 2005).”
Recent Updates on Salinity Stress in Rice: From Physiological to Molecular Responses (2011, background): “For some proteins of this group, namely acidic dehydrins, ion-binding activity is most likely one of the major biochemical functions, acting as calcium buffers or as calcium-dependent chaperonelike molecules (Alsheikh et al., 2005).”
Insights into Late Embryogenesis Abundant (LEA) Proteins in Plants: From Structure to the Functions (2014, background): “Phosphorylation sites are located in the serine motif [143].”
The role of dehydrins in plant response to cold (2007, background): “Recently, Alsheikh et al. (2005) showed that in vitro phosphorylated COR47 and ERD10 are also able to bind calcium ions and therefore it can be proposed that a calcium-binding activity is a trait shared by acidic dehydrins in A. thaliana.”