Structural characterizations of phosphorylatable residues in transmembrane proteins from Arabidopsis thaliana

Intrinsically Disordered Proteins
Bin Xue, Vladimir N Uversky

Abstract

Phosphorylation is a common post-translational modification that plays important roles in a wide range of biochemical and cellular processes. Many enzymes and receptors can be switched "on" or "off" by conformational changes induced by phosphorylation. The phosphorylation process is mediated by a family of enzymes called kinase. Currently, more than 1,000 different kinases have been identified in Arabidopsis thaliana proteome. Kinases interact with each other and with many regulatory proteins forming phosphorylation networks. These phosphorylation networks modulate the signaling processes and control the functions of cells. Normally, kinases phosphorylate serines, threonines, and tyrosines. However, in many proteins, not all of these 3 types of amino acids can be phosphorylated. Therefore, identifying the phosphorylation sites and the possible phosphorylation events is very important in decoding the processes of regulation and the function of phosphorylation networks. In this study, we applied computational and bioinformatics tools to characterize the association between phosphorylation events and structural properties of corresponding proteins by analyzing more than 50 trans-membrane proteins from Arabidopsis thaliana. In addi...Continue Reading

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Citations

May 30, 2019·The Journal of Membrane Biology·Rajeswari AppaduraiAnand Srivastava
Sep 1, 2015·Journal of Theoretical Biology·Jia Yuan, Bin Xue

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Methods Mentioned

BETA
RSA

Software Mentioned

NetsurfP
PONDR
VLXT
PhosPhAT
FIT

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