The myo-inositol signaling pathway in plants allows them to sense external environmental stimuli and respond to them. This signaling pathway depends on the dynamic levels of the second messenger, inositol(1,4,5)trisphosphate, which in turn is regulated by inositol polyphosphate 5-phosphatases (5PTases). Previous studies have shown that 5PTase 13 binds an important energy sensor, Sucrose non-fermenting (Snf) 1-related kinase (SnRK1.1) and also a novel protein P80. Studies from the lab have also shown that P80 is a part of a deubiquitinating enzyme complex along with WDR20 and Ubiquitin-specific protease called UBP3. Our p80 mutants have a root deficient phenotype under low energy conditions which is normalized by addition of sucrose. p80 mutants show reduced growth and early senescence under specific environmental conditions. This is opposite in nature to SnRK1.1 overexpressors. In this study, I have examined the possible interaction of P80 with SnRK1. I have studied the effects of expression of the exogenous SnRK1.1:GFP transgene under the control of the 35S CaMV promoter in the p80 mutant. This will facilitate the delineation of mechanisms that plants use for the control of energy sensing. I also examined the effects of the overexpression of SnRK1.2:GFP in the p80 mutant. Further, I have explored the presence of a new class of molecules, inositol phosphate molecules (InsPs) containing pyrophosphate bonds (PPx) in p80 mutants. Recent evidence has shown that this class of molecules has roles in sensing and signaling. I have demonstrated that InsP7 is present in developing seeds and vegetative tissue of higher plants. I have also demonstrated that p80 mutants have an alteration in the levels of PPx-InsPs. In addition, I have established spatial expression patterns of two enzymes involved in the synthesis of PPx-InsPx, known as VIP kinases. These studies will help resolve how PPx-InsPs are regulated in plants and thus help in their functional characterization.