Protein Phosphatases at the Interface of Sugar and Hormone Signaling Pathways to Balance Growth and Stress Responses in
Phosphorylation and dephosphorylation serve as one of the major posttranslational regulatory mechanisms of proteins to control cellular activities in eukaryotic organisms. Protein phosphatases are involved in the catalysis of the reversible dephosphorylat
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Protein Phosphatases at the Interface of Sugar and Hormone Signaling Pathways to Balance Growth and Stress Responses in Plants Harshita B. Saksena, Dhriti Singh, Manvi Sharma, Muhammed Jamsheer K., Sunita Jindal, Mohan Sharma, Archna Tiwari, Prakhar, Sanjay Singh Rawat, and Ashverya Laxmi
7.1 Introduction Plants are often exposed to fluctuating environmental conditions, and being sessile, they require intricate mechanisms for their survival. Plants rely on various stress sensing and signaling networks to respond to abiotic and biotic stresses. Posttranslational modifications through phosphorylation of proteins to regulate cellular functions are a phenomenon which is ubiquitous to all the organisms (Smith and Walker 1996). Protein kinases and phosphatases catalyze phosphorylation and dephosphorylation of cellular proteins, respectively (Smith and Walker 1996). Phosphorylation leads to conformational changes in proteins, thereby regulating their activity and interaction with other proteins to form a complex (Pawson 1995; Luan 2003). Intracellular signaling in response to external stimulus involves phosphorylation of many proteins in order to migrate to the destination site in the cell and regulate the target proteins. Reversible phosphorylation of cellular proteins controls a spectrum of biological functions like growth and development processes, metabolism, cell cycle control, and stress responses (Luan 2003). Protein phospha-
Harshita B. Saksena, Dhriti Singh, and Manvi Sharma contributed equally to this work. Muhammed Jamsheer K., Sunita Jindal, Mohan Sharma, Archna Tiwari, Prakhar, and Sanjay Singh Rawat contributed equally to this work. H. B. Saksena · D. Singh · M. Sharma · S. Jindal · M. Sharma · A. Tiwari · Prakhar · S. S. Rawat · A. Laxmi (*) National Institute of Plant Genome Research, New Delhi, India e-mail: [email protected] M. Jamsheer K. Amity Food and Agriculture Foundation, Amity University Uttar Pradesh, Noida, India © Springer Nature Switzerland AG 2020 G. K. Pandey (ed.), Protein Phosphatases and Stress Management in Plants, https://doi.org/10.1007/978-3-030-48733-1_7
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tases target hydroxyl group of specific amino acid residues, majorly of serine and threonine and seldom of tyrosine (Shenolikar 1994; Smith and Walker 1996). Several studies also report the evidence of phosphohistidine phosphorylation in eukaryotic organisms (Ota and Varshavsky 1993; Huber et al. 1994; Crovello et al. 1995; Smith and Walker 1996). Localization of protein phosphatase occurs majorly in subcellular organelles including nuclei, chloroplast, mitochondria, cytosol, and some membrane fractions (MacKintosh et al. 1991; Huber et al. 1994; Smith and Walker 1996). Protein phosphatases have been classified into type I (PP1) and type II (PP2) in mammals and plants on the basis of their specificity to certain substrates and sensitivity to the inhibitors, inhibitor-1 (I-1) and inhibitor-2 (I-2) (Ingebritsen and Cohen 1983; Cohen 1989; Smith and Walker 1996). PP1 targets the β-subunit o
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