Protein phosphatases and their targets: Comprehending the interactions in plant signaling pathways.

3区 生物学 Q1 Biochemistry, Genetics and Molecular Biology Advances in protein chemistry and structural biology Pub Date : 2023-01-01 DOI:10.1016/bs.apcsb.2022.11.003
Lokesh K Saini, Malathi Bheri, Girdhar K Pandey
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Abstract

Protein phosphorylation is a vital reversible post-translational modification. This process is established by two classes of enzymes: protein kinases and protein phosphatases. Protein kinases phosphorylate proteins while protein phosphatases dephosphorylate phosphorylated proteins, thus, functioning as 'critical regulators' in signaling pathways. The eukaryotic protein phosphatases are classified as phosphoprotein phosphatases (PPP), metallo-dependent protein phosphatases (PPM), protein tyrosine (Tyr) phosphatases (PTP), and aspartate (Asp)-dependent phosphatases. The PPP and PPM families are serine (Ser)/threonine (Thr) specific phosphatases (STPs) that dephosphorylate Ser and Thr residues. The PTP family dephosphorylates Tyr residues while dual-specificity phosphatases (DsPTPs/DSPs) dephosphorylate Ser, Thr, and Tyr residues. The composition of these enzymes as well as their substrate specificity are important determinants of their functional significance in a number of cellular processes and stress responses. Their role in animal systems is well-understood and characterized. The functional characterization of protein phosphatases has been extensively covered in plants, although the comprehension of their mechanistic basis is an ongoing pursuit. The nature of their interactions with other key players in the signaling process is vital to our understanding. The substrates or targets determine their potential as well as magnitude of the impact they have on signaling pathways. In this article, we exclusively overview the various substrates of protein phosphatases in plant signaling pathways, which are a critical determinant of the outcome of various developmental and stress stimuli.

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蛋白磷酸酶及其靶标:了解植物信号通路中的相互作用。
蛋白磷酸化是一个重要的可逆的翻译后修饰。这个过程是由两类酶建立的:蛋白激酶和蛋白磷酸酶。蛋白激酶使蛋白质磷酸化,而蛋白磷酸酶使磷酸化的蛋白质去磷酸化,因此,在信号通路中起“关键调节”的作用。真核生物蛋白磷酸酶分为磷酸蛋白磷酸酶(PPP)、金属依赖性蛋白磷酸酶(PPM)、蛋白酪氨酸(Tyr)磷酸酶(PTP)和天冬氨酸(Asp)依赖性磷酸酶。PPP和PPM家族是丝氨酸(Ser)/苏氨酸(Thr)特异性磷酸酶(stp),可使丝氨酸和苏氨酸残基去磷酸化。PTP家族使Tyr残基去磷酸化,而双特异性磷酸酶(dsptp / dsp)使Ser、Thr和Tyr残基去磷酸化。这些酶的组成以及它们的底物特异性是它们在许多细胞过程和应激反应中的功能意义的重要决定因素。它们在动物系统中的作用已经被很好地理解和描述。植物中蛋白磷酸酶的功能特征已经被广泛报道,尽管对其机制基础的理解仍是一个持续的追求。它们在信号传递过程中与其他关键参与者相互作用的性质对我们的理解至关重要。底物或靶标决定了它们对信号通路的潜在影响和影响程度。在本文中,我们专门概述了植物信号通路中蛋白磷酸酶的各种底物,它们是各种发育和胁迫刺激结果的关键决定因素。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Advances in protein chemistry and structural biology
Advances in protein chemistry and structural biology BIOCHEMISTRY & MOLECULAR BIOLOGY-
CiteScore
7.40
自引率
0.00%
发文量
66
审稿时长
>12 weeks
期刊介绍: Published continuously since 1944, The Advances in Protein Chemistry and Structural Biology series has been the essential resource for protein chemists. Each volume brings forth new information about protocols and analysis of proteins. Each thematically organized volume is guest edited by leading experts in a broad range of protein-related topics.
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