Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.16 (calcineurin)
 17,112 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the root, the transport of auxin from the tip to the elongation zone, referred to here as shootward, governs gravitropic bending. Shootward polar auxin transport, and hence gravitropism, depends on the polar deployment of the PIN-FORMED auxin efflux carrier PIN2. In Arabidopsis thaliana, PIN2 has the expected shootward localization in epidermis and lateral root cap; however, this carrier is localized toward the root tip (rootward) in cortical cells of the meristem, a deployment whose function is enigmatic. We use pharmacological and genetic tools to cause a shootward relocation of PIN2 in meristematic cortical cells without detectably altering PIN2 polarization in other cell types or PIN1 polarization. This relocation of cortical PIN2 was negatively regulated by the membrane trafficking factor GNOM and by the regulatory A1 subunit of type 2-A protein phosphatase (PP2AA1) but did not require the PINOID protein kinase. When GNOM was inhibited, PINOID abundance increased and PP2AA1 was partially immobilized, indicating both proteins are subject to GNOM-dependent regulation. Shootward PIN2 specifically in the cortex was accompanied by enhanced shootward polar auxin transport and by diminished gravitropism. These results demonstrate that auxin flow in the root cortex is important for optimal gravitropic response.
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PMID:Gravitropism of Arabidopsis thaliana roots requires the polarization of PIN2 toward the root tip in meristematic cortical cells. 2056 36

Within a multicellular tissue cells may coordinately form a singular or multiple polar axes, but it is unclear whether a common mechanism governs different types of polar axis formation. The phosphorylation status of PIN proteins, which is directly affected by the PINOID (PID) protein kinase and the PP2A protein phosphatase, is known to regulate the apical-basal polarity of PIN localization in bipolar cells of roots and shoot apices. Here, we provide evidence that the phosphorylation status-mediated PIN polarity switch is widely used to modulate cellular processes in Arabidopsis including multipolar pavement cells (PC) with interdigitated lobes and indentations. The degree of PC interdigitation was greatly reduced either when the FYPP1 gene, which encodes a PP2A called phytochrome-associated serine/threonine protein phosphatase, was knocked out or when the PID gene was overexpressed (35S::PID). These genetic modifications caused PIN1 localization to switch from lobe to indentation regions. The PP2A and PID mediated switching of PIN1 localization is strikingly similar to their regulation of the apical-basal polarity switch of PIN proteins in other cells. Our findings suggest a common mechanism for the regulation of PIN1 polarity formation, a fundamental cellular process that is crucial for pattern formation both at the tissue/organ and cellular levels.
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PMID:Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis. 2142 79

Protein phosphorylation is a key molecular switch used to transmit information in biological signalling networks. The output of these signalling circuits is governed by the counteracting activities of protein kinases and phosphatases that determine the direction of the switch. Whereas many kinases have been functionally characterized, it has been difficult to ascribe precise cellular roles to plant phosphatases, which are encoded by enlarged gene families that may provide a high degree of genetic redundancy. In this work we have analysed the role in planta of catalytic subunits of protein phosphatase 2A (PP2A), a family encoded by five genes in Arabidopsis. Our results indicate that the two members of subfamily II, PP2A-C3 and PP2A-C4, have redundant functions in controlling embryo patterning and root development, processes that depend on auxin fluxes. Moreover, polarity of the auxin efflux carrier PIN1 and auxin distribution, determined with the DR5(pro) :GFP proxy, are affected by mutations in PP2A-C3 and PP2A-C4. Previous characterization of mutants in putative PP2A regulatory subunits had established a link between this class of phosphatases and PIN dephosphorylation and subcellular distribution. Building on those findings, the results presented here suggest that PP2A-C3 and PP2A-C4 catalyse this reaction and contribute critically to the establishment of auxin gradients for proper plant development.
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PMID:Specialized functions of the PP2A subfamily II catalytic subunits PP2A-C3 and PP2A-C4 in the distribution of auxin fluxes and development in Arabidopsis. 2316 45

Recently, we reported that the D6 protein kinase subfamily, which belongs to the AGCVIII kinase family, is a critical component of hypocotyl phototropism in Arabidopsis seedlings. Furthermore, we demonstrated that AGC1-12, which is also a member of the AGCVIII kinase family, is involved in both the pulse-induced first positive phototropism and gravitropism in Arabidopsis hypocotyls. Those results indicated that phosphorylation control is an important mechanism in phototropic signaling. As phosphorylation regulation is controlled by both kinases and phosphatases, we investigated the roles of phosphatases in hypocotyl phototropism. Our physiological analysis, which was performed using Arabidopsis mutants, indicated that the flower-specific, phytochrome-associated protein phosphatase family, which functions as a catalytic subunit of protein phosphatase 6 (PP6), is involved in both the pulse-induced first positive phototropism and the time-dependent second positive phototropism, although it is not necessary for the continuous-light-induced second positive phototropism. These results suggest that not only kinases, but also phosphatases play critical roles in hypocotyl phototropism to control phosphorylation status and that PP6-type protein phosphatases may act antagonistically with AGCVIII protein kinases on the same targets, such as PIN-formed proteins.
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PMID:Involvement of PP6-type protein phosphatase in hypocotyl phototropism in Arabidopsis seedlings. 3037 70