CBL–CIPK module-mediated phosphoregulation: facts and hypothesis

Calcium (Ca2+) signaling is a versatile signaling network in plant and employs very efficient signal decoders to transduce the encoded message. The CBL–CIPK module is one of the sensor-relay decoders that have probably evolved with the acclimatization of land plant. The CBLs are unique proteins with non-canonical Ca2+ sensing EF-hands, N-terminal localization motif and a C-terminal phosphorylation motif. The partner CIPKs are Ser/Thr kinases with kinase and regulatory domains. Phosphorylation plays a major role in the functioning of the module. As the module has a functional kinase to transduce signal, it employs phosphorylation as a preferred mode for modulation of targets as well as its interaction with CBL. We analyze the data on the substrate regulation by the module from the perspective of substrate phosphorylation. We have also predicted some of the probable sites in the identified substrates that may be the target of the CIPK mediated phosphorylation. In addition, phosphatases have been implicated in reversing the CIPK mediated phosphorylation of substrates. Therefore, we have also presented the role of phosphatases in the modulation of the CBL–CIPK and its targets. We present here an overview of the phosphoregulation mechanism of the CBL–CIPK module.

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PARN-like Proteins Regulate Gene Expression in Land Plant Mitochondria by Modulating mRNA Polyadenylation

International Journal of Molecular Sciences ◽

10.3390/ijms221910776 ◽

2021 ◽

Vol 22 (19) ◽

pp. 10776

Author(s):

Takashi Hirayama

Keyword(s):

Mitochondrial Gene ◽

Plant Mitochondria ◽

Short Review ◽

Land Plant ◽

Mrna Processing ◽

Regulate Gene Expression ◽

Double Stranded Dna ◽

Regulatory Systems ◽

Mrna Polyadenylation

Mitochondria have their own double-stranded DNA genomes and systems to regulate transcription, mRNA processing, and translation. These systems differ from those operating in the host cell, and among eukaryotes. In recent decades, studies have revealed several plant-specific features of mitochondrial gene regulation. The polyadenylation status of mRNA is critical for its stability and translation in mitochondria. In this short review, I focus on recent advances in understanding the mechanisms regulating mRNA polyadenylation in plant mitochondria, including the role of poly(A)-specific ribonuclease-like proteins (PARNs). Accumulating evidence suggests that plant mitochondria have unique regulatory systems for mRNA poly(A) status and that PARNs play pivotal roles in these systems.

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Salicylic acid and formation of plant adaptive responses to abiotic stressors: role of signaling network components

Vestnik Tomskogo gosudarstvennogo universiteta Biologiya ◽

10.17223/19988591/55/8 ◽

2021 ◽

pp. 135-165

Author(s):

Yuriy E. Kolupaev ◽

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Tetiana O. Yastreb ◽

Aleksey K. Polyakov ◽

Alexander P. Dmitriev ◽

...

Keyword(s):

Salicylic Acid ◽

Signaling Network ◽

Adaptive Responses ◽

Abiotic Stressors

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Protein Phosphatases in G1 Regulation

International Journal of Molecular Sciences ◽

10.3390/ijms21020395 ◽

2020 ◽

Vol 21 (2) ◽

pp. 395 ◽

Cited By ~ 4

Author(s):

Ruth Martín ◽

Vilte Stonyte ◽

Sandra Lopez-Aviles

Keyword(s):

Cell Cycle ◽

Protein Phosphatases ◽

Eukaryotic Cells ◽

Signalling Pathways ◽

Cyclin Dependent Kinase ◽

Restriction Point ◽

Environmental Signals ◽

Substrate Phosphorylation ◽

Cell Cycle Machinery

Eukaryotic cells make the decision to proliferate, to differentiate or to cease dividing during G1, before passage through the restriction point or Start. Keeping cyclin-dependent kinase (CDK) activity low during this period restricts commitment to a new cell cycle and is essential to provide the adequate timeframe for the sensing of environmental signals. Here, we review the role of protein phosphatases in the modulation of CDK activity and as the counteracting force for CDK-dependent substrate phosphorylation, in budding and fission yeast. Moreover, we discuss recent findings that place protein phosphatases in the interface between nutritional signalling pathways and the cell cycle machinery.

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An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

Pathogens ◽

10.3390/pathogens9110916 ◽

2020 ◽

Vol 9 (11) ◽

pp. 916

Author(s):

Robert J. J. Jansens ◽

Sandra Marmiroli ◽

Herman W. Favoreel

Keyword(s):

Gene Expression ◽

Protein Kinase ◽

Pseudorabies Virus ◽

Signaling Network ◽

Cellular Proteins ◽

Future Research ◽

Nuclear Egress ◽

Infected Cells ◽

Important Virulence Factor

The US3 serine/threonine protein kinase is conserved among the alphaherpesvirus family and represents an important virulence factor. US3 plays a role in viral nuclear egress, induces dramatic alterations of the cytoskeleton, represses apoptosis, enhances gene expression and modulates the immune response. Although several substrates of US3 have been identified, an unbiased screen to identify US3 phosphorylation targets has not yet been described. Here, we perform a shotgun and phosphoproteomics analysis of cells expressing the US3 protein of pseudorabies virus (PRV) to identify US3 phosphorylation targets in an unbiased way. We identified several cellular proteins that are differentially phosphorylated upon US3 expression and validated the phosphorylation of lamin A/C at serine 404, both in US3-transfected and PRV-infected cells. These results provide new insights into the signaling network of the US3 protein kinase and may serve as a basis for future research into the role of the US3 protein in the viral replication cycle.

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