Structural basis for cytokinin receptor signaling: an evolutionary approach

Steklov, Mikhail; Lomin, Sergey N.; Osolodkin, Dmitry I.; Romanov, Georgy A.

doi:10.1007/s00299-013-1408-3

Cited by 46 publications

(69 citation statements)

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“…These histidine sensor kinases contain an extracellular domain of approximately 280 amino acids with putative N -glycosylation sites (Caesar et al, 2011; Steklov et al, 2013). The degree of N -glycosylation and the N -glycan structures of cytokinin receptors are not very well known, but for Arabidopsis AHK3 N -glycosylation could be shown by transient expression in tobacco (Caesar et al, 2011).…”

Section: The Function Of Complex N-glycansmentioning

confidence: 99%

Biological significance of complex N-glycans in plants and their impact on plant physiology

Strasser

2014

Front. Plant Sci.

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Asparagine (N)-linked protein glycosylation is a ubiquitous co- and post-translational modification which can alter the biological function of proteins and consequently affects the development, growth, and physiology of organisms. Despite an increasing knowledge of N-glycan biosynthesis and processing, we still understand very little about the biological function of individual N-glycan structures in plants. In particular, the N-glycan-processing steps mediated by Golgi-resident enzymes create a structurally diverse set of protein-linked carbohydrate structures. Some of these complex N-glycan modifications like the presence of β1,2-xylose, core α1,3-fucose or the Lewis a-epitope are characteristic for plants and are evolutionary highly conserved. In mammals, complex N-glycans are involved in different cellular processes including molecular recognition and signaling events. In contrast, the complex N-glycan function is still largely unknown in plants. Here, in this short review, I focus on important recent developments and discuss their implications for future research in plant glycobiology and plant biotechnology.

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Section: The Function Of Complex N-glycansmentioning

confidence: 99%

Biological significance of complex N-glycans in plants and their impact on plant physiology

Strasser

2014

Front. Plant Sci.

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“…Only the sequencing of more genomes from charophycean algae or species at the base of land plant evolution will allow us to identify the last common ancestor of these two receptor subfamilies. For such an analysis, the region of the CHASE domain might be enlarged, because recent analysis found high sequence conservation in the amino acids on both sides of the CHASE domain (Steklov et al, 2013).…”

Section: Cytokinin Perception Through the Chase Domain Might Have Emementioning

confidence: 99%

A Subfamily of Putative Cytokinin Receptors Is Revealed by an Analysis of the Evolution of the Two-Component Signaling System of Plants

et al. 2014

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The two-component signaling system-the major signaling pathway of bacteria-is found among higher eukaryotes only in plants, where it regulates diverse processes, such as the signaling of the phytohormone cytokinin. Cytokinin is perceived by a hybrid histidine (His) kinase receptor, and the signal is transduced by a multistep phosphorelay system of His phosphotransfer proteins and different classes of response regulators (RRs). To shed light on the origin and evolution of the two-component signaling system members in plants, we conducted a comprehensive domain-based phylogenetic study across the relevant kingdoms, including Charophyceae algae, the group of green algae giving rise to land plants. Surprisingly, we identified a subfamily of cytokinin receptors with members only from the early diverging land plants Marchantia polymorpha and Physcomitrella patens and then experimentally characterized two members of this subfamily. His phosphotransfer proteins of Charophyceae seemed to be more closely related to land plants than to other groups of green algae. Farther down the signaling pathway, the type-B RRs were found across all plant clades, but many members lack either the canonical Asp residue or the DNA binding domain. In contrast, the type-A RRs seemed to be limited to land plants. Finally, the analysis provided hints that one additional group of RRs, the type-C RRs, might be degenerated receptors and thus, of a different evolutionary origin than bona fide RRs.

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“…Cytokinin receptors are integral transmembrane proteins with histidine kinase activity (Kakimoto, ). Their hormone‐sensing domain is located on one side of the membrane whereas the histidine kinase and a receiver domain are always located on the other side (Steklov et al ., ). Activated receptors transmit the hormonal signal to the nucleus via His‐Asp phosphorelay with the participation of two additional proteins, phosphotransmitters and response regulators (Fig.…”

Section: Introductionmentioning

confidence: 97%

“…Similar to the bacterial prototype, the cytokinin receptors are thought to function as dimers. It was suggested that upon hormone binding the signal is transmitted by a piston‐type movement across the membrane (Steklov et al ., ; Bartrina et al ., ) followed by autophosphorylation of the receptor dimers at conserved His residues. Then this phosphate is transferred intramolecularly to a conserved Asp in the receiver domain at the C‐terminus of the protein.…”

Section: Introductionmentioning

confidence: 99%

Cytokinin signaling: from the ER or from the PM? That is the question!

2018

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Content Summary41I.Introduction41II.Historical outline42III.Recent developments43IV.Towards an integrative concept for cytokinin receptor signaling48Acknowledgements51References51 Summary Cytokinin signaling plays an important role in plant growth and development, and therefore its molecular characteristics are under extensive study. One characteristic is the subcellular localization of cytokinin signal initiation. This localization determines both the pathway for hormone delivery to the receptor, as well as molecular aspects of signal transfer to the primary cellular targets. Subcellular sites for the onset of cytokinin signaling are still uncertain and experimental data are in part controversial. A few years ago, cytokinin receptors were shown to be localized predominantly in the membrane of the endoplasmic reticulum (ER) and to possess some features, such as their pH activity profile, typical for intracellular proteins. Very recently, new data corroborating the functionality of ER‐located cytokinin receptors were reported. However, other work argued for cytokinin perception to occur at the plasma membrane (PM). Here, we discuss in detail these partially conflicting data and present an integrative model for cytokinin perception and signaling. In our opinion, the prevailing evidence argues for the ER being the predominant site of cytokinin signal perception but also that signal initiation at the PM might be relevant in some circumstances as well. The roles of these pathways in long‐distance, paracrine and autocrine cytokinin signaling are discussed.

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Structural basis for cytokinin receptor signaling: an evolutionary approach

Cited by 46 publications

References 46 publications

Biological significance of complex N-glycans in plants and their impact on plant physiology

Biological significance of complex N-glycans in plants and their impact on plant physiology

A Subfamily of Putative Cytokinin Receptors Is Revealed by an Analysis of the Evolution of the Two-Component Signaling System of Plants

Cytokinin signaling: from the ER or from the PM? That is the question!

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