Plant immunophilins: a review of their structure-function relationship

Vasudevan, Dileep; Gopalan, Gayathri; Kumar, Ashish; Garcia, Veder J.; Luan, Sheng; Swaminathan, Kunchithapadam

doi:10.1016/j.bbagen.2014.12.017

Cited by 40 publications

(50 citation statements)

References 147 publications

(282 reference statements)

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“…1). Cyclophilins (also called rotamases and referred to either as Cyps, or ROCs for rotamase Cyps) are named after their high affinity for the cyclic peptide, cyclosporin A [48][49][50], which binds to the core cyclophilin-like domain (see Fig. 1).…”

Section: Plant Immunophilins Are Implicated In Regulation Of Developmentmentioning

confidence: 99%

“…Interaction with the classical chaperone, HSP90, also suggest that TWD1 might function as co-chaperone (reviewed in Refs. [48][49][50]54,59]). Another frequently studied Arabidopsis FKBP protein, PAS-TICCINO (AtFKBP72/PAS1), is involved in the control of cell proliferation and differentiation and was suggested to chaperone the nuclear translocation of a NAC transcription factor [68,69].…”

Section: Plant Immunophilins Are Implicated In Regulation Of Developmentmentioning

confidence: 99%

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Master and servant: Regulation of auxin transporters by FKBPs and cyclophilins

2016

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Plant development and architecture are greatly influenced by the polar distribution of the essential hormone auxin. The directional influx and efflux of auxin from plant cells depends primarily on AUX1/LAX, PIN, and ABCB/PGP/MDR families of auxin transport proteins. The functional analysis of these proteins has progressed rapidly within the last decade thanks to the establishment of heterologous auxin transport systems. Heterologous co-expression allowed also for the testing of protein-protein interactions involved in the regulation of transporters and identified relationships with members of the FK506-Binding Protein (FKBP) and cyclophilin protein families, which are best known in non-plant systems as cellular receptors for the immunosuppressant drugs, FK506 and cyclosporin A, respectively. Current evidence that such interactions affect membrane trafficking, and potentially the activity of auxin transporters is reviewed. We also propose that FKBPs andcyclophilins might integrate the action of auxin transport inhibitors, such as NPA, on members of the ABCB and PIN family, respectively. Finally, we outline open questions that might be useful for further elucidation of the role of immunophilins as regulators (servants) of auxin transporters (masters).

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Section: Plant Immunophilins Are Implicated In Regulation Of Developmentmentioning

confidence: 99%

Section: Plant Immunophilins Are Implicated In Regulation Of Developmentmentioning

confidence: 99%

Master and servant: Regulation of auxin transporters by FKBPs and cyclophilins

2016

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“…19 CYPs were detected in the human genome, whereas Saccharomyces cerevisiae possesses 8, Schizosaccharomyces pombe 9, Caenorhabditis elegans 17, Drosophila melanogaster 14 44, 45 , and the fungus Leptosphaeria maculans 12 46 CYPs. Compared to other organisms, plants have a higher number of CYPs with 29 encoded in A. thaliana 47–49 , and 27 in rice 37 . To date, soybean ( Glycine max ) is reported to have the largest set of CYPs with 62 members 50 .…”

Section: Introductionmentioning

confidence: 99%

Bioinformatic and expression analysis of the Brassica napus L. cyclophilins

Hanhart

Thieß

Amari

et al. 2017

Sci Rep

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Cyclophilins (CYPs) are a group of ubiquitous proteins characterized by their ability to bind to the immunosuppressive drug cyclosporin A. The CYP family occurs in a wide range of organisms and contains a conserved peptidyl-prolyl cis/trans isomerase domain. In addition to fulfilling a basic role in protein folding, CYPs may also play diverse important roles, e.g. in protein degradation, mRNA processing, development, and stress responses. We performed a genome-wide database survey and identified a total of 94 CYP genes encoding 91 distinct proteins. Sequence alignment analysis of the putative BnCYP cyclophilin-like domains revealed highly conserved motifs. By using RNA-Seq, we could verify the presence of 77 BnCYP genes under control conditions. To identify phloem-specific BnCYP proteins in a complementary approach, we used LC-MS/MS to determine protein abundances in leaf and phloem extracts. We detected 26 BnCYPs in total with 12 being unique to phloem sap. Our analysis provides the basis for future studies concentrating on the functional characterization of individual members of this gene family in a plant of dual importance: as a crop and a model system for polyploidization and long-distance signalling.As one of the most important crops for nutritional oil, fodder, biodiesel, chemical and pharmaceutical products, Brassica napus (oilseed rape or canola) is widespread in agriculture, especially in the European Union, China, and Canada. Beside its essential agricultural significance, B. napus has also become a model plant for studying long-distance signalling 1-5 and evolutionary consequences of polyploidization 6,7 . Brassica napus is used as a model plant for studying long-distance signalling, because methods for the collection of sufficient quantities of pure xylem and phloem sap are well established 2, 4 . Compared to crops like wheat, soybean or rice, the domestication of B. napus was more recent. It is assumed that chromosome doubling occurred after spontaneous hybridization between Brassica rapa (Asian cabbage or turnip rape, 2n = 2 × 10 = 20, genome AA) and Brassica oleracea (Mediterranean cabbage, 2n = 2 × 9 = 18, genome CC) 8 . The profitable cultivation of B. napus (genome AACC, 2n = 38) has high importance for the economy 9 .A group of proteins involved in diverse fundamental cellular functions in many different organisms is called immunophilins, originally discovered as receptors for immunosuppressive drugs in mammals. The family of immunophilins consists of two major groups, FK506-binding proteins (FKBPs) 10, 11 and cyclophilins (CYPs) 12,13 . Despite the lack of sequence and structure similarity, FKBPs and CYPs each possess a conserved domain responsible for their common peptidyl-prolyl cis/trans isomerase (PPIase) activity, catalyzing the rate-limiting rotation of X-proline peptide bonds from a cis to a trans conformation 14 . These domains are called the FKBP and cyclophilin-like domain (CLD), respectively. An additional group of proteins exhibiting PPIase activity, the parvulins, cannot be clas...

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“…The PPIase superfamily in higher eukaryotes includes cyclophilins (CYP), FK506-binding proteins, parvulins and PP2A phosphatase activators 18,19 . In plants, cyclophilin-like genes have been identified from a variety of species, including both Arabidopsis and rice [20][21][22] . A number of plant CYP genes, mainly in Arabidopsis, have been functionally characterized, involved in a variety of physiological and developmental processes, including in flowering, phytohormone signalling, stress responses and immune responses [22][23][24][25][26][27] .…”

mentioning

confidence: 99%

“…In plants, cyclophilin-like genes have been identified from a variety of species, including both Arabidopsis and rice [20][21][22] . A number of plant CYP genes, mainly in Arabidopsis, have been functionally characterized, involved in a variety of physiological and developmental processes, including in flowering, phytohormone signalling, stress responses and immune responses [22][23][24][25][26][27] . Mutations in LRT2-like genes of the tomato DIAGEOTROPICA (DGT) and the moss Physcomitrella patens PpDGT genes also caused an auxin-resistant phenotype [28][29][30] , indicating that this class of highly conserved genes plays an important role in regulating auxin signalling in both lower and higher plants.…”

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confidence: 99%

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

et al. 2015

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In plants, auxin signalling is initiated by the auxin-promoted interaction between the auxin receptor TIR1, an E3 ubiquitin ligase, and the Aux/IAA transcriptional repressors, which are subsequently degraded by the proteasome. Gain-of-function mutations in the highly conserved domain II of Aux/IAAs abolish the TIR1-Aux/IAA interaction and thus cause an auxin-resistant phenotype. Here we show that peptidyl-prolyl isomerization of rice OsIAA11 catalysed by LATERAL ROOTLESS2 (LRT2), a cyclophilin-type peptidyl-prolyl cis/trans isomerase, directly regulates the stability of OsIAA11. NMR spectroscopy reveals that LRT2 efficiently catalyses the cis/trans isomerization of OsIAA11. The lrt2 mutation reduces OsTIR1-OsIAA11 interaction and consequently causes the accumulation of a higher level of OsIAA11 protein. Moreover, knockdown of the OsIAA11 expression partially rescues the lrt2 mutant phenotype in lateral root development. Together, these results illustrate cyclophilincatalysed peptidyl-prolyl isomerization promotes Aux/IAA degradation, as a mechanism regulating auxin signalling.

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Plant immunophilins: a review of their structure-function relationship

Cited by 40 publications

References 147 publications

Master and servant: Regulation of auxin transporters by FKBPs and cyclophilins

Master and servant: Regulation of auxin transporters by FKBPs and cyclophilins

Bioinformatic and expression analysis of the Brassica napus L. cyclophilins

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

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