Abstract:BackgroundN-ethyl-maleimide sensitive factor adaptor protein receptor (SNAREs) domain-containing proteins were known as key players in vesicle-associated membrane fusion. Genetic screening has revealed the function of SNAREs in different aspects of plant biology, but the role of many SNAREs are still unknown. In this study, we have characterized the role of Arabidopsis Qc-SNARE protein AtBS14b in brassinosteroids (BRs) signaling pathway.ResultsAtBS14b overexpression (AtBS14b ox) plants exhibited short hypocoty… Show more
“…Overexpression of the AtBS14b caused insensitivity to exogenously applied BRs. AtBS14b directly interacts with the Membrane Steroid-Binding Protein1 (MSBP1) at vesicular compartments, but not with BRI1 or BAK1 [ 96 ]. The MSBP1 protein is localized in the plasma membrane and endosomes, and is able to bind the BR ligand.…”
Section: The Br Signalosome—an Updatementioning
confidence: 99%
“…Transcription of the AtBS14b gene is down-regulated by BR in the BRI1-mediated process. AtBS14b acts via interacting with MSBP1 in the trans-Golgi network to enhance transport of MSBP1 to plasma membrane and its interaction with BAK1 [ 96 ] ( Figure 1 ).…”
Brassinosteroids (BRs) are a class of phytohormones, which regulate various processes during plant life cycle. Intensive studies conducted with genetic, physiological and molecular approaches allowed identification of various components participating in the BR signaling—from the ligand perception, through cytoplasmic signal transduction, up to the BR-dependent gene expression, which is regulated by transcription factors and chromatin modifying enzymes. The identification of new components of the BR signaling is an ongoing process, however an emerging view of the BR signalosome indicates that this process is interconnected at various stages with other metabolic pathways. The signaling crosstalk is mediated by the BR signaling proteins, which function as components of the transmembrane BR receptor, by a cytoplasmic kinase playing a role of the major negative regulator of the BR signaling, and by the transcription factors, which regulate the BR-dependent gene expression and form a complicated regulatory system. This molecular network of interdependencies allows a balance in homeostasis of various phytohormones to be maintained. Moreover, the components of the BR signalosome interact with factors regulating plant reactions to environmental cues and stress conditions. This intricate network of interactions enables a rapid adaptation of plant metabolism to constantly changing environmental conditions.
“…Overexpression of the AtBS14b caused insensitivity to exogenously applied BRs. AtBS14b directly interacts with the Membrane Steroid-Binding Protein1 (MSBP1) at vesicular compartments, but not with BRI1 or BAK1 [ 96 ]. The MSBP1 protein is localized in the plasma membrane and endosomes, and is able to bind the BR ligand.…”
Section: The Br Signalosome—an Updatementioning
confidence: 99%
“…Transcription of the AtBS14b gene is down-regulated by BR in the BRI1-mediated process. AtBS14b acts via interacting with MSBP1 in the trans-Golgi network to enhance transport of MSBP1 to plasma membrane and its interaction with BAK1 [ 96 ] ( Figure 1 ).…”
Brassinosteroids (BRs) are a class of phytohormones, which regulate various processes during plant life cycle. Intensive studies conducted with genetic, physiological and molecular approaches allowed identification of various components participating in the BR signaling—from the ligand perception, through cytoplasmic signal transduction, up to the BR-dependent gene expression, which is regulated by transcription factors and chromatin modifying enzymes. The identification of new components of the BR signaling is an ongoing process, however an emerging view of the BR signalosome indicates that this process is interconnected at various stages with other metabolic pathways. The signaling crosstalk is mediated by the BR signaling proteins, which function as components of the transmembrane BR receptor, by a cytoplasmic kinase playing a role of the major negative regulator of the BR signaling, and by the transcription factors, which regulate the BR-dependent gene expression and form a complicated regulatory system. This molecular network of interdependencies allows a balance in homeostasis of various phytohormones to be maintained. Moreover, the components of the BR signalosome interact with factors regulating plant reactions to environmental cues and stress conditions. This intricate network of interactions enables a rapid adaptation of plant metabolism to constantly changing environmental conditions.
“…They showed longer petioles, larger rosette diameters, less rosette leaves and slender shoots (Fig 5A and 5C and S2 Fig). We further observed the elongated hypocotyls in all these over-expressing lines (Fig 5B and 5D) [14]. Yet, they were all sensitive to BRZ (brassinozole) that specifically inhibits BR biosynthesis (Fig 5D and S3 Fig).…”
Brassinosteroids (BRs) are essential hormones for plant growth and development. Enzymes DET2 and CYP90 family are responsible for BR biosynthesis in seed plants. Yet, their roles in non-seed plants are unknown. Here, we report the first functional study of
DET2
and all 4
CYP90
genes isolated from
Selaginella moellendorfii
.
Sm89026
(
SmCPD
) belonged to a clade with
CYP90A1
(
CPD
) and
CYP90B1
(
DWF4
) while
Sm182839
,
Sm233379
and
Sm157387
formed a distinct clade with
CYP90C1
(
ROT3
) and
CYP90D1
.
SmDET2
,
SmCPD
and
Sm157387
were highly expressed in both leaves and strobili while
Sm233379
was only highly expressed in the leaves but not strobili, implying their differential functions in a tissue-specific manner in
S
.
moellendorfii
. We showed that only
SmDET2
and
SmCPD
completely rescued Arabidopsis
det2
and
cpd
mutant phenotypes, respectively, suggestive of their conserved BR biosynthetic functions. However, neither
SmCPD
nor other
CYP90
genes rescued any other
cyp90
mutants. Yet overexpression of
Sm233379
altered plant fertility and BR response, which means that
Sm233379
is not an ortholog of any
CYP90
genes in Arabidopsis but appears to have a BR function in the
S
.
moellendorfii
leaves. This function is likely turned off during the development of the strobili. Our results suggest a dramatic functional divergence of CYP90 family in the non-seed plants. While some of them are functionally similar to that of seed plants, the others may be functionally distinct from that of seed plants, shedding light for future exploration.
“…The YFP signals generated by GsCBRLK/GsBET11a co‐expression were mainly observed on the PM, as well as on some Golgi‐like punctate structures (Figure 1c). GsBET11a is homologous to AtBET11 (Figure 2a), which was suggested to be a Golgi‐located Qc‐SNARE (Bubeck et al ., 2008; Bolaños‐Villegas et al ., 2015), and AtBET12 was targeted at Golgi/TGN membranes (Bolaños‐Villegas et al ., 2015; Chung et al ., 2018) as well as the vesicular compartments surrounding the PM (Zhu et al ., 2014). In the present study, we showed that GsBET11a appeared in the Golgi/TGN‐like punctate structures and the PM (Figure 1e; Figure S1b), and this enabled its interaction with the PM‐located GsCBRLK (Yang et al ., 2010).…”
Summary
Plants have evolved numerous receptor‐like kinases (RLKs) that modulate environmental stress responses. However, little is known regarding soybean (Glycine max) RLKs. We have previously identified that Glycine soja Ca2+/CAM‐binding RLK (GsCBRLK) is involved in salt tolerance. Here, we report that soluble NSF attachment protein receptor proteins BET1s mediate subcellular localization of calmodulin‐binding receptor‐like cytoplasmic kinases CRCK1s to modulate salt stress responses. Direct interaction between GsCBRLK and GsBET11a was initially identified via yeast two‐hybrid and bimolecular fluorescence complementation assays. Further analysis demonstrated conserved interaction between BET1s and CRCK1s. GsCBRLK interacted with all BET1 proteins in wild soybean (Glycine soja) and Arabidopsis, and GsBET11a strongly associated with GsCRCK1a–1d, but slightly with AtCRCK1. In addition, GsBET11a interacted with GsCBRLK via its C‐terminal transmembrane domain (TMD), where the entire TMD, not the sequence, was critical for the interaction. Moreover, the N‐terminal variable domain (VD) of GsCBRLK was responsible for interacting with GsBET11a, and the intensity of interaction between GsCBRLK/AtCRCK1 and GsBET11a was dependent on VD. Furthermore, GsBET11a was able to mediate the GsCBRLK subcellular localization via direct interaction with VD. Additionally, knockout of AtBET11 or AtBET12 individually did not alter GsCBRLK localization, while GsBET11a expression caused partial internalization of GsCBRLK from the plasma membrane (PM). We further suggest the necessity of GsCBRLK VD for its PM localization via N‐terminal truncation assays. Finally, GsBET11a was shown to confer enhanced salt stress tolerance when overexpressed in Arabidopsis and soybean. These results revealed the conserved and direct interaction between BET1s and CRCK1s, and suggested their involvement in salt stress responses.
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