Evidence for in vivo interactions between dehydrins and the aquaporin AtPIP2B

Hernández-Sánchez, Itzell E.; Maruri-López, Israel; Molphe-Balch, Eugenio Pérez; Becerra-Flora, Alicia; Jaimes-Miranda, Fabiola; Jiménez-Bremont, Juan Francisco

doi:10.1016/j.bbrc.2019.01.095

Cited by 25 publications

(20 citation statements)

References 44 publications

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“…Dehydrins and aquaporins are also major components in plant stress defense systems 31,32 . Nodulin 26-like intrinsic proteins (NIP) group I functions as aquaglyceroporins mediating the flux of water and glycerol, while its phosphorylation level can be induced by water deficit resulting in enhanced transport activity 32 .…”

Section: Stress Protection-related Phosphorylated Proteins Associatedmentioning

confidence: 99%

Protein phosphorylation associated with drought priming-enhanced heat tolerance in a temperate grass species

Zhang¹,

Zhuang²,

Liu³

et al. 2020

Hortic Res

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Protein phosphorylation is known to play crucial roles in plant tolerance to individual stresses, but how protein phosphorylation is associated with cross-stress tolerance, particularly drought priming-enhanced heat tolerance is largely unknown. The objectives of the present study were to identify phosphorylated proteins and phosphorylation sites that were responsive to drought priming and to determine whether drought priming-enhanced heat tolerance in temperate grass species involves changes in protein phosphorylation. Comparative analysis of phosphoproteomic profiles was performed on leaves of tall fescue (Festuca arundinacea) exposed to heat stress (38/33 °C, day/night) with or without drought priming. A total of 569 differentially regulated phosphoproteins (DRPs) with 1098 phosphorylation sites were identified in response to drought priming or heat stress individually or sequentially. Most DRPs were nuclear-localized and cytosolic proteins. Motif analysis detected [GS], [DSD], and [S..E] as major phosphorylation sites in casein kinase-II and mitogen-activated protein kinases regulated by drought priming and heat stress. Functional annotation and gene ontology analysis demonstrated that DRPs in response to drought priming and in drought-primed plants subsequently exposed to heat stress were mostly enriched in four major biological processes, including RNA splicing, transcription control, stress protection/defense, and stress perception/signaling. These results suggest the involvement of post-translational regulation of the aforementioned biological processes and signaling pathways in drought priming memory and cross-tolerance with heat stress in a temperate grass species.

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Section: Stress Protection-related Phosphorylated Proteins Associatedmentioning

confidence: 99%

Protein phosphorylation associated with drought priming-enhanced heat tolerance in a temperate grass species

Zhang¹,

Zhuang²,

Liu³

et al. 2020

Hortic Res

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“…A dehydrin LEAP from the cactus Opuntia streptacantha , when overexpressed in Arabidopsis , led to enhanced cold tolerance [ 88 ]. This dehydrin as well as three from Arabidopsis (COR47, ERD10, and RAB18; see Table S1 for details for abbreviations) were found to bind to the aquaporin AtPIP2B (At2g37170) on the inside face of the plasma membrane [ 89 ] ( Figure 6 ). Because both AtPIP2B and the dehydrins influence cold tolerance positively when overexpressed (a parity of phenotypes ( Figure 1 d)), these authors speculate that there may be a functional relationship in the LEAP–client protein interaction because aquaporins are known to be susceptible to denaturation that can be minimized in another species (at least during heat stress) by association with a chaperonin (ALPHA-CRYSTALLIN) [ 90 ].…”

Section: Introductionmentioning

confidence: 99%

“…Because both AtPIP2B and the dehydrins influence cold tolerance positively when overexpressed (a parity of phenotypes ( Figure 1 d)), these authors speculate that there may be a functional relationship in the LEAP–client protein interaction because aquaporins are known to be susceptible to denaturation that can be minimized in another species (at least during heat stress) by association with a chaperonin (ALPHA-CRYSTALLIN) [ 90 ]. If we assume that the mechanism of aquaporin denaturation due to supra- or sub-optimal temperature perturbations is the same as in planta, AtPIP2B association with the cactus dehydrin, or any of the three con-specific dehydrins, may protect AtPIP2B from cold stress denaturation in the same manner as ALPHA-CRYSTALLIN during heat stress [ 89 ]. However, the dehydrins bind only to the inside face of the aquaporin/plasma membrane ( Figure 6 ) while the aquaporin denatured by heat stress converted predominantly alpha-helical conformations to predominantly beta-sheets when denatured [ 90 ].…”

Section: Introductionmentioning

confidence: 99%

“…Both the dehydrin and the aquaporin are degraded in this manner, reducing the water channel abundance in the plasma membrane of the roots such that hydrolytic conductivity between the plant and the soil is reduced ([ 113 ]; Figure 12 ). Apparently, the role of dehydrin binding to aquaporins varies depending on the stress imposed because, during cold stress [ 89 ], dehydrin binding to AtPIP2B stabilized the water channel in the membrane to improve cold tolerance ( Figure 6 ).…”

Section: Introductionmentioning

confidence: 99%

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Late Embryogenesis Abundant Protein–Client Protein Interactions

Dirk

Abdel

Ahmad

et al. 2020

Plants

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The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs providing a shield molecule function, possibly by instigating liquid-liquid phase separations. Some LEAPs bind directly to their client proteins, exerting a holdase-type chaperonin function. Finally, instances of LEAP–client protein interactions have been documented, where the LEAP modulates (interferes with) the function of the client protein, acting as a surreptitious rheostat of cellular homeostasis. From the examples identified to date, it is apparent that client protein modulation also serves to mitigate stress. While some LEAPs can physically bind and protect client proteins, some apparently bind to assist the degradation of the client proteins with which they associate. Documented instances of LEAP–client protein binding, even in the absence of stress, brings to the fore the necessity of identifying how the LEAPs are degraded post-stress to render them innocuous, a first step in understanding how the cell regulates their abundance.

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“…The plant aquaporins (AQPs) are part of the Major Intrinsic Proteins (MIPs) family that are integral α-helical proteins and allow passive water and neutral solute bidirectional transport across biological membranes and, also have a significant role in cell response to cold stress (Rouge and Barre, 2008;Hernandez-Sanchez et al, 2019) and to osmotic stress (Balarynová et al, 2018), also are important during leaf and petal movements, cell elongation, reproduction, and seed germination (Maurel, 2007).…”

Section: Introductionmentioning

confidence: 99%

Plant Aquaporins

Curticăpean

2019

Acta Biologica Marisiensis

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This mini-review briefly presents the main types of plant aquaporins, highlighting their importance for different plant species and for plant cellular functions. Aquaporins (AQPs), families of water channel proteins (WCPs) are transmembrane proteins that are present in prokaryotes, animals, plants, and humans. The plant aquaporins are part of the Major Intrinsic Proteins (MIPs) family which resides in the following plant organs: roots, stems, leaves, flowers, fruits, and seeds. According to the sub-cellular localization, to their sequence homologies and to their phylogenetic distribution, plant aquaporins have been divided in five subgroups: (a) plasma membrane intrinsic proteins (PIPs); (b) tonoplast intrinsic proteins (TIPs); (c) Nodulin26-like intrinsic membrane proteins (NIPs); (d) small basic intrinsic proteins (SIPs) and (e) uncharacterized intrinsic proteins (XIPs). Different subclasses of the plant aquaporins allow several types of transport using: water, glycerol, urea, hydrogen peroxide, organic acids, ethanol, methanol, arsenite, lactic acid, and gaseous compounds. Plant aquaporins have a significant role in cell response to cold stress, photosynthesis, plant growth, cell elongation, reproduction, and seed germination.

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Evidence for in vivo interactions between dehydrins and the aquaporin AtPIP2B

Cited by 25 publications

References 44 publications

Protein phosphorylation associated with drought priming-enhanced heat tolerance in a temperate grass species

Protein phosphorylation associated with drought priming-enhanced heat tolerance in a temperate grass species

Late Embryogenesis Abundant Protein–Client Protein Interactions

Plant Aquaporins

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