Calmodulin binding to Arabidopsis cyclic nucleotide gated ion channels

Abdel-Hamid, Huda; Chin, Kimberley; Shahinas, Dea; Moeder, Wolfgang; Yoshioka, Keiko

doi:10.4161/psb.5.9.12676

Cited by 8 publications

(3 citation statements)

References 29 publications

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“…For example, CaM was related to K þ channel gating activities and thus had a probable impact in controlling K þ fluxes (Hoeflich and Ikura, 2002). Various Ca 2þ channels are known to be controlled by CaM (Abdel-Hamid et al, 2010). Our previous study had found that 1): Al 3þ pre-treatment increased F accumulation in tea plants; 2) plasma membrane Ca 2þ -ATPase activities was significantly decreased about by 54% in tea roots exposed to 1.05 mM Al 3þ in comparison with control (S Fig.…”

Section: Introductionmentioning

confidence: 81%

Ca 2+ and CaM are involved in Al 3+ pretreatment-promoted fluoride accumulation in tea plants ( Camellia sinesis L.)

Zhang

Gao

et al. 2015

Plant Physiology and Biochemistry

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Section: Introductionmentioning

confidence: 81%

Ca 2+ and CaM are involved in Al 3+ pretreatment-promoted fluoride accumulation in tea plants ( Camellia sinesis L.)

Zhang

Gao

et al. 2015

Plant Physiology and Biochemistry

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“…They play a role in signal transduction in animals and are also present in other non-neuronal tissues [ 102 ]. These ion transport proteins have also been identified in plants [ 74 , 103 , 104 ] and have been known to be involved in a variety of biological processes, ranging from plant development and stress tolerance, disease resistance [ 105 , 106 ], thermal tolerance [ 107 ], and salt stress [ 108 ]. These channels are typically localized at the plasma membrane and in the model plant A. thaliana, which consists of 20 family members [ 109 ].…”

Section: Plant Ion Channelsmentioning

confidence: 99%

Deciphering the Role of Ion Channels in Early Defense Signaling against Herbivorous Insects

Gandhi

Kariyat

Harikishore

et al. 2021

Cells

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Plants and insect herbivores are in a relentless battle to outwit each other. Plants have evolved various strategies to detect herbivores and mount an effective defense system against them. These defenses include physical and structural barriers such as spines, trichomes, cuticle, or chemical compounds, including secondary metabolites such as phenolics and terpenes. Plants perceive herbivory by both mechanical and chemical means. Mechanical sensing can occur through the perception of insect biting, piercing, or chewing, while chemical signaling occurs through the perception of various herbivore-derived compounds such as oral secretions (OS) or regurgitant, insect excreta (frass), or oviposition fluids. Interestingly, ion channels or transporters are the first responders for the perception of these mechanical and chemical cues. These transmembrane pore proteins can play an important role in plant defense through the induction of early signaling components such as plasma transmembrane potential (Vm) fluctuation, intracellular calcium (Ca2+), and reactive oxygen species (ROS) generation, followed by defense gene expression, and, ultimately, plant defense responses. In recent years, studies on early plant defense signaling in response to herbivory have been gaining momentum with the application of genetically encoded GFP-based sensors for real-time monitoring of early signaling events and genetic tools to manipulate ion channels involved in plant-herbivore interactions. In this review, we provide an update on recent developments and advances on early signaling events in plant-herbivore interactions, with an emphasis on the role of ion channels in early plant defense signaling.

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“…In response to a Ca 2+ signal, CaM interacts with and regulates various proteins including calmodulin-dependent protein kinases and phosphatases, cytoskeletal proteins, ion channels, and pumps. Unraveling its diverse roles in activation mechanisms and target recognition has received extensive attention [ 1 , 2 , 3 , 4 , 5 , 6 , 7 ]. CaM contains two globular domains connected by a flexible linker [ 8 , 9 ].…”

Section: Introductionmentioning

confidence: 99%

The Recognition of Calmodulin to the Target Sequence of Calcineurin—A Novel Binding Mode

2017

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Calcineurin (CaN) is a Ca2+/calmodulin-dependent Ser/Thr protein phosphatase, which plays essential roles in many cellular and developmental processes. CaN comprises two subunits, a catalytic subunit (CaN-A, 60 kDa) and a regulatory subunit (CaN-B, 19 kDa). CaN-A tightly binds to CaN-B in the presence of minimal levels of Ca2+, but the enzyme is inactive until activated by CaM. Upon binding to CaM, CaN then undergoes a conformational rearrangement, the auto inhibitory domain is displaced and thus allows for full activity. In order to elucidate the regulatory role of CaM in the activation processes of CaN, we used NMR spectroscopy to determine the structure of the complex of CaM and the target peptide of CaN (CaNp). The CaM/CaNp complex shows a compact ellipsoidal shape with 8 α-helices of CaM wrapping around the CaNp helix. The RMSD of backbone and heavy atoms of twenty lowest energy structures of CaM/CaNp complex are 0.66 and 1.14 Å, respectively. The structure of CaM/CaNp complex can be classified as a novel binding mode family 1–18 with major anchor residues Ile396 and Leu413 to allocate the largest space between two domains of CaM. The relative orientation of CaNp to CaM is similar to the CaMKK peptide in the 1–16 binding mode with N- and C-terminal hydrophobic anchors of target sequence engulfed in the hydrophobic pockets of the N- and C-domain of CaM, respectively. In the light of the structural model of CaM/CaNp complex reported here, we provide new insight in the activation processes of CaN by CaM. We propose that the hydrophobic interactions between the Ca2+-saturated C-domain and C-terminal half of the target sequence provide driving forces for the initial recognition. Subsequent folding in the target sequence and structural readjustments in CaM enhance the formation of the complex and affinity to calcium. The electrostatic repulsion between CaM/CaNp complex and AID may result in the displacement of AID from active site for full activity.

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Calmodulin binding to Arabidopsis cyclic nucleotide gated ion channels

Cited by 8 publications

References 29 publications

Ca 2+ and CaM are involved in Al 3+ pretreatment-promoted fluoride accumulation in tea plants ( Camellia sinesis L.)

Ca 2+ and CaM are involved in Al 3+ pretreatment-promoted fluoride accumulation in tea plants ( Camellia sinesis L.)

Deciphering the Role of Ion Channels in Early Defense Signaling against Herbivorous Insects

The Recognition of Calmodulin to the Target Sequence of Calcineurin—A Novel Binding Mode

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