2017
DOI: 10.1016/j.pbi.2017.07.002
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Plant mechanosensitive ion channels: an ocean of possibilities

Abstract: Mechanosensitive ion channels, transmembrane proteins that directly couple mechanical stimuli to ion flux, serve to sense and respond to changes in membrane tension in all branches of life. In plants, mechanosensitive channels have been implicated in the perception of important mechanical stimuli such as osmotic pressure, touch, gravity, and pathogenic invasion. Indeed, three established families of plant mechanosensitive ion channels play roles in cell and organelle osmoregulation and root mechanosensing—and … Show more

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Cited by 130 publications
(103 citation statements)
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“…Mechanosensitive ion channels are membrane-localized, tension-gated proteins that are activated upon membrane stretch, thus converting mechanical stimuli to ion transport (Basu & Haswell, 2017;Hamant & Haswell, 2017). Arabidopsis MID1-COMPLEMENTING ACTIVITY1 (MCA1) is a putative stretch-activated Ca 2+ channel (Nakagawa et al, 2007) (Fig.…”
Section: Reviewmentioning
confidence: 99%
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“…Mechanosensitive ion channels are membrane-localized, tension-gated proteins that are activated upon membrane stretch, thus converting mechanical stimuli to ion transport (Basu & Haswell, 2017;Hamant & Haswell, 2017). Arabidopsis MID1-COMPLEMENTING ACTIVITY1 (MCA1) is a putative stretch-activated Ca 2+ channel (Nakagawa et al, 2007) (Fig.…”
Section: Reviewmentioning
confidence: 99%
“…The homolog of MCA1 has also been characterized in maize and functions to coordinate organ growth and patterning, likely by transmitting extrinsic and intrinsic cues via Ca 2+ (Rosa et al, 2017). For a full overview of mechanosensitive ion channels other than MCA1, we highly recommended that readers refer to recent review articles by Hamilton et al (2015), Basu & Haswell (2017), and Hamant & Haswell (2017). For a full overview of mechanosensitive ion channels other than MCA1, we highly recommended that readers refer to recent review articles by Hamilton et al (2015), Basu & Haswell (2017), and Hamant & Haswell (2017).…”
Section: Reviewmentioning
confidence: 99%
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“…Each Ec MscS monomer contributes three transmembrane (TM) domains and a relatively large soluble cytoplasmic domain. Like other MscS‐like superfamily proteins, MSL1, MSL2, and MSL3 share a conserved region corresponding to the pore‐lining helix and about 100 amino acids of the cytoplasmic C‐terminus called the MscS domain (Basu & Haswell, , indicated in yellow in Figure ). Outside of this domain, the topology of organellar MSL channels differs from Ec MscS and from each other in a number of ways.…”
Section: Resultsmentioning
confidence: 99%
“…Each Ec MscS monomer contributes three transmembrane (TM) domains and a relatively large soluble cytoplasmic domain. Like other MscS-like superfamily proteins, MSL1, MSL2 and MSL3 share a conserved region corresponding to the pore-lining helix and about 100 amino acids of the cytoplasmic C-terminus called the MscS domain ((Basu and Haswell, 2017), indicated in yellow in Figure 1 ). Outside of this domain, the topology of organellar MSL channels differ from Ec MscS and from each other in a number of ways.…”
Section: Resultsmentioning
confidence: 99%