Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli

The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 20...
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Gespeichert in:

Autor*in:	Sebastian Jojoa-Cruz [verfasserIn] Adrienne E Dubin [verfasserIn] Wen-Hsin Lee [verfasserIn] Andrew B Ward [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2024

Schlagwörter:	cryoEM mechanotransduction ion channels

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 12(2024)
Übergeordnetes Werk:	volume:12 ; year:2024

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.93147

Katalog-ID:	DOAJ091472326

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allfieldsSound	10.7554/eLife.93147 doi (DE-627)DOAJ091472326 (DE-599)DOAJ6b02f796555742be94f58f6e2a2a0086 DE-627 ger DE-627 rakwb eng QH301-705.5 Sebastian Jojoa-Cruz verfasserin aut Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 2018). Interestingly, while OSCA1, 2, and 3 clades are activated by membrane stretch in cell-attached patches (i.e. they are stretch-activated channels), they differ in their ability to transduce membrane deformation induced by a blunt probe (poking). Here, in an effort to understand the domains contributing to mechanical signal transduction, we used cryo-electron microscopy to solve the structure of Arabidopsis thaliana (At) OSCA3.1, which, unlike AtOSCA1.2, only produced stretch- but not poke-activated currents in our initial characterization (Murthy et al., 2018). Mutagenesis and electrophysiological assessment of conserved and divergent putative mechanosensitive features of OSCA1.2 reveal a selective disruption of the macroscopic currents elicited by poking without considerable effects on stretch-activated currents (SAC). Our results support the involvement of the amphipathic helix and lipid-interacting residues in the membrane fenestration in the response to poking. Our findings position these two structural elements as potential sources of functional diversity within the family. cryoEM mechanotransduction ion channels Medicine R Science Q Biology (General) Adrienne E Dubin verfasserin aut Wen-Hsin Lee verfasserin aut Andrew B Ward verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 12(2024) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:12 year:2024 https://doi.org/10.7554/eLife.93147 kostenfrei https://doaj.org/article/6b02f796555742be94f58f6e2a2a0086 kostenfrei https://elifesciences.org/articles/93147 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2024
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authorswithroles_txt_mv	Sebastian Jojoa-Cruz @@aut@@ Adrienne E Dubin @@aut@@ Wen-Hsin Lee @@aut@@ Andrew B Ward @@aut@@
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callnumber-first	Q - Science
author	Sebastian Jojoa-Cruz
spellingShingle	Sebastian Jojoa-Cruz misc QH301-705.5 misc cryoEM misc mechanotransduction misc ion channels misc Medicine misc R misc Science misc Q misc Biology (General) Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli
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topic	misc QH301-705.5 misc cryoEM misc mechanotransduction misc ion channels misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli
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title_full	Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli
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title_sort	structure-guided mutagenesis of oscas reveals differential activation to mechanical stimuli
callnumber	QH301-705.5
title_auth	Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli
abstract	The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 2018). Interestingly, while OSCA1, 2, and 3 clades are activated by membrane stretch in cell-attached patches (i.e. they are stretch-activated channels), they differ in their ability to transduce membrane deformation induced by a blunt probe (poking). Here, in an effort to understand the domains contributing to mechanical signal transduction, we used cryo-electron microscopy to solve the structure of Arabidopsis thaliana (At) OSCA3.1, which, unlike AtOSCA1.2, only produced stretch- but not poke-activated currents in our initial characterization (Murthy et al., 2018). Mutagenesis and electrophysiological assessment of conserved and divergent putative mechanosensitive features of OSCA1.2 reveal a selective disruption of the macroscopic currents elicited by poking without considerable effects on stretch-activated currents (SAC). Our results support the involvement of the amphipathic helix and lipid-interacting residues in the membrane fenestration in the response to poking. Our findings position these two structural elements as potential sources of functional diversity within the family.
abstractGer	The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 2018). Interestingly, while OSCA1, 2, and 3 clades are activated by membrane stretch in cell-attached patches (i.e. they are stretch-activated channels), they differ in their ability to transduce membrane deformation induced by a blunt probe (poking). Here, in an effort to understand the domains contributing to mechanical signal transduction, we used cryo-electron microscopy to solve the structure of Arabidopsis thaliana (At) OSCA3.1, which, unlike AtOSCA1.2, only produced stretch- but not poke-activated currents in our initial characterization (Murthy et al., 2018). Mutagenesis and electrophysiological assessment of conserved and divergent putative mechanosensitive features of OSCA1.2 reveal a selective disruption of the macroscopic currents elicited by poking without considerable effects on stretch-activated currents (SAC). Our results support the involvement of the amphipathic helix and lipid-interacting residues in the membrane fenestration in the response to poking. Our findings position these two structural elements as potential sources of functional diversity within the family.
abstract_unstemmed	The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 2018). Interestingly, while OSCA1, 2, and 3 clades are activated by membrane stretch in cell-attached patches (i.e. they are stretch-activated channels), they differ in their ability to transduce membrane deformation induced by a blunt probe (poking). Here, in an effort to understand the domains contributing to mechanical signal transduction, we used cryo-electron microscopy to solve the structure of Arabidopsis thaliana (At) OSCA3.1, which, unlike AtOSCA1.2, only produced stretch- but not poke-activated currents in our initial characterization (Murthy et al., 2018). Mutagenesis and electrophysiological assessment of conserved and divergent putative mechanosensitive features of OSCA1.2 reveal a selective disruption of the macroscopic currents elicited by poking without considerable effects on stretch-activated currents (SAC). Our results support the involvement of the amphipathic helix and lipid-interacting residues in the membrane fenestration in the response to poking. Our findings position these two structural elements as potential sources of functional diversity within the family.
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title_short	Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli
url	https://doi.org/10.7554/eLife.93147 https://doaj.org/article/6b02f796555742be94f58f6e2a2a0086 https://elifesciences.org/articles/93147 https://doaj.org/toc/2050-084X
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Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli

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