Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations

Li, Jinyuan Vero; Ng, Chai Ann; Cheng, Delfine; Zhou, Zijing; Yao, Mingxi; Guo, Yang; Yu, Ze‐Yan; Ramaswamy, Yogambha; Ju, Lining Arnold; Kuchel, Philip W.; Feneley, Michael P.; Fatkin, Diane; Cox, Charles D.

doi:10.1038/s42003-021-02528-w

Cited by 18 publications

(13 citation statements)

References 78 publications

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“…Polyclonal rabbit and monoclonal mouse anti-Piezo1 was from Novus Biologicals (NBP1-78446 and NBP2-75617); both have been validated by Piezo1 knockdown/knockoff experiments ( 15 , 78 ). For all Piezo1 localization quantifications, the monoclonal NBP2-75617 antibody was used.…”

Section: Methodsmentioning

confidence: 99%

Force- and cell state–dependent recruitment of Piezo1 drives focal adhesion dynamics and calcium entry

et al. 2022

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Mechanosensing is an integral part of many physiological processes including stem cell differentiation, fibrosis, and cancer progression. Two major mechanosensing systems—focal adhesions and mechanosensitive ion channels—can convert mechanical features of the microenvironment into biochemical signals. We report here unexpectedly that the mechanosensitive calcium-permeable channel Piezo1, previously perceived to be diffusive on plasma membranes, binds to matrix adhesions in a force-dependent manner, promoting cell spreading, adhesion dynamics, and calcium entry in normal but not in most cancer cells tested except some glioblastoma lines. A linker domain in Piezo1 is needed for binding to adhesions, and overexpression of the domain blocks Piezo1 binding to adhesions, decreasing adhesion size and cell spread area. Thus, we suggest that Piezo1 is a previously unidentified component of focal adhesions in nontransformed cells that catalyzes adhesion maturation and growth through force-dependent calcium signaling, but this function is absent in most cancer cells.

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Section: Methodsmentioning

confidence: 99%

Force- and cell state–dependent recruitment of Piezo1 drives focal adhesion dynamics and calcium entry

et al. 2022

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“…Polyclonal Rabbit and monoclonal mouse anti-Piezo1 was from Novus Biologicals (NBP1-78446, NBP2- 75617), both have been validated by Piezo1 knock down/knock off experiments( 15, 75 ). For all Piezo1 localization quantifications, the monoclonal NBP2-75617 antibody was used.…”

Section: Methodsmentioning

confidence: 99%

Force-dependent recruitment of Piezo1 drives adhesion maturation and calcium entry in normal but not tumor cells

Yao

Tijore

Cox

et al. 2020

Preprint

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Piezo1 is a mechanosensitive Ca 2+ -permeable channel that has been implicated in a number of mechanosensing processes. It is diffusive on plasma membranes and activated by local membrane tension changes yet recent data suggest that Piezo1 activity is tightly coupled to the integrin-mediated actin cytoskeleton through a poorly understood mechanism. In our studies, we found that Piezo1 stably localizes to RGD matrix adhesions in normal but not in transformed cells. Piezo1 binding requires contractility and triggers local Ca 2+ entry during adhesion formation and turnover. In transformed cells, Piezo1 level does not affect adhesion morphology; and there is no detectable Ca 2+ influx around adhesions. Based upon these findings, we suggest that Piezo1 is a novel component of integrin-based adhesions in non-transformed cells and contributes to the distinct mechanosensing and Ca 2+ signaling in normal vs transformed cells.Concentration of Piezo1 at adhesions is a key factor underlying Piezo1's physiological functions.

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“…Thus, other mechanisms may contribute to shearing force-induced ENaC activation. Notably, Li et al (2021) indicated that the status of N-linked glycosylated PIEZO1 is critical for membrane trafficking. The N-glycan of PIEZO1 may interact with other membrane proteins or the ECM molecules, which suggests an extra ECM-modulating mechanism to regulate mechanosensitivity.…”

Section: The Role Of Ecm In the Force-from-tether Modelmentioning

confidence: 99%

Force From Filaments: The Role of the Cytoskeleton and Extracellular Matrix in the Gating of Mechanosensitive Channels

Chuang

Chen

2022

Front. Cell Dev. Biol.

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The senses of proprioception, touch, hearing, and blood pressure on mechanosensitive ion channels that transduce mechanical stimuli with high sensitivity and speed. This conversion process is usually called mechanotransduction. From nematode MEC-4/10 to mammalian PIEZO1/2, mechanosensitive ion channels have evolved into several protein families that use variant gating models to convert different forms of mechanical force into electrical signals. In addition to the model of channel gating by stretching from lipid bilayers, another potent model is the opening of channels by force tethering: a membrane-bound channel is elastically tethered directly or indirectly between the cytoskeleton and the extracellular molecules, and the tethering molecules convey force to change the channel structure into an activation form. In general, the mechanical stimulation forces the extracellular structure to move relative to the cytoskeleton, deforming the most compliant component in the system that serves as a gating spring. Here we review recent studies focusing on the ion channel mechanically activated by a tethering force, the mechanotransduction-involved cytoskeletal protein, and the extracellular matrix. The mechanosensitive channel PIEZO2, DEG/ENaC family proteins such as acid-sensing ion channels, and transient receptor potential family members such as NompC are discussed. State-of-the-art techniques, such as polydimethylsiloxane indentation, the pillar array, and micropipette-guided ultrasound stimulation, which are beneficial tools for exploring the tether model, are also discussed.

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Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations

Cited by 18 publications

References 78 publications

Force- and cell state–dependent recruitment of Piezo1 drives focal adhesion dynamics and calcium entry

Force- and cell state–dependent recruitment of Piezo1 drives focal adhesion dynamics and calcium entry

Force-dependent recruitment of Piezo1 drives adhesion maturation and calcium entry in normal but not tumor cells

Force From Filaments: The Role of the Cytoskeleton and Extracellular Matrix in the Gating of Mechanosensitive Channels

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