PIEZO1

Piezo-type mechanosensitive ion channel component 1
Identifiers
Symbols	PIEZO1 ; DHS; FAM38A; Mib
External IDs	OMIM: 611184 HomoloGene: 124356 GeneCards: PIEZO1 Gene
Gene ontology Molecular function • cation channel activity • mechanically-gated ion channel activity Cellular component • endoplasmic reticulum • endoplasmic reticulum membrane • plasma membrane • integral component of membrane • endoplasmic reticulum-Golgi intermediate compartment membrane Biological process • cation transport • positive regulation of integrin activation • positive regulation of cell-cell adhesion mediated by integrin • regulation of membrane potential • detection of mechanical stimulus • cation transmembrane transport Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9780	234839
Ensembl	ENSG00000103335	ENSMUSG00000014444
UniProt	Q92508	n/a
RefSeq (mRNA)	NM_001142864	NM_001037298
RefSeq (protein)	NP_001136336	NP_001032375
Location (UCSC)	Chr 16: 88.72 – 88.79 Mb	Chr 8: 122.48 – 122.55 Mb
PubMed search

Piezo1 is a mechanosensitive ion channel protein that in humans is encoded by the gene PIEZO1. Piezo1 and its close homolog piezo2 were cloned in 2010, using an siRNA-based screen for mechanosensitive ion channels.^[1] Piezo1 and piezo2 share 47% identity with each other and they have no similarity to any other protein and contain no known protein domains. They are predicted to have 24-36 transmembrane domains, depending on the prediction algorithm used. In the original publication the authors were careful not to call the piezo proteins ion channels, but a more recent study by the same lab convincingly demonstrated that indeed piezo1 is the pore forming subunit of a mechanosensitive channel.^[2] Piezo1 is expressed in the lungs, bladder and skin, where mechanosensation has important biological roles. Unlike Piezo2 which is highly expressed in sensory dorsal root ganglia, piezo1 is not expressed in sensory neurons.^[1] Piezo1 is also found in red blood cells, and gain of function mutations in the channels are associated with hereditary xerocytosis or stomatocytosis.^[3][4][5]

References

1. Coste B, Mathur J, Schmidt M, Earley TJ, Ranade S, Petrus MJ, Dubin AE, Patapoutian A (2010). "Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels". Science 330: 55–60. doi:10.1126/science.1193270. PMC 3062430. PMID 20813920.
2. Coste B, Xiao B, Santos JS, Syeda R, Grandl J, Spencer KS, Kim SE, Schmidt M, Mathur J, Dubin AE, Montal M, Patapoutian A (2012). "Piezo proteins are pore-forming subunits of mechanically activated channels.". Nature 483: 176–81. doi:10.1038/nature10812. PMC 3297710. PMID 22343900.
3. Zarychanski R, Schulz VP, Houston BL, Maksimova Y, Houston DS, Smith B, Rinehart J, Gallagher PG (2012). "Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis.". Blood 120: 1908–15. doi:10.1182/blood-2012-04-422253. PMID 22529292.
4. Bae C, Gnanasambandam R, Nicolai C, Sachs F, Gottlieb PA. (2013). "Xerocytosis is caused by mutations that alter the kinetics of the mechanosensitive channel PIEZO1." 110: E1162-8. doi:10.1073/pnas.1219777110. PMID 23487776.
5. Albuisson J, Murthy SE, Bandell M, Coste B, Louis-Dit-Picard H, Mathur J, Fénéant-Thibault M, Tertian G, de Jaureguiberry JP, Syfuss PY, Cahalan S, Garçon L, Toutain F, Simon Rohrlich P, Delaunay J, Picard V, Jeunemaitre X, Patapoutian A. (2013). "Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels.". Nature Communications 4: 1884. doi:10.1038/ncomms2899. PMID 23695678.