The stomatin-domain defines a family of proteins that are found in all classes of life. The ubiquity of stomatin-family proteins and their high degree of homology suggest that they have a unifying cellular function, which has yet to be defined. The five stomatin family proteins in mammals show varying expression patterns and different sub-cellular distributions. In surveying the relevant literature, three common themes emerge; stomatin family members are oligomeric; they mostly localise to membrane domains; and in many cases, they have been shown to modulate ion channel activity. How oligomerisation and membrane localisation contribute to the modulation of channel function is unclear to date. Future studies into the precise structure and mechanism of stomatin-like proteins need to address these important questions to clarify the detailed cellular function of stomatin-domain containing proteins.
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A Conserved Role for Stomatin Domain Genes in Olfactory Behavior.
eNeuro
March 2023
Department of Biological Sciences, Southern Methodist University, Dallas, Texas 75275
The highly-conserved stomatin domain has been identified in genes throughout all classes of life. In animals, different stomatin domain-encoding genes have been implicated in the function of the kidney, red blood cells, and specific neuron types, although the underlying mechanisms remain unresolved. In one well-studied example of stomatin domain gene function, the gene and its mouse homolog are required for the function of mechanosensory neurons, where they modulate the activity of mechanosensory ion channels on the plasma membrane.
View Article and Find Full Text PDFExpression pattern of Stomatin-domain proteins in the peripheral olfactory system.
Sci Rep
July 2022
Neurobiology Group, SISSA, Scuola Internazionale Superiore di Studi Avanzati, 34136, Trieste, Italy.
Recent data show that Stomatin-like protein 3 (STOML3), a member of the stomatin-domain family, is expressed in the olfactory sensory neurons (OSNs) where it modulates both spontaneous and evoked action potential firing. The protein family is constituted by other 4 members (besides STOML3): STOM, STOML1, STOML2 and podocin. Interestingly, STOML3 with STOM and STOML1 are expressed in other peripheral sensory neurons: dorsal root ganglia.
View Article and Find Full Text PDFTuning Piezo ion channels to detect molecular-scale movements relevant for fine touch.
Nat Commun
March 2014
Department of Neuroscience, Max-Delbrück Center for Molecular Medicine, Robert-Rössle Straße 10, D-13092 Berlin, Germany.
In sensory neurons, mechanotransduction is sensitive, fast and requires mechanosensitive ion channels. Here we develop a new method to directly monitor mechanotransduction at defined regions of the cell-substrate interface. We show that molecular-scale (~13 nm) displacements are sufficient to gate mechanosensitive currents in mouse touch receptors.
View Article and Find Full Text PDFSubunit-specific inhibition of acid sensing ion channels by stomatin-like protein 1.
J Physiol
February 2014
Department of Neuroscience, Growth Factor & Regeneration Group, Max-Delbrueck Center for Molecular Medicine, Robert-Roessle Strasse 10, D-13092 Berlin, Germany. or
There are five mammalian stomatin-domain genes, all of which encode peripheral membrane proteins that can modulate ion channel function. Here we examined the ability of stomatin-like protein 1 (STOML1) to modulate the proton-sensitive members of the acid-sensing ion channel (ASIC) family. STOML1 profoundly inhibits ASIC1a, but has no effect on the splice variant ASIC1b.
View Article and Find Full Text PDFStomatin-domain protein interactions with acid-sensing ion channels modulate nociceptor mechanosensitivity.
J Physiol
November 2013
G. R. Lewin: Department of Neuroscience, Max-Delbrück Center for Molecular Medicine, Robert-Rössle Str. 10, D-13125, Berlin, Germany.
Acid-sensing ion channels (ASICs) and their interaction partners of the stomatin family have all been implicated in sensory transduction. Single gene deletion of asic3, asic2, stomatin, or stoml3 all result in deficits in the mechanosensitivity of distinct cutaneous afferents in the mouse. Here, we generated asic3(-/-):stomatin(-/-), asic3(-/-):stoml3(-/-) and asic2(-/-):stomatin(-/-) double mutant mice to characterize the functional consequences of stomatin-ASIC protein interactions on sensory afferent mechanosensitivity.
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