title: Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: history, properties, mechanisms and pharmacology.
abstract: Sensing the energy from mechanical inputs is ubiquitous--and perhaps the oldest form of biological energy transduction. However, the tools available to probe the mechanisms of transduction are far fewer than for the chemical and electric field sensitive transducers. The one pharmacological tool available for mechansensitive ion channels (MSCs) is a peptide (GsMTx-4) isolated from venom of the tarantula, Grammostola spatulata, that blocks cationic MSCs found in non-specialized eukaryotic tissues. In this review, we summarize the current knowledge of GsMTx-4, and discuss the inevitable crosstalk between the MSC behavior and the mechanical properties of the cell cortex.
authors.affiliation: Center for Single Molecule Biophysics and The Department of Physiology and Biophysics, SUNY at Buffalo, Buffalo, NY 14214, USA. bowman@buffalo.edu
authors.forename: Charles L
authors.initials: CL
authors.lastname: Bowman
authors.forename: Philip A
authors.initials: PA
authors.lastname: Gottlieb
authors.forename: Thomas M
authors.initials: TM
authors.lastname: Suchyna
authors.forename: Yolanda K
authors.initials: YK
authors.lastname: Murphy
authors.forename: Frederick
authors.initials: F
authors.lastname: Sachs
mesh_terms: D000818:Animals; D001483:Base Sequence; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D015640:Ion Channel Gating / Q000187:drug effects / Q000502:physiology; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D013111:Spider Venoms / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D036341:Intercellular Signaling Peptides and Proteins; C411249:MTx4 protein, Grammostola spatulata; D010455:Peptides; D013111:Spider Venoms