title: Atomic force microscopy imaging of the structure of the motor protein prestin reconstituted into an artificial lipid bilayer.
abstract: Prestin is the motor protein of cochlear outer hair cells and is essential for mammalian hearing. The present study aimed to clarify the structure of prestin by atomic force microscopy (AFM). Prestin was purified from Chinese hamster ovary cells which had been modified to stably express prestin, and then reconstituted into an artificial lipid bilayer. Immunofluorescence staining with anti-prestin antibody showed that the cytoplasmic side of prestin was possibly face up in the reconstituted lipid bilayer. AFM observation indicated that the cytoplasmic surface of prestin was ring-like with a diameter of about 11 nm.
authors.affiliation: Department of Bioengineering and Robotics, Tohoku University, Sendai, Japan.
authors.forename: Shun
authors.initials: S
authors.lastname: Kumano
authors.forename: Michio
authors.initials: M
authors.lastname: Murakoshi
authors.forename: Koji
authors.initials: K
authors.lastname: Iida
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Hamana
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Wada
mesh_terms: D000818:Animals; D015153:Blotting, Western; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D008051:Lipid Bilayers / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods*; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D008051:Lipid Bilayers; D020409:Molecular Motor Proteins