Visualizing Individual Rhodopsin (a G Protein-Coupled Receptor) Molecules in Native Disk and Reconstituted Membranes via Atomic Force Microscopy

نویسندگان

  • Eugene J. Choi
  • Albert J. Jin
  • Shui-Lin Niu
  • Paul D. Smith
  • Burton J. Litman
چکیده

Individual rhodopsin molecules have been resolved with atomic force microscopy as both monomers and various oligomeric organizations that are sensitively dependent upon the physical state of membranes and environmental conditions. In intact native disk membranes, rhodopsin molecules are observed as randomly dispersed monomers and small oligomers. In reconstituted rhodopsin-DPPC (dipalmitoylphosphatidylcholine, di16:0-PC) membranes, phase separation of lipid and rhodopsin results in paracrystalline arrays of rhodopsin molecules. Since the coupling of rhodopsin and G proteins is an essential step in visual transduction, the results from this study could provide further insight into the structural relationship of rhodopsin to its function in vision and may have applications in nanotechnology.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes.

Rhodopsin, the prototypical G-protein-coupled receptor, which is densely packed in the disc membranes of rod outer segments, was proposed to function as a monomer. However, a growing body of evidence indicates dimerization and oligomerization of numerous G-protein-coupled receptors, and atomic force microscopy images revealed rows of rhodopsin dimers in murine disc membranes. In this work we de...

متن کامل

The G protein-coupled receptor rhodopsin in the native membrane.

The higher-order structure of G protein-coupled receptors (GPCRs) in membranes may involve dimerization and formation of even larger oligomeric complexes. Here, we have investigated the organization of the prototypical GPCR rhodopsin in its native membrane by electron and atomic force microscopy (AFM). Disc membranes from mice were isolated and observed by AFM at room temperature. In all experi...

متن کامل

Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes.

G protein-coupled receptors (GPCRs), which constitute the largest and structurally best conserved family of signaling molecules, are involved in virtually all physiological processes. Crystal structures are available only for the detergent-solubilized light receptor rhodopsin. In addition, this receptor is the only GPCR for which the presumed higher order oligomeric state in native membranes ha...

متن کامل

Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

Rhodopsin in the disk membranes of rod outer segments serves as the dim-light photoreceptor and is a prototypic member of a G protein-coupled receptor family. Electron and atomic-force microscopy indicate that rhodopsin is present as dimers in the native membranes. Here, we have expressed the protein, opsin, in COS1 cells and have studied its molecular state by using FRET and by intermolecular ...

متن کامل

Different properties of the native and reconstituted heterotrimeric G protein transducin.

Visual signal transduction serves as one of the best understood G protein-coupled receptor signaling systems. Signaling is initiated when a photon strikes rhodopsin (Rho) causing a conformational change leading to productive interaction of this G protein-coupled receptor with the heterotrimeric G protein, transducin (Gt). Here we describe a new method for Gt purification from native bovine rod ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2004