Lateral Movements of Membrane Glycoproteins Restricted by Dynamic Cytoplasmic Barriers
- 29 November 1991
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 254 (5036), 1379-1382
- https://doi.org/10.1126/science.1835798
Abstract
Cell membranes often are patchy, composed of lateral domains. These domains may be formed by barriers within or on either side of the membrane bilayer. Major histocompatibility complex (MHC) class 1 molecules that were either transmembrane- (H-2Db) or glycosylphosphatidylinositol (GPI)-anchored (Qa2) were labeled with antibody-coated gold particles and moved across the cell surface with a laser optical tweezers until they encountered a barrier, the barrier-free path length (BFP). At room temperature, the BFPs of Qa2 and H-2Db were 1.7 +/- 0.2 and 0.6 +/- 0.1 (micrometers +/- SEM), respectively. Barriers persisted at 34 degrees C, although the BFP for both MHC molecules was fivefold greater at 34 degrees C than at 23 degrees C. This indicates that barriers to lateral movement are primarily on the cytoplasmic half of the membrane and are dynamic.Keywords
This publication has 15 references indexed in Scilit:
- Preferential attachment of membrane glycoproteins to the cytoskeleton at the leading edge of lamella.The Journal of cell biology, 1991
- Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains.The Journal of cell biology, 1991
- Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with Nanovid microscopy.The Journal of cell biology, 1991
- Molecules Related to Class-I Major Histocompatibility Complex AntigensAnnual Review of Immunology, 1990
- Spectrin: a structural mediator between diverse plasma membrane proteins and the cytoplasmCurrent Opinion in Cell Biology, 1990
- Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movementsNature, 1989
- Lateral mobility of proteins and lipids in the red cell membrane and the activation of adenylate cyclase by β‐adrenergic receptorsFEBS Letters, 1988
- A single gene encodes soluble and membrane-bound forms of the major histocompatibility Qa-2 antigen: Anchoring of the product by a phospholipid tailCell, 1987
- Lateral Diffusion of Proteins in MembranesAnnual Review of Physiology, 1987
- Observation of a single-beam gradient force optical trap for dielectric particlesOptics Letters, 1986