Association of spectrin with its membrane attachment site restricts lateral mobility of human erythrocyte integral membrane proteins

1978 ◽  
Vol 8 (2) ◽  
pp. 215-221 ◽  
Author(s):  
Velia Fowler ◽  
Vann Bennett
Keyword(s):  
Membrane Proteins ◽  
Human Erythrocyte ◽  
Attachment Site ◽  
Integral Membrane Proteins ◽  
Lateral Mobility ◽  
Membrane Attachment

Lateral mobility of human erythrocyte integral membrane proteins

Nature ◽  
1977 ◽  
Vol 268 (5615) ◽  
pp. 23-26 ◽  
Author(s):  
Velia Fowler ◽  
Daniel Branton
Keyword(s):  
Membrane Proteins ◽  
Human Erythrocyte ◽  
Integral Membrane Proteins ◽  
Lateral Mobility

Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein

Science ◽  
1988 ◽  
Vol 240 (4860) ◽  
pp. 1780-1782 ◽  
Author(s):  
BM Phelps ◽  
P Primakoff ◽  
DE Koppel ◽  
MG Low ◽  
DG Myles
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Diffusion Rate ◽  
Lateral Diffusion ◽  
Surface Protein ◽  
Integral Membrane Proteins ◽  
Testicular Sperm ◽  
Lateral Mobility ◽  
Sperm Membrane ◽  
Lipid Diffusion

The rate of lateral diffusion of integral membrane proteins is constrained in cells, but the constraining factors for most membrane proteins have not been defined. PH-20, a sperm surface protein involved in sperm-egg adhesion, was shown to be anchored in the plasma membrane by attachment to the lipid phosphatidylinositol and to have a diffusion rate that is highly restricted on testicular sperm, being more than a thousand times slower than lipid diffusion. These results support the hypothesis that lateral mobility of a membrane protein can be regulated exclusively by interactions of its ectodomain.

Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes

Nature ◽  
1980 ◽  
Vol 285 (5765) ◽  
pp. 510-512 ◽  
Author(s):  
Michael P. Sheetz ◽  
Melvin Schindler ◽  
Dennis E. Koppel
Keyword(s):  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Lateral Mobility

scholarly journals Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

1994 ◽  
Vol 299 (1) ◽  
pp. 191-196 ◽  
Author(s):  
N J Hemming ◽  
D J Anstee ◽  
W J Mawby ◽  
M E Reid ◽  
M J Tanner
Keyword(s):  
Amino Acid ◽  
Human Erythrocyte ◽  
Synthetic Peptide ◽  
Attachment Site ◽  
Amino Acid Residues ◽  
Protein 4.1 ◽  
Attachment Sites ◽  
Underlying Network ◽  
Membrane Attachment ◽  
Glycophorin C

The flexibility of the human erythrocyte membrane is mediated by an underlying network of skeletal proteins which interact with the membrane through ankyrin and protein 4.1. The nature of the membrane attachment site(s) for protein 4.1 has yet to be fully elucidated. In this paper we show that purified protein 4.1 binds much less strongly to alkali-stripped membranes from erythrocytes of individuals with total glycophorin C and D deficiency (Leach phenotype) than to alkali-stripped normal membranes. We further show that a synthetic peptide corresponding to amino acid residues 82-98 of the cytoplasmic domain of glycophorin C specifically binds to purified protein 4.1 and inhibits protein 4.1 binding to alkali-stripped normal membranes. The same synthetic peptide binds directly to membranes from individuals with glycophorin C and D deficiency but not to normal membranes. These results indicate that glycophorins C and D provide major membrane attachment sites for protein 4.1 in normal erythrocytes and that this interaction is mediated by protein 4.1 binding to amino acid residues 82-98 of glycophorin C and 61-77 of glycophorin D.

Image Analysis of Intramembrane Particles in Freeze-Fractured Biomembranes Using Computer Simulation Techniques

1975 ◽  
Vol 33 ◽  
pp. 214-215
Author(s):  
D.J. Benefiel ◽  
R.S. Weinstein
Keyword(s):  
Membrane Proteins ◽  
Freeze Fracture ◽  
Integral Membrane Proteins ◽  
Systematic Evaluation ◽  
Intramembrane Particles ◽  
Modeling Methods ◽  
Simulation Techniques ◽  
Freeze Fracture Electron Microscopy ◽  
Fracture Electron ◽  
Computer Simulation Techniques

Intramembrane particles (IMP or MAP) are components of most biomembranes. They are visualized by freeze-fracture electron microscopy, and they probably represent replicas of integral membrane proteins. The presence of MAP in biomembranes has been extensively investigated but their detailed ultrastructure has been largely ignored. In this study, we have attempted to lay groundwork for a systematic evaluation of MAP ultrastructure. Using mathematical modeling methods, we have simulated the electron optical appearances of idealized globular proteins as they might be expected to appear in replicas under defined conditions. By comparing these images with the apearances of MAPs in replicas, we have attempted to evaluate dimensional and shape distortions that may be introduced by the freeze-fracture technique and further to deduce the actual shapes of integral membrane proteins from their freezefracture images.

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