help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 55: 21-28 (1989)
© 1989 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Saxton, M J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saxton, M J

The spectrin network as a barrier to lateral diffusion in erythrocytes. A percolation analysis.

M J Saxton

Department of Agronomy and Range Science, University of California, Davis 95616.

ABSTRACT

The spectrin network on the cytoplasmic surface of an erythrocyte can be modeled as a triangular lattice of spectrin tetramers (Tsuji, A., and S. Ohnishi, 1986. Biochemistry. 25:6133-6139). The tetramers act as barriers to protein diffusion, while dissociated dimer pairs, single dimers, and missing tetramers do not. Diffusion in the presence of these barriers is shown to be equivalent to bond percolation on the honeycomb lattice. Monte Carlo calculations for this system then yield the relative diffusion constant of a mobile integral protein as a function of the fraction of spectrin tetramers. At high concentrations of spectrin tetramer, long-range diffusion is blocked, but short-range diffusion is still possible. Monte Carlo calculations yield the average distance over which short-range diffusion can occur, as a function of the fraction of spectrin tetramers. Applications to erythrocyte development and hereditary hemolytic anemia are discussed.




This article has been cited by other articles:


Home page
Biophys. JHome page
Y. M. Umemura, M. Vrljic, S. Y. Nishimura, T. K. Fujiwara, K. G. N. Suzuki, and A. Kusumi
Both MHC Class II and its GPI-Anchored Form Undergo Hop Diffusion as Observed by Single-Molecule Tracking
Biophys. J., July 1, 2008; 95(1): 435 - 450.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
N. Morone, T. Fujiwara, K. Murase, R. S. Kasai, H. Ike, S. Yuasa, J. Usukura, and A. Kusumi
Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography
J. Cell Biol., September 11, 2006; 174(6): 851 - 862.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
K. Suzuki, K. Ritchie, E. Kajikawa, T. Fujiwara, and A. Kusumi
Rapid Hop Diffusion of a G-Protein-Coupled Receptor in the Plasma Membrane as Revealed by Single-Molecule Techniques
Biophys. J., May 1, 2005; 88(5): 3659 - 3680.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
L. C.-L. Lin and F. L. H. Brown
Dynamics of Pinned Membranes with Application to Protein Diffusion on the Surface of Red Blood Cells
Biophys. J., February 1, 2004; 86(2): 764 - 780.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
F. L. H. Brown
Regulation of Protein Mobility via Thermal Membrane Undulations
Biophys. J., February 1, 2003; 84(2): 842 - 853.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
M. Tomishige, Y. Sako, and A. Kusumi
Regulation Mechanism of the Lateral Diffusion of Band 3 in Erythrocyte Membranes by the Membrane Skeleton
J. Cell Biol., August 24, 1998; 142(4): 989 - 1000.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1989 by the Biophysical Society.