Role of the membrane skeleton in creation of microdomains.

作者: Ken Ritchie , Akihiro Kusumi

DOI: 10.1007/978-1-4757-5806-1_7

关键词:

摘要: The membrane skeleton is a specialized part of the cytoskeleton that in close proximity to cell with protein composition and structure differs from bulk cytoskeleton. various transmembrane proteins bound it form mosaic compartments responsible for temporary confinement lipids controls rate their repetitive hop movements between these skeleton-based compartments, known as “hop diffusion”, found by observation single-molecule diffusion. Such diffusion has been be universal compartment sizes range 30 700 nm, depending on type. directly involved temporal molecules successfully imaged raster scanning single molecule using an optical trap (single force imaging). compartmentalization enables dynamic spatial regulation signal transduction plasma membrane, arresting signaling complexes activated receptor enlarged, stabilized rafts within compartment. Furthermore, high concentrations its associated immobile are formation polarity such across initial segment axon body neurons. Argument advanced creation domains must influenced skeleton.

参考文章(22)
K. Ritchie, A. Kusumi, Single molecule probe scanning optical force imaging microscopefor viewing live cells. Journal of Biological Physics. ,vol. 28, pp. 619- 626 ,(2002) , 10.1023/A:1021282504628
K Jacobson, E. Sheets, R Simson, Revisiting the fluid mosaic model of membranes. Science. ,vol. 268, pp. 1441- 1442 ,(1995) , 10.1126/SCIENCE.7770769
Jeff Gelles, Bruce J. Schnapp, Michael P. Sheetz, Tracking kinesin-driven movements with nanometre-scale precision Nature. ,vol. 331, pp. 450- 453 ,(1988) , 10.1038/331450A0
S. J. Singer, G. L. Nicolson, The Fluid Mosaic Model of the Structure of Cell Membranes Science. ,vol. 175, pp. 720- 731 ,(1972) , 10.1126/SCIENCE.175.4023.720
Nicholas J. P. Ryba, Laszlo I. Horvath, Anthony Watts, Derek Marsh, Molecular exchange at the lipid-rhodopsin interface: spin-label electron spin resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants. Biochemistry. ,vol. 26, pp. 3234- 3240 ,(1987) , 10.1021/BI00385A045
M.J. Saxton, Single-particle tracking: effects of corrals Biophysical Journal. ,vol. 69, pp. 389- 398 ,(1995) , 10.1016/S0006-3495(95)79911-8
Yasushi Sako, Akira Nagafuchi, Shoichiro Tsukita, Masatoshi Takeichi, Akihiro Kusumi, Cytoplasmic Regulation of the Movement of E-Cadherin on the Free Cell Surface as Studied by Optical Tweezers and Single Particle Tracking: Corralling and Tethering by the Membrane Skeleton Journal of Cell Biology. ,vol. 140, pp. 1227- 1240 ,(1998) , 10.1083/JCB.140.5.1227
Dennis F. Kucik, Elliot L. Elson, Michael P. Sheetz, Forward transport of glycoproteins on leading lamellipodia in locomoting cells. Nature. ,vol. 340, pp. 315- 317 ,(1989) , 10.1038/340315A0
Michael P. Sheetz, Stephen Turney, Hong Qian, Elliot L. Elson, Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movements Nature. ,vol. 340, pp. 284- 288 ,(1989) , 10.1038/340284A0
M.M. Sperotto, O.G. Mouritsen, Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins Biophysical Journal. ,vol. 59, pp. 261- 270 ,(1991) , 10.1016/S0006-3495(91)82219-6