Spectrin is the major constituent protein of the erythrocyte cytoskeleton which forms a filamentous network on the cytoplasmic face of the membrane by providing a scaffold for a variety of proteins. In this review, several aspects of spectrin organization are highlighted, particularly with respect to its ability to bind hydrophobic ligands and its interaction with membrane surfaces. The characteristic binding of the fluorescent hydrophobic probes Prodan and pyrene to spectrin, which allows an estimation of the polarity of the hydrophobic probe binding site, is illustrated. In addition, the contribution of uniquely localized and conserved tryptophan residues in the ‘spectrin repeats’ in these processes is discussed. A functional implication of the presence of hydrophobic binding sites in spectrin is its recently discovered chaperone-like activity. Interestingly, spectrin exhibits residual structural integrity even after denaturation which could be considered as a hallmark of cytoskeletal proteins. Future research could provide useful information about the possible role played by spectrin in cellular physiology in healthy and diseased states.
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Review Article|
November 17 2006
Spectrin Organization and Dynamics: New Insights
Abhijit Chakrabarti;
Abhijit Chakrabarti
1Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, 700 064, India
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Devaki A. Kelkar;
Devaki A. Kelkar
2Centre for Cellular and Molecular Biology, Hyderabad, 500 007, India
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Amitabha Chattopadhyay
Amitabha Chattopadhyay
2Centre for Cellular and Molecular Biology, Hyderabad, 500 007, India
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Publisher: Portland Press Ltd
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 2006 Springer Science+Business Media, LLC
2006
Biosci Rep (2006) 26 (6): 369–386.
Citation
Abhijit Chakrabarti, Devaki A. Kelkar, Amitabha Chattopadhyay; Spectrin Organization and Dynamics: New Insights. Biosci Rep 17 November 2006; 26 (6): 369–386. doi: https://doi.org/10.1007/s10540-006-9024-x
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