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Spectrin Organization and Dynamics: New Insights

  • Original paper
  • Published:
Bioscience Reports

Abstract

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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Abbreviations

2,3-DPG:

2,3-Diphosphoglycerate

ANS:

1-Anilinonapthalene-8-sulfonic acid

PC:

Phosphatidylcholine

PE:

Phosphatidylethanolamine

PS:

Phosphatidylserine

PRODAN:

6-Propionyl-2-dimethylaminonaphthalene

REES:

Red edge excitation shift

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Acknowledgements

Work in A. Chattopadhyay’s laboratory was supported by a grant (00-141 RG/BIO/AS) from The Third World Academy of Sciences, Trieste, Italy, and by the Council of Scientific and Industrial Research, Government of India. Work in A. Chakrabarti’s laboratory was supported by the Department of Atomic Energy, Government of India. D.A.K. thanks the Life Sciences Research Board for the award of a Postdoctoral Fellowship. A. Chattopadhyay is an Honorary Professor of the Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore (India). Some of the work described in this article was carried out by former members of our research groups. We would like to thank members of the Chattopadhyay laboratory for critically reading the manuscript.

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  1. Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, 700 064, India

    Abhijit Chakrabarti

  2. Centre for Cellular and Molecular Biology, Hyderabad, 500 007, India

    Devaki A. Kelkar & Amitabha Chattopadhyay

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Chakrabarti, A., Kelkar, D.A. & Chattopadhyay, A. Spectrin Organization and Dynamics: New Insights. Biosci Rep 26, 369–386 (2006). https://doi.org/10.1007/s10540-006-9024-x

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