A Fresh Look at the Structure, Regulation, and Functions of Fodrin.

Jamuna S Sreeja, Rince John, Dhrishya Dharmapal, Rohith Kumar Nellikka, Suparna Sengupta

Molecular and cellular biology 2020 Aug 14

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Fodrin and its erythroid cell-specific isoform spectrin are actin-associated fibrous proteins that play crucial roles in the maintenance of structural integrity in mammalian cells, which is necessary for proper cell function. Normal cell morphology is altered in diseases such as various cancers and certain neuronal disorders. Fodrin and spectrin are two-chain (αβ) molecules that are encoded by paralogous genes and share many features but also demonstrate certain differences. Fodrin (in humans, typically a heterodimer of the products of the SPTAN1 and SPTBN1 genes) is expressed in nearly all cell types and is especially abundant in neuronal tissues, whereas spectrin (in humans, a heterodimer of the products of the SPTA1 and SPTB1 genes) is expressed almost exclusively in erythrocytes. To fulfill a role in such a variety of different cell types, it was anticipated that fodrin would need to be a more versatile scaffold than spectrin. Indeed, as summarized here, domains unique to fodrin and its regulation by Ca2+, calmodulin, and a variety of posttranslational modifications (PTMs) endow fodrin with additional specific functions. However, how fodrin structural variations and misregulated PTMs may contribute to the etiology of various cancers and neurodegenerative diseases needs to be further investigated. Copyright © 2020 American Society for Microbiology.

Citation

Jamuna S Sreeja, Rince John, Dhrishya Dharmapal, Rohith Kumar Nellikka, Suparna Sengupta. A Fresh Look at the Structure, Regulation, and Functions of Fodrin. Molecular and cellular biology. 2020 Aug 14;40(17)