Spectrin interactome under normal and HbE-disease conditions
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ORIGINAL ARTICLE
Spectrin interactome under normal and HbE‑disease conditions Dipayan Bose1,3 · Sk Ramiz Islam2,3 · Sutapa Saha4 · Abhijit Chakrabarti1,3 Received: 18 September 2020 / Revised: 8 October 2020 / Accepted: 9 October 2020 © Springer Nature Singapore Pte Ltd. 2020
Abstract Spectrin, the major component of the erythrocyte membrane skeleton, is a key player in red cell biology. It has a significant role in signalling pathways, and as such knowledge of spectrin interactors becomes crucial. Here, we report the cytosolic interactome of human erythroid spectrin (ProteomeXchange id: PXD021525). This is to the best of our knowledge the first report of the interactome of human erythroid spectrin. We have further investigated the spectrin interactome under HbEdisease conditions. Our findings indicate that there is no difference in the identity of the proteins interacting with spectrin between normal and disease conditions. However, relative abundance of the interacting partners is seen to change. Very interestingly, the interacting chaperone proteins, heme-containing proteins and redox active proteins are seen to be up-regulated in HbE-disease state. This is consistent with our previous observation that the presence of oxidation prone hemoglobin variants leads to an increase of redox regulators and chaperones in the red cell proteome. Spectrin can also interact with horse radish peroxidase and oxidatively cross-link hemoglobin, which has possible implications in oxidative stress management. Since a large fraction of spectrin interacting proteins are chaperones and redox active proteins, it is possible that spectrin may have a broader role in redox regulation, especially in cases where there are unstable hemoglobin variants present. Keywords Spectrin · Hemoglobin · Redox · Interactome · Chaperone Abbreviations HbA Hemoglobin A HbE Hemoglobin E
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s42485-020-00050-x) contains supplementary material, which is available to authorized users. * Abhijit Chakrabarti [email protected] 1
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India
2
Biophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India
3
Homi Bhabha National Institute, Mumbai 400094, India
4
Department of Life Sciences, Presidency University, Kolkata 700073, India
Introduction Spectrin is the major component of the membrane skeleton in mature human erythrocytes (RBCs) (Bennett 1985). Available literature shows that spectrin has a role as a component of the cellular signalling machinery and also serves as a structural platform for cytoskeletal protein assemblies (Djinovic-Carugo et al. 2002; Deng et al. 2015; Fletcher et al. 2015). Moreover, studies from our laboratory have demonstrated that spectrin is able to interact with hemoglobin, the most abundant protein of the RBC cytosol (Basu and Chakrabarti
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