Figure - available from: Journal of Proteins and Proteomics
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Pie chart representing the different classes of proteins that spectrin interacting proteins belong to. Classification of proteins into different classes was done with the help of PANTHER database
Source publication
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 kn...
Similar publications
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 knowl...
Citations
... Spectrin is a cytoskeletal protein ubiquitous in metazoan (multicellular mitochondrial) cells 1,2 that acts as a liaison between the plasma membrane and the cellular interior, 3 on account of its interaction with a wide range of cytoplasmic, membrane-bound, and cytoskeletal proteins. 4 The emergence of this protein is believed to be linked to the evolution of metazoans from unicellular protists. 5 The spectrin meshwork (along with other cytoskeletal components such as actin) 6 imparts mechanical stability to the plasma membrane and regulates cellular morphology. ...
Hemoglobin oxidation due to oxidative stress and disease conditions leads to generation of ROS (reactive oxygen species) and membrane attachment of hemoglobin in‐vivo, where its redox activity leads to peroxidative damage of membrane lipids and proteins. Spectrin, the major component of the red blood cell (RBC) membrane skeleton, is known to interact with hemoglobin and, here this interaction is shown to increase hemoglobin peroxidase activity in the presence of reducing substrate ABTS (2’, 2’‐Azino‐Bis‐3‐Ethylbenzothiazoline‐6‐Sulfonic Acid). It is also shown that in the absence of reducing substrate, spectrin forms covalently cross‐linked aggregates with hemoglobin which display no peroxidase activity. This may have implications in the clearance of ROS and limiting peroxidative damage. Spectrin is found to modulate the peroxidase activity of different hemoglobin variants like A, E, and S, and of isolated globin chains from each of these variants. This may be of importance in disease states like sickle cell disease and HbE‐β‐thalassemia, where increased oxidative damage and free globin subunits are present due to the defects inherent in the hemoglobin variants associated with these diseases. This hypothesis is corroborated by lipid peroxidation experiments. The modulatory role of spectrin is shown to extend to other heme proteins, namely catalase and cytochrome‐c. Experiments with free heme and Raman spectroscopy of heme proteins in the presence of spectrin show that structural alterations occur in the heme moiety of the heme proteins on spectrin binding, which may be the structural basis of increased enzyme activity.
