Abstract
Calregulin is a calcium buffering protein that regulates calcium storage and release within the endoplasmic reticulum. Calregulin is highly conserved across many species and associates and regulates the function of several proteins. We previously investigated the regulation of MARCKS by calcium/calmodulin. Here, we investigated putative protein binding partners of calregulin at the apical membrane where MARCKS is known to function. Cytoplasmic proteins from HEK293 cells were resolved by two‐dimensional gel electrophoresis. Calregulin was identified among the protein spots by mass spectrometry. Calregulin expression was not limited to the ER but also present in the cytoplasm as demonstrated by sucrose density gradient and Western blot analysis. Calregulin co‐immunoprecipitated with the transmembrane protein, phospholipase C beta‐3, and the actin cytoskeletal protein, spectrin. This interaction required the presence of phosphatase inhibitors, suggesting a requirement for phosphorylation. Future studies will be necessary to identify a potential role for calregulin in regulating the function of phospholipase C beta‐3 and spectrin and calcium binding proteins such as calmodulin.
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