|Ref Sequence Id||NP_776642.1|
|Amino Acid Lenth||581|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||localized at the plasma membrane in actin-rich surface structures such as microvilli, membrane ruffles, and lamellipodia in gut cells, lymphocytes, hepatocytes, spermatozoids, fibroblasts and in a variety of other cell types|
|Protein Function||Member of ERM proteins; morphogenesis, cancer metastasis and virus infection; establishment of cell polarity, cell motility and cell signaling; linkers between the plasma membrane and the cortical actin cytoskeleton; crucial molecule in the dissemination of two pediatric tumors, rhabdomyosarcoma and osteosarcoma; overexpression increased migration of metastatic melanoma; interaction with podocalyxin increase the invasiveness of cancer cells; involved in the functional localization of PKA; regulates the structure of the cortical cytoskeleton to control cell surface topography|
|Biochemical Properties||N-terminal domain of ezrin associates with the membrane, whereas the C-terminal half links it to the cytoskeleton; substrates for certain tyrosine kinases;ezrin in soluble extracts of intestinal or placental tissues is monomeric; presence of polyproline stretch|
|Significance in milk||maintainence of 3 dimensional structure of matrix which is required in both cell survival and differentiation has been well documented for mammary gland epithelial cells|
|PTMs||Phosphorylated; C-terminal threonine phosphorylation|
|Significance of PTMs||Phosphorylation of ezrin is required for both conformational activation and for signaling to downstream events|
|Additional Comments||originally purified from the microfilament bundle of isolated intestinal microvilli, yet the native protein possessed no convincing F-actin binding activity|
|Bibliography||1. Algrain, M., Turunen, O., Vaheri, A., Louvard, D., & Arpin, M. (1993). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. The Journal of Cell Biology, 120(1), 129–139. https://doi.org/10.1083/jcb.120.1.129. |
2. Dransfield, D. T., Bradford, A. J., Smith, J., Martin, M., Roy, C., Mangeat, P. H., & Goldenring, J. R. (1997). Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. EMBO Journal, 16(1), 35–43. https://doi.org/10.1093/emboj/16.1.35.
3. Bretscher, A. (1983). Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. The Journal of Cell Biology, 97(2), 425–432. https://doi.org/10.1083/jcb.97.2.425.
4. Gautreau, A., Poullet, P., Louvard, D., & Arpin, M. (1999). Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proceedings of the National Academy of Sciences of the United States of America, 96(13), 7300–7305. https://doi.org/10.1073/pnas.96.13.7300.
5. Srivastava, J., Elliott, B. E., Louvard, D., & Arpin, M. (2005). Src-dependent ezrin phosphorylation in adhesion-mediated signaling. Molecular Biology of the Cell, 16(3), 1481–1490. https://doi.org/10.1091/mbc.e04-08-0721