Research HER
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HER Dimerization
Structure of a dimerized receptor complex
This image shows the crystal structure of the extracellular portion of a dimerized pair of HER1/EGFR receptors. Note that the 2 receptors are bound to each other as well as to 2 molecules of EGF, a ligand specific to HER1/EGFR. Dimerization enables activation of the tyrosine kinase domain of the receptors and subsequent molecular signaling within the cell.1,3 Reprinted from Cell vol 110, Ogiso H, Ishitani R, Nureki O, et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains, pp 775-787, Copyright 2002, with permission from Elsevier.
Dimerization is a key step in HER signaling pathways
- Activation of HER family receptors does not occur until the receptors have dimerized, making dimerization a critical step in the cellular signaling process3
HER receptor dimers have multiple effects on cellular signaling
With 4 members of the HER family of receptors, each of which is able to homodimerize or to heterodimerize with other members of the HER family, multiple receptor combinations are possible.1
- Each possible pairing of HER family receptors stimulates a different combination of signaling pathways within the cell1
- These pathways overlap, creating a highly complex system of signals
- HER2 is the preferred dimerization partner for all members of the HER family of receptors1,7
- However, less common dimers not including HER2, such as the HER3/HER4 heterodimer, do exist5
- Signals from dimerized, activated HER family receptors can lead to multiple effects, including1,5:
- Growth
- Proliferation
- Survival/decreased apoptosis
- Cellular migration
- Angiogenesis