Cellular growth signals are often transmitted through a process called phosphorylation, in which an enzyme called tyrosine kinase attaches a phosphate tag to another protein. This phosphate tag is derived from a molecule called ATP.2
HER2 is a protein in the receptor tyrosine kinase family. This protein consists of a receptor domain outside the cell connected to a tyrosine kinase domain inside the cell.3
The kinase domain of HER2 is inactive by itself, but when two kinase domains come together to form a dimer, the kinase is activated, allowing phosphorylation to transmit growth signals.3
HER2 is activated during specific stages of development by dimerizing with other similar proteins, such as EGFR or HER3. It is responsible for the development of various organs, such as the heart and the mammary gland.4,5 Of note, the expression level of HER2 is tightly controlled so that growth signals are generated only when necessary.
However, in some types of cancer, HER2 is overexpressed. Due to enhanced pairing of HER2 with other similar proteins and also itself, uncontrolled growth signals are produced that drive cancer proliferation.3
Fam-trastuzumab deruxtecan-nxki is an antibody-drug conjugate that comprises of toxic molcules called DXd attached to an antibody called trastuzumab, which can specifically recognize and bind to HER2.6
(1) When fam-trastuzumab deruxtecan-nxki binds to HER2, it can get internalized into the cell along with HER2. (2) Some internalized HER2 proteins are degraded, which releases DXd that can kill the cell. Since trastuzumab specifically recognizes HER2, cells expressing the highest amounts of HER2, i.e. the cancer cells, are targeted for killing, while most other cells are spared.6