Final answer:
Experimentally separating α/β heterodimer integrin subunits disrupts the integrin-mediated adhesion and signaling, possibly affecting focal adhesion formation and cell viability and function.
Step-by-step explanation:
Integrins are transmembrane receptors that facilitate cell-extracellular matrix (ECM) adhesion. Upon ligand binding to the heterodimer structure comprised of α (alpha) and β (beta) subunits, integrins undergo conformational changes that affect intracellular signaling pathways. If you were to experimentally separate the α/β heterodimer integrin subunits, several biological responses could be affected.
Models like the one proposed by Deshpande and colleagues suggest that integrin-mediated adhesion dynamics are influenced by the equilibrium between low and high affinity states of the integrins and are modulated by the mechanical forces via the cytoskeleton. Moreover, the formation of focal adhesions, structures that connect the ECM to the actin cytoskeleton and are essential for cell motility, signaling, and survival, might be disrupted due to altered integrin interactions. In the context of cancer, loss of function or mutations in integrin subunits can result in defective cell adhesion, which plays a role in cancer progression.
Therefore, upon the artificial separation of the α/β heterodimer, the previously coordinated cellular functions such as attachment to the ECM, intracellular signaling, and formation of cell junctions may be impaired, potentially influencing cell viability and function.