cAMP is a compound synthesized in cells by adenylate cyclase in response to a variety of extracellular signals.
However, the topography and mechanical properties of the ECM also come to play an important role in powerful, complex crosstalk with the cells growing on or inside the matrix.
[7] For example, integrin-mediated cytoskeleton assembly and even cell motility are affected by the physical state of the ECM.
[7] In turn, binding of the same integrin (α5β1) to an immobilized fibronectin ligand is seen to form highly phosphorylated focal contacts/focal adhesion (cells involved in matrix adhesion) within the membrane and reduces cell migration rates[7] In another example of crosstalk, this change in the composition of focal contacts in the cytoskeleton can be inhibited by members of yet another pathway: inhibitors of myosin light-chain kinases or Rho kinases, H-7 or ML-7, which reduce cell contractility and consequently motility.
Newly formed cAMP is released from the membrane and diffuses across the intracellular space where it serves to activate PKA.
[4] This cleavage in turn activates PKA by exposing the catalytic sites of the C subunits, which can then phosphorylate an array of proteins in the cell.
[4] In lymphocytes, the intracellular levels of cAMP increase upon antigen-receptor stimulation and even more so in response to prostaglandin E and other immunosuppression agents.
Phosphorylation of this third site by PKAs from the cAMP pathway inhibits binding of MAP kinases to HePTP and thereby upregulates the MAPK/ERK signaling cascade.
This prevents HePTP from binding to Erk and frees the MAPK pathway from inhibition, allowing downstream signaling to continue (see figure 4).