Protein kinases are able to perform Circean tasks in the cell by daubing phosphate molecules onto other proteins and thus instantly changing the behavior of the recipient proteins.

Hydrolysis and release of ADP and a phosphate molecule resets the protein.

Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines.

MuSK is a receptor tyrosine kinase - meaning that it induces cellular signaling by binding phosphate molecules to self regions like tyrosines, and to other targets in the cytoplasm.

The couple coaxes other proteins into the cell division process by adding phosphate molecules to the deputy proteins, which changes their form and function.

The first step involves displacement of CoA from succinyl CoA by a nucleophilic inorganic phosphate molecule to form succinyl phosphate.

This reaction is irreversible because the pyrophosphate that is formed is hydrolyzed into two inorganic phosphate molecules by the enzyme inorganic pyrophosphatase.

TrkC is a receptor tyrosine kinase (meaning it mediates its actions by causing the addition of phosphate molecules on certain tyrosines in the cell, activating cellular signaling).

Recent structural studies have shown that phosphate molecules bind to the GTP site.

Of every six triose phosphate molecules produced, one is removed to form further carbohydrates and five are "recycled" back into the cycle to regenerate the original carbon dioxide acceptor, RuBP.