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Serine-Threonine Phosphorylation

Phosphorylation, or the addition of a phosphate group to a protein, can happen to tyrosine, serine, and threonine. This results in a functional change in the phosphorylated protein, and will cause enzyme activity, cellular location, or its association with other proteins to change. In essence, it's being changed to a different substance. A few serine and threonine proteins can phosphorylate themselves.

Though tyrosine is the rarest of these phosphorylations, it is also the easiest to study and therefore has been the most heavily studied. But serine/threonine phosphorylation has recently been examined as well. And though tyrosine has been thought to transduce a number of signals on its own, it has recently grown clear that tyrosine interacts with serine and threonine pathways as well in order to achieve maximal activation.

Serine/threonine phosphorylation has been implicated in the genesis and activation of several human cancers, such as chronic lymphocytic leukemia, and in immunodeficiencies, including HIV. Serine/threonine phosphorylation may also be an appropriate target for some chemotherapy drugs, which will recognize activated proteins but ignore inactive ones; this could deter or even inactivate cancers like chronic lymphocytic leukemia.

Web Resources On Serine-Threonine Phosphorylation

Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2
Pathway: Serine/Threonine Phosphorylation

Book Resources On Serine-Threonine Phosphorylation

Biological phosphorylations;: Development of concepts by Herman M. Kalckar
Oxidative Phosphorylation in Health and Disease by Jan A.M. Smeitink

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