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Multisite protein phosphorylation – from molecular mechanisms to kinetic models
Author(s) -
Salazar Carlos,
Höfer Thomas
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07027.x
Subject(s) - phosphorylation , protein phosphorylation , processivity , biology , mechanism (biology) , phosphorylation cascade , function (biology) , microbiology and biotechnology , computational biology , chemistry , biochemistry , enzyme , protein kinase a , philosophy , epistemology , polymerase
Multisite phosphorylation is an important mechanism for fine‐tuned regulation of protein function. Mathematical models developed over recent years have contributed to elucidation of the functional consequences of a variety of molecular mechanisms involved in processing of the phosphorylation sites. Here we review the results of such models, together with salient experimental findings on multisite protein phosphorylation. We discuss how molecular mechanisms that can be distinguished with respect to the order and processivity of phosphorylation, as well as other factors, regulate changes in the sensitivity and kinetics of the response, the synchronization of molecular events, signalling specificity, and other functional implications.