tailieunhanh - Báo cáo khoa học: Versatile regulation of multisite protein phosphorylation by the order of phosphate processing and protein–protein interactions

Multisite protein phosphorylation is a common regulatory mechanism in cell signaling, and dramatically increases the possibilities for protein– protein interactions, conformational regulation, and phosphorylation path-ways. However, there is at present no comprehensive picture of how these factors shape the response of a protein’s phosphorylation state to changes in kinase and phosphatase activities. | ễFEBS Journal Versatile regulation of multisite protein phosphorylation by the order of phosphate processing and protein-protein interactions Carlos Salazar1 and Thomas Heifer1 2 1 TheoreticalBiophysics Institute for Biology Humboldt University Berlin Germany 2 German Cancer Research Center Heidelberg Germany Keywords multisite phosphorylation order of phosphate processing stimulus-response relationship transition time ultrasensitivity Correspondence T. Hofer TheoreticalBiophysics Institute for Biology Humboldt University Berlin Invalidenstr. 42 10115 Berlin Germany Fax 49 30 2093 8813 Tel 49 30 2093 8592 E-mail Website http theorybp Received 30 October 2006 revised 13 December 2006 accepted 18 December 2006 doi Multisite protein phosphorylation is a common regulatory mechanism in cell signaling and dramatically increases the possibilities for proteinprotein interactions conformational regulation and phosphorylation pathways. However there is at present no comprehensive picture of how these factors shape the response of a protein s phosphorylation state to changes in kinase and phosphatase activities. Here we provide a mathematical theory for the regulation of multisite protein phosphorylation based on the mechanistic description of elementary binding and catalytic steps. Explicit solutions for the steady-state response curves and characteristic de phos-phorylation times have been obtained in special cases. The order of phosphate processing and the characteristics of protein-protein interactions turn out to be of overriding importance for both sensitivity and speed of response. Random phosphate processing gives rise to shallow response curves favoring intermediate phosphorylation states of the target and rapid kinetics. Sequential processing is characterized by steeper response curves and slower kinetics. We show systematically how qualitative differences in target .

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