Chapter 13 Analysis of Protein-Tyrosine Phosphorylation by Mass Spectrometry

Zhang, Guoan; Xu, Chong-Feng; Neubert, Thomas A.

doi:10.1016/s0166-526x(08)00213-4

Cited by 1 publication

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“…While phosphorylations at threonine (Di Croce and Shiekhattar, 2008; Kulasekara and Miller, 2007), and certainly tyrosine (Franco and Tamagnone, 2008; Girault, 2006; Grangeasse et al, 2007; Nag and Chaudhary, 2009; Roskoski, 2008; Zhang et al, 2009), are of great importance, this overview focuses on serine phosphorylation (For nice complementary discussions from the groups of Otaka and Ojea, primarily focusing on the chemistry of other phosphono-AA's see: (Fernandez et al, 2006; Otaka et al, 2000; Otaka et al, 2004)). More specifically, we will examine the use of the (α,α-difluoromethylene)phosphonate functionality to mimic the phosphate monoester form of serine residues, in proteins that are subject to regulation via serine phosphorylation.…”

Section: Introductionmentioning

confidence: 99%

The α,α-Difluorinated Phosphonate L-pSer-Analogue: An Accessible Chemical Tool for Studying Kinase- Dependent Signal Transduction

Panigrahi

Eggen

Maeng

et al. 2009

Chemistry & Biology

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SUMMARY This overview focuses on the (α,α-difluoromethylene)phosphonate mimic of phosphoserine (pCF2Ser) and its application to the study of kinase-mediated signal transduction – pathways of great interest to drug development. The most versatile modes of access to these chemical biological tools are discussed, organized by method of PCF2-C bond. The pCF2-Ser mimic may be site-specifically incorporated into peptides (SPPS) and proteins (expressed protein ligation). This isopolar, dianionic pSer mimic results in a “constitutive phosphorylation” phenotype, and is seen to support native protein-protein interactions that depend upon serine phosphorylation. Signal transduction pathways studied with this chemical biological approach include the regulation of p53 tumor suppressor protein activity, and of melatonin production. Given these successes, the future is bright for the use of such “teflon phospho-amino acid mimics” to map kinase-based signaling pathways.

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