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Submitted on January 18, 2005
Revised on March 18, 2005
Accepted on March 18, 2005

Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer

Anne Benzinger, Nemone Muster, Heike B. Koch, John R. Yates 3rd, and Heiko Hermeking

Molecular Oncology, Max-Planck-Institute of Biochemistry, Martinsried 82152

Corresponding Author: herme{at}biochem.mpg.de

In order to comprehensively identify proteins interacting with 14-3-3 in vivo, tandem affinity purification (TAP) and the multidimensional protein identification technology (MudPIT) were combined to characterize 117 proteins presumably associated with 14-3-3sigma in human cells. The majority of identified proteins contained one or several phosphorylatable 14-3-3 binding sites indicating a potential direct interaction with 14-3-3sigma. 25 proteins were not previously assigned to any function and were named SIP2-26 (for 14-3-3sigma-interacting-protein). Among the 92 interactors with known function were a number of proteins previously implicated in oncogenic signaling (APC, A-RAF, B-RAF, c-RAF) and cell cycle regulation (AJUBA, c-TAK, PTOV-1, WEE1). The largest functional classes comprised proteins involved in the regulation of cytoskeletal dynamics, polarity, adhesion, mitogenic signaling and motility. Accordingly, ectopic 14-3-3sigma expression prevented cellular migration in a wounding assay and enhanced MAP-kinase signaling. The functional diversity of the identified proteins indicates that induction of 14-3-3sigma could allow p53 to affect numerous processes in addition to the previously characterized inhibitory effect on G2/M progression. The data suggest that the cancer-specific loss of 14-3-3sigmaexpressionby epigenetic silencing or p53 mutations contributes to cancer formation by multiple routes.


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