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Molecular & Cellular Proteomics 4:785-795, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Targeted Proteomic Analysis of 14-3-3, a p53 Effector Commonly Silenced in Cancer^*,S

Anne Benzinger, Nemone Muster^,¶, Heike B. Koch, John R. Yates, III^,¶ and Heiko Hermeking^,||

From the Molecular Oncology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried/Munich, Germany and Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037

To comprehensively identify proteins interacting with 14-3-3 in vivo, tandem affinity purification and the multidimensional protein identification technology were combined to characterize 117 proteins associated with 14-3-3 in human cells. The majority of identified proteins contained one or several phosphorylatable 14-3-3-binding sites indicating a potential direct interaction with 14-3-3. 25 proteins were not previously assigned to any function and were named SIP2–26 (for 14-3-3-interacting protein). Among the 92 interactors with known function were a number of proteins previously implicated in oncogenic signaling (APC, A-RAF, B-RAF, and c-RAF) and cell cycle regulation (AJUBA, c-TAK, PTOV-1, and WEE1). The largest functional classes comprised proteins involved in the regulation of cytoskeletal dynamics, polarity, adhesion, mitogenic signaling, and motility. Accordingly ectopic 14-3-3 expression prevented cellular migration in a wounding assay and enhanced mitogen-activated protein kinase signaling. The functional diversity of the identified proteins indicates that induction of 14-3-3 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 14-3-3 expression by epigenetic silencing or p53 mutations contributes to cancer formation by multiple routes.

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