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Sci. STKE, 18 December 2007
Vol. 2007, Issue 417, p. pl8
[DOI: 10.1126/stke.4172007pl8]


Identification of Redox-Active Cell-Surface Proteins by Mechanism-Based Kinetic Trapping

Ulla Schwertassek{dagger}, Lars Weingarten, and Tobias P. Dick*

Redox Regulation Research Group (A160), German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
{dagger}Present address: Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.

Abstract: A number of thiol-dependent oxidoreductases are released from cells and act on the cell surface. Correspondingly, several cell-surface processes appear to depend on catalyzed thiol-disulfide exchange, including integrin activation and the fusion of viral particles with the host membrane. Tumor cells frequently increase the abundance of secreted and cell-surface forms of particular oxidoreductases, and evidence suggests that oxidoreductases released from tumor cells promote growth and contribute to the remodeling of the cellular microenvironment. Few cell-surface or membrane proteins that are targeted by extracellular redox enzymes have been identified. One major reason for this slow progress is the highly transient nature of thiol-disulfide exchange, making its detection by conventional techniques difficult or impossible. Here we describe the application of an activity-based proteomics approach, also known as "mechanism-based kinetic trapping," to identify individual cell-surface target proteins that engage in disulfide exchange with thiol-dependent oxidoreductases. Although we have applied this approach to thioredoxin-1, it should also be applicable to other members of the thioredoxin superfamily whose activity is based on the CXXC active-site motif.

*Corresponding author. E-mail, t.dick{at}

Citation: U. Schwertassek, L. Weingarten, T. P. Dick, Identification of Redox-Active Cell-Surface Proteins by Mechanism-Based Kinetic Trapping. Sci. STKE 2007, pl8 (2007).

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