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A Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function

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Science  05 Jul 2013:
Vol. 341, Issue 6141, pp. 74-76
DOI: 10.1126/science.1238279

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Form and Function

The contribution of disulfide bonding to oxidative protein folding and assembly, quality control, and stress responses in the endoplasmic reticulum (ER) are widely recognized. In contrast, catalysis of disulfide bond formation downstream of the ER is uncharted territory. QSOX, a Golgi-localized or secreted disulfide catalyst, was identified in the 1970s and was more recently shown to be upregulated in many cancers. However, the physiological importance of QSOX catalytic activity has been unclear. Ilani et al. (p. 74, published online 23 May) found that human QSOX1 is essential for incorporation of laminin into the extracellular matrix, with profound effects on the capability of the matrix to support integrin-mediated cell adhesion and migration.

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