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First published online November 27, 2006
doi: 10.1242/10.1242/jcs.03270

Journal of Cell Science 119, 4803-4810 (2006)
Published by The Company of Biologists 2006
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All in the CCN family: essential matricellular signaling modulators emerge from the bunker

Andrew Leask1,* and David J. Abraham2

1 CIHR Group in Skeletal Development and Remodeling, Division of Oral Biology, and Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, University of Western Ontario, Dental Sciences Building, London, ON N6A 5C1, Canada
2 Centre for Rheumatology and Connective Tissue Diseases, Royal Free and University College Medical School, University College London (Royal Free Campus), Rowland Hill Street, London, NW3 2PF, UK


Figure 1
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  		Fig. 1. Structure of CCN family members. The CCN family members, CCN1 (Cyr61), CCN2 (CTGF), CCN3 (nov), CCN4 (WISP-1), CCN5 (WISP-2) and CCN6 (WISP-3) have a shared structure, consisting of a secretory signal peptide (SP), an IGF-binding domain (Module I), a von Willebrand type C domain (VWC, Module II), a thrombospondin-1 domain (TSP-1, Module III) and a cysteine knot (Module IV) domain. Domains are linked by hinge regions, susceptible to protease cleavage.

 

Figure 2
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  		Fig. 2. Signaling by CCN family members. CCN1, CCN2 and CCN3 bind TGFß, fibronectin, integrins, LRP1 and HSPGs as indicated. CCN proteins appear to signal principally through the C-terminal quarter (domain IV) to activate adhesive signaling pathways and hence amplify responses to TGFß or fibronectin.

 

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  		Fig. 3. Regulation of the CCN2 promoter and 3' untranslated region (3' UTR). The CCN2 promoter contains recognition sequences for HIF, Smad, BCE-1, Ets-1 and Sp1, as indicated. The 3' UTR of the gene (white rectangle) contains a cis-acting element of structure-anchored repression (CAESAR). Hypoxia, TGFß and endothelin-1 induce CCN2 as indicated.

 

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© The Company of Biologists Ltd 2006