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Published online April 16, 2007
doi:10.1083/jcb.200701158
The Journal of Cell Biology, Vol. 177, No. 2, 211-218
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Nicholson et al.
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Identification of a novel functional specificity signal within the GPI anchor signal sequence of carcinoembryonic antigen



Thomas B. Nicholson1,2 and Clifford P. Stanners1,2

1 McGill Cancer Centre and 2 Biochemistry Department, McGill University, Montréal, Québec H3G 1Y6, Canada

Correspondence to Clifford P. Stanners: cliff.stanners{at}mcgill.ca

Exchanging the glycophosphatidylinositol (GPI) anchor signal sequence of neural cell adhesion molecule (NCAM) for the signal sequence of carcinoembryonic antigen (CEA) generates a mature protein with NCAM external domains but CEA-like tumorigenic activity. We hypothesized that this resulted from the presence of a functional specificity signal within this sequence and generated CEA/NCAM chimeras to identify this signal. Replacing the residues (GLSAG) 6–10 amino acids downstream of the CEA anchor addition site with the corresponding NCAM residues resulted in GPI-anchored proteins lacking the CEA-like biological functions of integrin modulation and differentiation blockage. Transferring this region from CEA into NCAM in conjunction with the upstream proline (PGLSAG) was sufficient to specify the addition of the CEA anchor. Therefore, this study identifies a novel specificity signal consisting of six amino acids located within the GPI anchor attachment signal, which is necessary and sufficient to specify the addition of a particular functional GPI anchor and, thereby, the ultimate function of the mature protein.

Abbreviations used in this paper: CC1, CEA-related cell adhesion molecule 1; CEA, carcinoembryonic antigen; Fn, fibronectin; GPI, glycophosphatidylinositol; NCAM, neural cell adhesion molecule; PIPLC, phosphatidylinositol PLC; TM, transmembrane.


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