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J. Biol. Chem., Vol. 281, Issue 46, 99936, November 17, 2006

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Cell Adhesion Surprise

Patrick Doherty and Frank Walsh were among the first investigators to use molecular approaches to study cell adhesion molecules (CAMs) and how they function in regulating neurite growth. While studying NCAM, they identified a sequence in the FGF receptor (FGFR) that was homologous to sequences in N-cadherin and L1, two other CAMs that promote neurite growth. They dubbed this region the "CAM homology domain" and conducted experiments using peptides from the domain to argue that the FGFR directly interacted with the CAMs to promote neurite growth. This hypothesis was controversial, but subsequent pharmacological, genetic, and structural studies have given it support.

NCAM co-localizes with FGFR.

In this Paper of the Week, Elena Sanchez-Heras and her colleagues in Doherty's laboratory use co-immunoprecipitation and co-clustering assays to map sites on the FGFR that are required for interaction with N-cadherin and NCAM. They demonstrate for the first time that all of the major isoforms of NCAM can interact with the FGFR. Surprisingly, they also find that the interactions require an "acid box" region in the FGFR but not the CAM homology domain. This result leads to an unexpected situation in which FGFR-CAM interactions are confirmed, but a role for the CAM homology domain is excluded.

FOOTNOTES

See referenced article, J. Biol. Chem. 2006, 281, 35208-35216

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Related Collections Papers Of The Week Social Bookmarking                      What's this?