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This article is part of the supplement: Annual Meeting of the Study Group Neurochemistry. International Conference of the Gesellschaft für Biochemie und Molekularbiologie 2006 (GBM 2006): Molecular pathways in health and disease of the nervous system

Open Access Poster presentation

Two-step proteolytic cleavage of the human protocadherin Fat1 and translocation of the intracellular domain to the nucleus

Dietmar Schreiner* and Hans Werner Hofer

  • * Corresponding author: Dietmar Schreiner

Author Affiliations

University of Konstanz, Department of Biology, Konstanz, Germany

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BMC Neuroscience 2007, 8(Suppl 1):P22  doi:10.1186/1471-2202-8-S1-P22

The electronic version of this article is the complete one and can be found online at:


Published:23 March 2007

© 2007 Schreiner and Hofer; licensee BioMed Central Ltd.

Poster presentation

The giant member of the protocadherin family, hFat1, is of pivotal importance during embryonal and fetal development of various organs including frontal brain. hFat1 is also essential in podocyte and slit membrane formation of renal glomeruli. In cultured cells, the transmembrane form of hFat1 is located at lamellipodial edges and filopodial tips. Its involvement in the regulation of actin cyto-skeleton dynamics by interacting with mammalian Ena/Vasp proteins has been reported. In HEK293 cells we have expressed a transmembrane construct of hFat1 comprising the extracellular EGF-like domains and the intracellular domain. The localization pattern of the construct agrees with that of endogenous hFat1. Our data also suggest that the transmembrane form of hFat1 undergoes a regulated two step proteolytic process similar to that described for other members of the cadherin family. Apparently, the cleavages occurs spontaneously in some cell lines. In a first step, the extracellular domain is cleaved and released into the culture medium. A subsequent cleavage process releases the intracellular domain. The intracellular domain is predominantly translocated to the nucleus. This is partly due to the unmasking of a N-terminal nuclear localisation sequence but additional effects, such as binding to nuclear proteins may also contribute.