Journal
DEVELOPMENT GROWTH & DIFFERENTIATION
Volume 54, Issue 2, Pages 167-176Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1440-169X.2011.01315.x
Keywords
nuclear localization signal; nuclear translocation; proteolytic cleavage; PRTG; -secretase
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Funding
- Japan Society for the Promotion of Science (JSPS)
- Grants-in-Aid for Scientific Research [22570199] Funding Source: KAKEN
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Protogenin (PRTG) is a transmembrane protein of immunoglobulin superfamily, which has multiple roles in embryogenesis as a receptor or an adhesion molecule. In this study, we present sequential proteolytic cleavage of PRTG. The cleavage first occurs at the extracellular domain, then at the interface of the transmembrane and the intracellular domain by ?-secretase, which results in the release of the intracellular domain of PRTG (PRTG-ICD). PRTG-ICD contains putative nuclear localization signal (NLS) at its N-terminal, and translocates to the nucleus in cultured cells and in the neuroepithelial cells of chick embryos. We propose that the PRTG-ICD is cleaved by ?-secretase and translocates to the nucleus, which is potentially implicated in signaling for neural differentiation and in cell adhesion mediated by PRTG.
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