Saitohin,which is nested within the tau gene,interacts with tau and Abl and its human‐specific allele influences Abl phosphorylation |
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| Authors: | Yan Wang Lei Gao Christopher G Conrad Athena Andreadis |
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| Institution: | 1. Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655;2. Shriver Center at University of Massachusetts Medical School, Waltham, Massachusetts 02452;3. Department of Pathology, Columbia University, New York, New York 10027 |
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| Abstract: | Saitohin (STH) is a gene unique to humans and their closest relatives whose function is not yet known. STH contains a single polymorphism (Q7R); the Q allele is human‐specific and confers susceptibility to several neurodegenerative diseases. In previous work, we discovered that STH interacts with Peroxiredoxin 6 (Prdx6), a unique member of that family which is bifunctional and whose levels increase in Pick's disease. In this study, we report that STH also interacts with tau and the non‐receptor tyrosine kinase c‐Abl (Abl). Furthermore, Abl phosphorylates STH on its single tyrosine residue and STH increases tyrosine phosphorylation by Abl. The effect of Saitohin on Abl‐mediated phosphorylation appears to be allele‐specific, providing evidence for a new cellular function for STH. J. Cell. Biochem. 112: 3482–3488, 2011. © 2011 Wiley Periodicals, Inc. |
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| Keywords: | SAITOHIN INTERACTIONS PRIMATE‐SPECIFIC GENE HUMAN‐SPECIFIC ALLELE MAP tau TYROSINE KINASE Abl ALLELE‐SPECIFIC EFFECTS NEURODEGENERATION |
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