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.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Wang Y,Gao L,Conrad CG,Andreadis Adoi
10.1002/jcb.23279subject
Has Abstractpub_date
2011-11-01 00:00:00pages
3482-8issue
11eissn
0730-2312issn
1097-4644journal_volume
112pub_type
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