Saitohin, which is nested within the tau gene, interacts with tau and Abl and its human-specific allele influences Abl phosphorylation
Document Type
Journal ArticlePublication Date
2011-11-01Keywords
AllelesAmino Acid Sequence
Base Sequence
Blotting, Western
Humans
Immunoprecipitation
Molecular Sequence Data
Phosphorylation
Protein Binding
Proto-Oncogene Proteins c-abl
Reverse Transcriptase Polymerase Chain Reaction
tau Proteins
Cell Biology
Metadata
Show full item recordAbstract
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.Source
J Cell Biochem. 2011 Nov;112(11):3482-8. doi: 10.1002/jcb.23279.DOI
10.1002/jcb.23279Permanent Link to this Item
http://hdl.handle.net/20.500.14038/25687PubMed ID
21769920Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1002/jcb.23279