@article{694e618669194eff9b858a96b86218ca,
title = " Glucose-regulated protein 78 (GRP78) binds directly to PIP 3 phosphatase SKIP and determines its localization ",
abstract = " Skeletal muscle and kidney-enriched inositol polyphosphate phosphatase (SKIP), a PIP 3 phosphatase, has been implicated in the regulation of insulin signaling in skeletal muscle. SKIP interacts with Pak1 and glucose-regulated protein 78 (GRP78), both of which are necessary for the regulation of insulin signaling. In this study, we showed that GRP78 directly binds to the SKIP C-terminal homology (SKICH) domain of SKIP and that this binding is necessary for the localization of SKIP at the ER. In addition, in vitro binding analysis showed that GRP78 and Pak1 competitively bind to SKIP. Taken together, these findings suggest a model by which GRP78 regulates intracellular localization of SKIP and how SKIP binds to Pak1 on insulin stimulation. ",
author = "Takeshi Ijuin and Naoya Hatano and Tadaomi Takenawa",
note = "Funding Information: We thank Dr Daizo Hamada (Kobe University Graduate School of Medicine) for helpful discussions and assistance. This work was supported in part by grants from T.I. from Japan society for the Promotion of Science (JSPS; Kakenhi Grant Number, 25460365). Additionally, this work was grant-in-aid from T. T., supported by the Ministry of Education, Culture, Sports, Science, and Technology (Kakenhi Grant Number Scientific Research, 23227005). These funding agencies had no role in the study design, data collection and analysis, decision to publish, and presentation of the manuscript. The authors declare that there are no competing interests. Publisher Copyright: {\textcopyright} 2016 the Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.",
year = "2016",
month = may,
day = "1",
doi = "10.1111/gtc.12353",
language = "English",
volume = "21",
pages = "457--465",
journal = "Genes to Cells",
issn = "1356-9597",
publisher = "Wiley-Blackwell",
number = "5",
}