Glucose-regulated protein 78 (GRP78) binds directly to PIP3 phosphatase SKIP and determines its localization

Takeshi Ijuin, Naoya Hatano, Tadaomi Takenawa

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Skeletal muscle and kidney-enriched inositol polyphosphate phosphatase (SKIP), a PIP3 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.

Original languageEnglish
Pages (from-to)457-465
Number of pages9
JournalGenes to Cells
Volume21
Issue number5
DOIs
Publication statusPublished - May 1 2016
Externally publishedYes

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Phosphoric Monoester Hydrolases
Insulin
Skeletal Muscle
Polyphosphates
Kidney
glucose-regulated proteins

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Glucose-regulated protein 78 (GRP78) binds directly to PIP3 phosphatase SKIP and determines its localization. / Ijuin, Takeshi; Hatano, Naoya; Takenawa, Tadaomi.

In: Genes to Cells, Vol. 21, No. 5, 01.05.2016, p. 457-465.

Research output: Contribution to journalArticle

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