Glucose-regulated protein 78 (GRP78) binds directly to PIP 3 phosphatase SKIP and determines its localization

Takeshi Ijuin, Naoya Hatano, Tadaomi Takenawa

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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.

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

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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