HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Institute for Genetic Medicine >
Peer-reviewed Journal Articles, etc >

Phosphorylation-dependent Akt-Inversin interaction at the basal body of primary cilia

Creative Commons License

Files in This Item:
1346.full.pdf4.44 MBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Phosphorylation-dependent Akt-Inversin interaction at the basal body of primary cilia
Authors: Suizu, Futoshi Browse this author →KAKEN DB
Hirata, Noriyuki Browse this author
Kimura, Kohki Browse this author
Edamura, Tatsuma Browse this author
Tanaka, Tsutomu Browse this author
Ishigaki, Satoko Browse this author
Donia, Thoria Browse this author
Noguchi, Hiroko Browse this author
Iwanaga, Toshihiko Browse this author →KAKEN DB
Noguchi, Masayuki Browse this author →KAKEN DB
Keywords: Akt
primary cilia
signal transduction
Issue Date: 15-Jun-2016
Publisher: EMBO Press
Journal Title: EMBO Journal
Volume: 35
Issue: 12
Start Page: 1346
End Page: 1363
Publisher DOI: 10.15252/embj.201593003
Abstract: A primary cilium is a microtubule-based sensory organelle that plays an important role in human development and disease. However, regulation of Akt in cilia and its role in ciliary development has not been demonstrated. Using yeast two-hybrid screening, we demonstrate that Inversin (INVS) interacts with Akt. Mutation in the INVS gene causes nephronophthisis type II (NPHP2), an autosomal recessive chronic tubulointerstitial nephropathy. Co-immunoprecipitation assays show that Akt interacts with INVS via the C-terminus. In vitro kinase assays demonstrate that Akt phosphorylates INVS at amino acids 864-866 that are required not only for Akt interaction, but also for INVS dimerization. Co-localization of INVS and phosphorylated form of Akt at the basal body is augmented by PDGF-AA. Akt-null MEF cells as well as siRNA-mediated inhibition of Akt attenuated ciliary growth, which was reversed by Akt reintroduction. Mutant phosphodeador NPHP2-related truncated INVS, which lack Akt phosphorylation sites, suppress cell growth and exhibit distorted lumen formation and misalignment of spindle axis during cell division. Further studies will be required for elucidating functional interactions of Akt-INVS at the primary cilia for identifying the molecular mechanisms underlying NPHP2.
Type: article
Appears in Collections:遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 野口 昌幸

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


Feedback - Hokkaido University