2. Academic Validation
  3. MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1

MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1

  • Biochem Biophys Res Commun. 2008 Dec 12;377(2):573-578. doi: 10.1016/j.bbrc.2008.10.038.
Hideo Nonaka 1,  Kimiko Takei 1,  Masato Umikawa 1,  Minoru Oshiro 1,  Kouichi Kuninaka 1,  Maitsetseg Bayarjargal 1,  Tsuyoshi Asato 1,  Yoshito Yamashiro 1,  Yukiko Uechi 2,  Shogo Endo 3,  Tatsuo Suzuki 4,  Ken-Ichi Kariya 5
Affiliations

Affiliations

  • 1 Division of Cell Biology, Graduate School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara-cho, Okinawa 903-0215, Japan.
  • 2 Division of Cell Biology, Graduate School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara-cho, Okinawa 903-0215, Japan; Unit for Molecular Neurobiology of Learning and Memory, Initial Research Project, Okinawa Institute of Science and Technology, Japan.
  • 3 Unit for Molecular Neurobiology of Learning and Memory, Initial Research Project, Okinawa Institute of Science and Technology, Japan.
  • 4 Department of Neuroplasticity, Shinshu University Graduate School of Medicine, Japan.
  • 5 Division of Cell Biology, Graduate School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara-cho, Okinawa 903-0215, Japan. Electronic address: [email protected].
PMID: 18930710 DOI: 10.1016/j.bbrc.2008.10.038
Abstract

Rap1 and Rap2 are similar Ras-like G proteins but perform distinct functions. By the affinity chromatography/mass-spectrometry approach and the yeast two-hybrid screening, we identified Misshapen/NIKs-related kinase (MINK) as a novel Rap2-interacting protein that does not interact with Rap1 or Ras. MINK is a member of the STE20 group of mitogen-activated protein kinase kinase kinase kinases. The interaction between MINK and Rap2 was GTP-dependent and required Phe39 within the effector region of Rap2; the corresponding residue in Rap1 and Ras is Ser. MINK was enriched in the brain, and both MINK and its close relative, Traf2- and Nck-interacting kinase (TNIK), interacted with a postsynaptic scaffold protein containing tetratricopeptide repeats, ankyrin repeats and a coiled-coil region (TANC1) and induced its phosphorylation, under control of Rap2 in cultured cells. These are novel actions of MINK and TNIK, and consistent with a role of MINK as a Rap2 effector in the brain.

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