1. Academic Validation
  2. 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: kariya@med.u-ryukyu.ac.jp.
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.

Figures