Tyrosine Kinase 2 Interacts with and Phosphorylates Receptor for Activated C Kinase-1, a WD Motif-Containing Protein | Zendy

Takashi Haro | Zendy; Kazuya Shimoda | Zendy; Haruko Kakumitsu | Zendy; Kenjirou Kamezaki | Zendy; Akihiko Numata | Zendy; Fumihiko Ishikawa | Zendy; Yuichi Sekine | Zendy; Ryuta Muromoto | Zendy; Tadashi Matsuda | Zendy; Mine Harada | Zendy

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Tyrosine Kinase 2 Interacts with and Phosphorylates Receptor for Activated C Kinase-1, a WD Motif-Containing Protein

Author(s) -

Takashi Haro,

Kazuya Shimoda,

Haruko Kakumitsu,

Kenjirou Kamezaki,

Akihiko Numata,

Fumihiko Ishikawa,

Yuichi Sekine,

Ryuta Muromoto,

Tadashi Matsuda,

Mine Harada

Publication year - 2004

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.173.2.1151

Subject(s) - phosphorylation , tropomyosin receptor kinase c , receptor tyrosine kinase , chemistry , tyrosine kinase , microbiology and biotechnology , protein kinase a , motif (music) , mitogen activated protein kinase kinase , receptor , platelet derived growth factor receptor , biochemistry , biology , growth factor , art , aesthetics

Receptor for activated C kinase (Rack)-1 is a protein kinase C-interacting protein, and contains a WD repeat but has no enzymatic activity. In addition to protein kinase C, Rack-1 also binds to Src, phospholipase Cgamma, and ras-GTPase-activating proteins. Thus, Rack-1 is thought to function as a scaffold protein that recruits specific signaling elements. In a cytokine signaling cascade, Rack-1 has been reported to interact with the IFN-alphabeta receptor and Stat1. In addition, we show here that Rack-1 associates with a member of Jak, tyrosine kinase 2 (Tyk2). Rack-1 interacts weakly with the kinase domain and interacts strongly with the pseudokinase domain of Tyk2. Rack-1 associates with Tyk2 via two regions, one in the N terminus and one in the middle portion (aa 138-203) of Rack-1. Jak activation causes the phosphorylation of tyrosine 194 on Rack-1. After phosphorylation, Rack-1 is translocated toward the perinuclear region. In addition to functioning as a scaffolding protein, these results raise the possibility that Rack-1 functions as a signaling molecule in cytokine signaling cascades.

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