大阪大学 · 生化学・遺伝学・分子生物学
黒田俊一教授の研究室は、細胞内シグナル伝達のメカニズムに焦点を当てており、特にLIMドメインを有するタンパク質が細胞骨格や筋肉の発達、心筋の肥大反応に関与する分子機構を解明しています。PKCやFEZ1、ENHといったシグナル分子の相互作用やリン酸化制御、膜移動の動態を解析することで、発生・発達や心臓病態における力学的ストレス応答の分子基盤を解明しています。また、NELL1がMAPK経路を介して骨形成を誘導するメカニズムの解明も進めており、再生医療への応用が期待されています。
Figures are computed from collected data and may differ slightly.
The LIM domain comprising two zinc-finger motifs is found in a variety of proteins and has been proposed to direct protein-protein interactions. During the identification of protein kinase C (PKC)-interacting proteins by a yeast two-hybrid assay, a novel protein containing three LIM domains, designated ENH, was shown to associate with PKC in an isoform-specific manner. Deletion analysis demonstrated that any single LIM domain of ENH associates with the NH2-terminal region of PKC. ENH associated
By the yeast two-hybrid screening of a rat brain cDNA library with the regulatory domain of protein kinase C zeta (PKCzeta) as a bait, we have cloned a gene coding for a novel PKCzeta-interacting protein homologous to the Caenorhabditis elegans UNC-76 protein involved in axonal outgrowth and fasciculation. The protein designated FEZ1 (fasciculation and elongation protein zeta-1) consisting of 393 amino acid residues shows a high Asp/Glu content and contains several regions predicted to form amph
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAlanine dehydrogenases from two Bacillus species with distinct thermostabilities: molecular cloning, DNA and protein sequence determination, and structural comparison with other NAD(P)+-dependent dehydrogenasesShunichi Kuroda, Katsuyuki Tanizawa, Hidehiko Tanaka, Kenji Soda, and Yonekazu SakamotoCite this: Biochemistry 1990, 29, 4, 1009–1015Publication Date (Print):January 30, 1990Publication History Published online1 May 2002Published inissue 30 Janua
NELL1 is an extracellular protein inducing osteogenic differentiation and bone formation of osteoblastic cells. To elucidate the intracellular signaling cascade evoked by NELL1, we have shown that NELL1 protein transiently activates the MAPK signaling cascade, induces the phosphorylation of Runx2, and promotes the rapid intracellular accumulation of Tyr-phosphorylated proteins. Unlike BMP2, NELL1 protein does not activate the Smad signaling cascade. These findings suggest that upon binding to a
Antagonistic splice variants of ENH may play a central role in the adaptive changes of the link between mechanical stress-sensing and signalling occurring during embryonic development and/or heart hypertrophy.
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