The University of Osaka · Biochemistry, Genetics and Molecular Biology
Professor Shun’ichi Kuroda’s research lab focuses on cellular signaling mechanisms, particularly the roles of LIM domain-containing proteins and their interactions in regulating cell growth, differentiation, and stress responses. The lab investigates key signaling pathways such as MAPK and PKC, with a strong emphasis on how protein-protein interactions and post-translational modifications mediate cellular responses in development and disease. A central theme is the molecular mechanisms underlying osteogenic differentiation and cardiac adaptation, including the function of proteins like NELL1 and ENH splice variants in mechanotransduction and tissue remodeling. The lab integrates molecular biology, biochemistry, and cell biology to dissect intracellular signaling cascades in physiological and pathological contexts.
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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