The University of Osaka · 생화학·유전·분자생물학
Kuroda 교수의 연구실은 신호전달 및 세포 성장 조절을 담당하는 단백질 상호작용, 특히 LIM 도메인을 가진 단백질과 프로테인 키나제 C(PKC) 간의 상호작용을 중심으로 연구를 진행하고 있습니다. 특히 ENH와 FEZ1과 같은 신호전달 단백질이 세포 내에서 기계적 자극에 반응하여 세그멘테이션 및 심장 비대와 같은 생리적 변화를 유도하는 메커니즘을 규명하고 있습니다. 또한, 뼈 형성 유도 단백질 NELL1이 MAPK 경로를 통해 신호를 전달하는 방식을 밝혀내며, 세포 내 신호 전달의 다양성과 조절 메커니즘을 탐구하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
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.
