TAILIEUCHUNG - Báo cáo khoa học: Phosphorylation of the large subunit of replication factor C is associated with adipocyte differentiation

Adipocyte differentiation is an ordered multistep process requiring the sequential activation of several groups of adipogenic transcription factors, including CCAAT⁄enhancer-binding protein-a and peroxisome prolifera-tor-activated receptor-c, and coactivators. Here we show that replication factor C 140, which was known to act as a coactivator for CCAAT⁄ | ỊFEBS Journal Phosphorylation of the large subunit of replication factor C is associated with adipocyte differentiation Min Jung Park1 Min Young Lee1 Jung Hae Choi1 Hyun Kook Cho1 Yung Hyun Choi2 Ung Suk Yang3 and JaeHun Cheong1 1 Department of Molecular Biology Pusan National university Jang-Jeon Dong Keum-Jeong Gu Busan Korea 2 Department of Biochemistry College of OrientalMedicine Dongeui University Busan Korea 3 Department of InternalMedicine Bongseng Memorial Hospital Busan Korea Keywords adipocyte differentiation CaMKII C EBPa phosphorylation RFC140 Correspondence J. Cheong Department of Molecular Biology Pusan NationalUniversity Busan 607-935 Korea Fax 82 51 513 9258 Tel 82 51 510 2277 E-mail molecule85@ Received 31 October 2006 revised 14 December 2006 accepted 22 December 2006 doi Adipocyte differentiation is an ordered multistep process requiring the sequential activation of several groups of adipogenic transcription factors including CCAAT enhancer-binding protein-a and peroxisome prolifera-tor-activated receptor-y and coactivators. Here we show that replication factor C 140 which was known to act as a coactivator for CCAAT enhancer-binding protein-a in our previous study was phosphorylated on the proliferating cell nuclear antigen-bindng domain during the adipocyte differentiation process. Calmodulin-dependent protein kinase II was responsible for phosphorylating replication factor C 140 in the process of adipocyte differentiation. Ser518 of replication factor C 140 was identified as a major target of calmodulin-dependent protein kinase II phosphorylation in vitro. Calmodulin-dependent protein kinase II inhibitor attenuated phosphorylation of replication factor C 140 by differentiation inducers and blocked replication factor C 140-derived transcriptional activation. Taken together these findings demonstrate that calmodulin-dependent protein kinase II signaling leads the cooperative transactivation of CCAA-T .

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