Serine 62 is a phosphorylation site in folliculin, the Birt-Hogg-Dubé gene product |
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Authors: | Lu Wang Xianghua Piao Yumiko Takagi Hikari Taka Masaaki Abe Yoshiaki Hagiwara Izumi Matsumoto Okio Hino |
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Institution: | a Department of Pathology and Oncology, Juntendo University School of Medicine, Tokyo 113-8421, Japan b Respiratory Medicine, Juntendo University School of Medicine, Tokyo 113-8421, Japan c Division of Proteomics and BioMolecular Science, Juntendo University School of Medicine, Tokyo 113-8421, Japan d Research and Development, Immuno-Biological Laboratories Co., Ltd., Fujioka-shi, Gunma 375-0005, Japan e Research Administration, Dainippon Sumitomo Pharma Co., Ltd., Osaka 564-0053, Japan f Safety Research Laboratories, Dainippon Sumitomo Pharma Co., Ltd., Osaka 554-0022, Japan |
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Abstract: | Recently, it was reported that the product of Birt-Hogg-Dubé syndrome gene (folliculin, FLCN) is directly phosphorylated by 5′-AMP-activated protein kinase (AMPK). In this study, we identified serine 62 (Ser62) as a phosphorylation site in FLCN and generated an anti-phospho-Ser62-FLCN antibody. Our analysis suggests that Ser62 phosphorylation is indirectly up-regulated by AMPK and that another residue is directly phosphorylated by AMPK. By binding with FLCN-interacting proteins (FNIP1 and FNIP2/FNIPL), Ser62 phosphorylation is increased. A phospho-mimic mutation at Ser62 enhanced the formation of the FLCN-AMPK complex. These results suggest that function(s) of FLCN-AMPK-FNIP complex is regulated by Ser62 phosphorylation.Structured summaryMINT-7298145, MINT-7298166: Flcn (uniprotkb:Q76JQ2) physically interacts (MI:0915) with AMPK alpha 1 (uniprotkb:P54645) by anti tag coimmunoprecipitation (MI:0007)MINT-7298267: AMPK alpha 1 (uniprotkb:Q13131) phosphorylates (MI:0217) tsc2 (uniprotkb:P49816) by protein kinase assay (MI:0424)MINT-7298182: FNIP1 (uniprotkb:Q8TF40) physically interacts (MI:0915) with Flcn (uniprotkb:Q76JQ2) by anti tag coimmunoprecipitation (MI:0007)MINT-7298132: AMPK alpha 1 (uniprotkb:Q13131) phosphorylates (MI:0217) Flcn (uniprotkb:Q76JQ2) by protein kinase assay (MI:0424)MINT-7298229: FNIPL (uniprotkb:Q9P278) physically interacts (MI:0915) with Flcn (uniprotkb:Q76JQ2) by anti tag coimmunoprecipitation (MI:0007) |
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Keywords: | AMPK 5&prime -AMP-activated protein kinase FLCN folliculin FNIP FLCN-interacting protein |
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