The novel circFKBP8/miR-432-5p/E2F7 cascade functions as a regulatory network in breast cancer. | The novel circFKBP8/miR-432-5p/E2F7 cascade functions as a regulatory network in breast cancer. Jin Z, Xu W, Yu K, Luo C, Luo X, Lian T, Liu C., Free PMC Article | 10/7/2024 |
GPX4 inhibits apoptosis of thyroid cancer cells through regulating the FKBP8/Bcl-2 axis. | GPX4 inhibits apoptosis of thyroid cancer cells through regulating the FKBP8/Bcl-2 axis. Dang T, Yu J, Yu Y, Jiang J, Shi Y, Yu S, Peng C, Min X, Xiong Y, Long P, Zhou W, Dai D., Free PMC Article | 06/6/2024 |
FKBP38 suppresses endometrial cancer cell proliferation and metastasis by inhibiting the mTOR pathway. | FKBP38 suppresses endometrial cancer cell proliferation and metastasis by inhibiting the mTOR pathway. Yan Y, Wang S, Zhang Z, Tang M, Zhao AZ, Li Z, Wu X, Li F. | 02/4/2024 |
FKBP38 Regulates Self-Renewal and Survival of GBM Neurospheres. | FKBP38 Regulates Self-Renewal and Survival of GBM Neurospheres. Dowling AL, Walbridge S, Ertekin C, Namagiri S, Camacho K, Chowdhury A, Bryant JP, Kohut E, Heiss JD, Brown DA, Kumbar SG, Banasavadi-Siddegowda YK., Free PMC Article | 11/15/2023 |
Tacrolimus-binding protein FKBP8 directs myosin light chain kinase-dependent barrier regulation and is a potential therapeutic target in Crohn's disease. | Tacrolimus-binding protein FKBP8 directs myosin light chain kinase-dependent barrier regulation and is a potential therapeutic target in Crohn's disease. Zuo L, Kuo WT, Cao F, Chanez-Paredes SD, Zeve D, Mannam P, Jean-François L, Day A, Vallen Graham W, Sweat YY, Shashikanth N, Breault DT, Turner JR., Free PMC Article | 04/7/2023 |
[Fkbp38 deletion induces premature ovarian insufficiency in mice by activating mTOR signaling and inducing granulosa cell apoptosis]. | [Fkbp38 deletion induces premature ovarian insufficiency in mice by activating mTOR signaling and inducing granulosa cell apoptosis]. Zhou Y, Zhao H, Shuai L, She J, Diao R, Wang L., Free PMC Article | 01/11/2023 |
FKBP8 is a novel molecule that participates in the regulation of the autophagic pathway. | FKBP8 is a novel molecule that participates in the regulation of the autophagic pathway. Aguilera MO, Robledo E, Melani M, Wappner P, Colombo MI. | 03/19/2022 |
FKBP8 variants are risk factors for spina bifida. | FKBP8 variants are risk factors for spina bifida. Tian T, Cao X, Kim SE, Lin YL, Steele JW, Cabrera RM, Karki M, Yang W, Marini NJ, Hoffman EN, Han X, Hu C, Wang L, Wlodarczyk BJ, Shaw GM, Ren A, Finnell RH, Lei Y., Free PMC Article | 08/28/2021 |
FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. | FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. Yoo SM, Yamashita SI, Kim H, Na D, Lee H, Kim SJ, Cho DH, Kanki T, Jung YK. | 10/3/2020 |
This study identifies FK506 binding protein 8 (FKBP8) as a candidate interacting protein of VISA through the yeast two-hybrid technique. A novel function of FKBP8 in innate immunity antiviral signaling regulation was revealed in this study. | FKBP8 inhibits virus-induced RLR-VISA signaling. Xu SS, Xu LG, Yuan C, Li SN, Chen T, Wang W, Li C, Cao L, Rao H. | 02/15/2020 |
Results demonstrated that FKBP8 physically interacts and co-localizes with SPP in endoplasmic reticulum, supporting that FKBP8 is a bona fide substrate of SPP. Also, the data support the involvement of inverse regulation of FKBP8 and mTOR signaling in SPP-enhanced tumorigenicity. | Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation. Hsu FF, Chou YT, Chiang MT, Li FA, Yeh CT, Lee WH, Chau LY. | 05/18/2019 |
FKBP8 Enhances Protein Stability of the CLC-1 Chloride Channel at the Plasma Membrane | FKBP8 Enhances Protein Stability of the CLC-1 Chloride Channel at the Plasma Membrane. Peng YJ, Lee YC, Fu SJ, Chien YC, Liao YF, Chen TY, Jeng CJ, Tang CY., Free PMC Article | 03/16/2019 |
Cycling between the inactive GDP- and the active GTP-bound state modulates the backbone dynamics of a C-terminal truncated form, RhebDeltaCT, which is suggested to influence its interactions. We further investigated the interactions between RhebDeltaCT and the proposed Rheb-binding domain of the regulatory protein FKBP38. | NMR analysis of the backbone dynamics of the small GTPase Rheb and its interaction with the regulatory protein FKBP38. De Cicco M, Kiss L, Dames SA. | 12/1/2018 |
Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described. | Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β. Peng YJ, Huang JJ, Wu HH, Hsieh HY, Wu CY, Chen SC, Chen TY, Tang CY., Free PMC Article | 05/19/2018 |
Co-expression of FKBP8 with LC3A profoundly induces Parkin-independent mitophagy. Strikingly, even when acting as a mitophagy receptor, FKBP8 avoids degradation by escaping from mitochondria. In summary, this study identifies novel roles for FKBP8 and LC3A, which act together to induce mitophagy. | FKBP8 recruits LC3A to mediate Parkin-independent mitophagy. Bhujabal Z, Birgisdottir ÅB, Sjøttem E, Brenne HB, Øvervatn A, Habisov S, Kirkin V, Lamark T, Johansen T., Free PMC Article | 02/24/2018 |
FKBP8 binding to Hsp90 did not substantially influence its ATPase activity | The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90. Blundell KL, Pal M, Roe SM, Pearl LH, Prodromou C., Free PMC Article | 09/9/2017 |
The information presented here provides important clues for understanding the catalytic activity of FKBP38, its regulation by the unique N-terminal extension, and the potential calcium- and calmodulin-mediated activation of FKBP38. | Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS., Free PMC Article | 07/12/2014 |
Overexpression of permanently active S100P in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2, resulting in the suppression of Bcl-2 stability | Ca2+/S100 proteins inhibit the interaction of FKBP38 with Bcl-2 and Hsp90. Shimamoto S, Tsuchiya M, Yamaguchi F, Kubota Y, Tokumitsu H, Kobayashi R. | 04/19/2014 |
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability | FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability. Hutt DM, Roth DM, Chalfant MA, Youker RT, Matteson J, Brodsky JL, Balch WE., Free PMC Article | 09/22/2012 |
The derived structure model of the complex between Bcl-2 and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 interaction by Ca(2+). | The FKBP38 catalytic domain binds to Bcl-2 via a charge-sensitive loop. Haupt K, Jahreis G, Linnert M, Maestre-Martínez M, Malesevic M, Pechstein A, Edlich F, Lücke C., Free PMC Article | 08/25/2012 |
Data support a dual role for FKBP38 in regulating CFTR synthesis and post-translational folding. | FKBP38 peptidylprolyl isomerase promotes the folding of cystic fibrosis transmembrane conductance regulator in the endoplasmic reticulum. Banasavadi-Siddegowda YK, Mai J, Fan Y, Bhattacharya S, Giovannucci DR, Sanchez ER, Fischer G, Wang X., Free PMC Article | 03/31/2012 |
a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR and allosterically stimulates the catalytic activity of mTORC1. | Phosphatidic acid activates mammalian target of rapamycin complex 1 (mTORC1) kinase by displacing FK506 binding protein 38 (FKBP38) and exerting an allosteric effect. Yoon MS, Sun Y, Arauz E, Jiang Y, Chen J., Free PMC Article | 10/22/2011 |
this charge-sensitive site in the FKBP domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2+) | A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding. Maestre-Martínez M, Haupt K, Edlich F, Neumann P, Parthier C, Stubbs MT, Fischer G, Lücke C. | 07/30/2011 |
These results demonstrate that FKBP38 is a novel regulator of the oncogenic protein PRL-3 abundance and that alteration in the stability of PRL-3 can have a dramatic impact on cell proliferation. | The essential role of FKBP38 in regulating phosphatase of regenerating liver 3 (PRL-3) protein stability. Choi MS, Min SH, Jung H, Lee JD, Lee TH, Lee HK, Yoo OJ. | 05/7/2011 |
novel insights into the structural arrangement of FKBP38/calmodulin complex | New structural aspects of FKBP38 activation. Maestre-Martínez M, Haupt K, Edlich F, Jahreis G, Jarczowski F, Erdmann F, Fischer G, Lücke C. | 02/26/2011 |