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https://www.readbyqxmd.com/read/28419802/programming-post-translational-control-over-the-metabolic-labeling-of-cellular-proteins-with-a-non-canonical-amino-acid
#1
Emily E Thomas, Naresh Pandey, Sarah E Knudsen, Zachary T Ball, Jonathan J Silberg
Transcriptional control can be used to program cells to label proteins with non-canonical amino acids by regulating the expression of orthogonal aminoacyl tRNA synthetases (aaRSs). However, we cannot yet program cells to control labeling in response to aaRS and ligand binding. To identify aaRSs whose activities can be regulated by interactions with ligands, we used a combinatorial approach to discover fragmented variants of Escherichia coli methionyl tRNA synthetase (MetRS) that require fusion to associating proteins for maximal activity...
April 18, 2017: ACS Synthetic Biology
https://www.readbyqxmd.com/read/28391244/introducing-inducible-fluorescent-split-cholesterol-oxidase-to-mammalian-cells
#2
Konstantin G Chernov, Maarit Neuvonen, Ivonne Brock, Elina Ikonen, Vladislav V Verkhusha
Cholesterol oxidase (COase) is a bacterial enzyme catalyzing the first step in the biodegradation of cholesterol. COase is an important biotechnological tool for clinical diagnostics and production of steroid drugs and insecticides. It is also used for tracking of intracellular cholesterol, however, its utility is limited by the lack of an efficient temporal control of its activity. To overcome this, we have developed a regulatable fragment complementation system for COase cloned from Chromobacterium sp. The enzyme was split into two moieties that were fused to FKBP (FK506-binding protein) and FRB (rapamycin-binding domain) pair and split GFP fragments...
April 7, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28381481/fkbp8-recruits-lc3a-to-mediate-parkin-independent-mitophagy
#3
Zambarlal Bhujabal, Åsa B Birgisdottir, Eva Sjøttem, Hanne B Brenne, Aud Øvervatn, Sabrina Habisov, Vladimir Kirkin, Trond Lamark, Terje Johansen
Mitophagy, the selective removal of damaged or excess mitochondria by autophagy, is an important process in cellular homeostasis. The outer mitochondrial membrane (OMM) proteins NIX, BNIP3, FUNDC1, and Bcl2-L13 recruit ATG8 proteins (LC3/GABARAP) to mitochondria during mitophagy. FKBP8 (also known as FKBP38), a unique member of the FK506-binding protein (FKBP) family, is similarly anchored in the OMM and acts as a multifunctional adaptor with anti-apoptotic activity. In a yeast two-hybrid screen, we identified FKBP8 as an ATG8-interacting protein...
April 5, 2017: EMBO Reports
https://www.readbyqxmd.com/read/28325828/the-prolyl-isomerase-pin1-is-a-novel-target-of-6-7-4-trihydroxyisoflavone-for-suppressing-esophageal-cancer-growth
#4
Tae-Gyu Lim, Sung-Young Lee, Zhaoheng Duan, Mee-Hyun Lee, Hanyong Chen, Fangfang Liu, Kangdong Liu, Sung Keun Jung, Dong Joon Kim, Ann M Bode, Ki Won Lee, Zigang Dong
Intake of soy isoflavones is inversely associated with the risk of esophageal cancer. Numerous experimental results have supported the anticancer activity of soy isoflavones. This study aimed to determine the anti-esophageal cancer activity of 6,7,4'-trihydroxyisoflavone (6,7,4'-THIF), a major metabolite of daidzein, which is readily metabolized in the human body. Notably, 6,7,4'-THIF inhibited proliferation and increased apoptosis of esophageal cancer cells. On the basis of a virtual screening analysis, Pin1 was identified as a target protein of 6,7,4'-THIF...
March 21, 2017: Cancer Prevention Research
https://www.readbyqxmd.com/read/28287617/small-molecule-induced-domain-swapping-as-a-mechanism-for-controlling-protein-function-and-assembly
#5
Joshua M Karchin, Jeung-Hoi Ha, Kevin E Namitz, Michael S Cosgrove, Stewart N Loh
Domain swapping is the process by which identical proteins exchange reciprocal segments to generate dimers. Here we introduce induced domain swapping (INDOS) as a mechanism for regulating protein function. INDOS employs a modular design consisting of the fusion of two proteins: a recognition protein that binds a triggering molecule, and a target protein that undergoes a domain swap in response to binding of the triggering ligand. The recognition protein (FK506 binding protein) is inserted into functionally-inactivated point mutants of two target proteins (staphylococcal nuclease and ribose binding protein)...
March 13, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28274284/the-antimalarial-action-of-fk506-and-rapamycin-evidence-for-a-direct-effect-on-fk506-binding-protein-pffkbp35
#6
Paul Monaghan, Darren B Leneghan, Wesley Shaw, Angus Bell
FK506 and rapamycin (Rap) are immunosuppressive drugs that act principally on T-lymphocytes. The receptors for both drugs are FK506-binding proteins (FKBPs), but the molecular mechanisms of immunosuppression differ. An FK506-FKBP complex inhibits the protein phosphatase calcineurin, blocking a key step in T-cell activation, while the Rap -FKBP complex binds to the protein kinase target of rapamycin (TOR), which is involved in a subsequent signalling pathway. Both drugs, and certain non-immunosuppressive compounds related to FK506, have potent antimalarial activity...
March 9, 2017: Parasitology
https://www.readbyqxmd.com/read/28273459/anterograde-transport-of-rab4-associated-vesicles-regulates-synapse-organization-in-drosophila
#7
Swagata Dey, Gary Banker, Krishanu Ray
Local endosomal recycling at synapses is essential to maintain neurotransmission. Rab4GTPase, found on sorting endosomes, is proposed to balance the flow of vesicles among endocytic, recycling, and degradative pathways in the presynaptic compartment. Here, we report that Rab4-associated vesicles move bidirectionally in Drosophila axons but with an anterograde bias, resulting in their moderate enrichment at the synaptic region of the larval ventral ganglion. Results from FK506 binding protein (FKBP) and FKBP-Rapamycin binding domain (FRB) conjugation assays in rat embryonic fibroblasts together with genetic analyses in Drosophila indicate that an association with Kinesin-2 (mediated by the tail domain of Kinesin-2α/KIF3A/KLP64D subunit) moves Rab4-associated vesicles toward the synapse...
March 7, 2017: Cell Reports
https://www.readbyqxmd.com/read/28257089/blockade-of-y177-and-nuclear-translocation-of-bcr-abl-inhibits-proliferation-and-promotes-apoptosis-in-chronic-myeloid-leukemia-cells
#8
Qianyin Li, Zhenglan Huang, Miao Gao, Weixi Cao, Qin Xiao, Hongwei Luo, Wenli Feng
The gradual emerging of resistance to imatinib urgently calls for the development of new therapy for chronic myeloid leukemia (CML). The fusion protein Bcr-Abl, which promotes the malignant transformation of CML cells, is mainly located in the cytoplasm, while the c-Abl protein which is expressed in the nucleus can induce apoptosis. Based on the hetero-dimerization of FKBP (the 12-kDa FK506- and rapamycin-binding protein) and FRB (the FKBP-rapamycin binding domain of the protein kinase, mTOR) mediated by AP21967, we constructed a nuclear transport system to induce cytoplasmic Bcr-Abl into nuclear...
March 2, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28251183/opposing-transcriptional-mechanisms-regulate-toxoplasma-development
#9
Dong-Pyo Hong, Joshua B Radke, Michael W White
The Toxoplasma biology that underlies human chronic infection is developmental conversion of the acute tachyzoite stage into the latent bradyzoite stage. We investigated the roles of two alkaline-stress-induced ApiAP2 transcription factors, AP2IV-3 and AP2IX-9, in bradyzoite development. These factors were expressed in two overlapping waves during bradyzoite development, with AP2IX-9 increasing expression earlier than AP2IV-3, which peaked as AP2IX-9 expression was declining. Disruption of the AP2IX-9 gene enhanced, while deletion of AP2IV-3 gene decreased, tissue cyst formation, demonstrating that these factors have opposite functions in bradyzoite development...
January 2017: MSphere
https://www.readbyqxmd.com/read/28236226/nmr-resonance-assignments-of-the-fkbp-domain-of-human-aryl-hydrocarbon-receptor-interacting-protein-like-1-aipl1-in-complex-with-a-farnesyl-ligand
#10
Liping Yu, Ravi P Yadav, Nikolai O Artemyev
Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a specialized chaperone of phosphodiesterase 6, a key effector enzyme in the phototransduction cascade. The FKBP domain of AIPL1 is known to bind the farnesyl moiety of PDE6. Mutations in AIPL1, including many missense mutations in the FKBP domain, have been associated with Leber congenital amaurosis, a severe blinding disease. Here, we report the backbone and sidechain assignments of the N-terminal FKBP(Δloop) (with a loop deletion) of AIPL1 in complex with a farnesyl ligand...
April 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/28077437/sensitized-signalling-between-l-type-ca2-channels-and-ryanodine-receptors-in-the-absence-or-inhibition-of-fkbp12-6-in-cardiomyocytes
#11
Yan-Ting Zhao, Yun-Bo Guo, Lei Gu, Xue-Xin Fan, Hua-Qian Yang, Zheng Chen, Peng Zhou, Qi Yuan, Guang-Ju Ji, Shi-Qiang Wang
Aims: The heart contraction is controlled by the Ca2+-induced Ca2+ release (CICR) between L-type Ca2+ channels and ryanodine receptors (RyRs). The FK506-binding protein FKBP12.6 binds to RyR subunits, but its role in stabilizing RyR function has been debated for long. Recent reports of high-resolution RyR structure show that the HD2 domain that binds to the SPRY2 domain of neighbouring subunit in FKBP-bound RyR1 is detached and invisible in FKBP-null RyR2. The present study was to test the consequence of FKBP12...
March 1, 2017: Cardiovascular Research
https://www.readbyqxmd.com/read/28000119/overexpression-of-phytochelatin-synthase-pcs-enhances-abiotic-stress-tolerance-by-altering-the-proteome-of-transformed-anabaena-sp-pcc-7120
#12
Neha Chaurasia, Yogesh Mishra, Antra Chatterjee, Ruchi Rai, Shivam Yadav, L C Rai
The present study provides data on the insertion of an extra copy of phytochelatin synthase (alr0975) in Anabaena sp. PCC 7120. The recombinant strain (AnFPN-pcs) compared to wild type showed approximately 22.3% increase in growth rate under UV-B, NaCl, heat, CuCl2, carbofuran, and CdCl2. It also registered 2.25-fold enhanced nitrogenase activity and 5-fold higher phytochelatin production. A comparison of the protein profile of wild type with the recombinant strain revealed that recombinant strain accumulated proteins belonging to the following categories: (i) detoxification (nutrient stress induced DNA binding protein, Mn-SOD, Alr0946 (CalA)), (ii) protein folding and modification (molecular chaperone DnaK, FKBP-type peptidyl-prolyl cis-trans isomerase), (iii) nucleotide and amino acid biosynthesis (dihydroorotase and Ketol-acid reductoisomerase), (iv) photosynthesis and respiration (coproporphyrinogen III oxidase, phycocyanin alpha chain, ferredoxin-NADP(+) reductase), and (v) transport (sugar transport ATP-binding protein)...
December 20, 2016: Protoplasma
https://www.readbyqxmd.com/read/27994056/inducible-inhibition-of-g%C3%AE-%C3%AE-reveals-localization-dependent-functions-at-the-plasma-membrane-and-golgi
#13
Lauren M Klayman, Philip B Wedegaertner
Heterotrimeric G proteins signal at a variety of endomembrane locations, in addition to their canonical function at the cytoplasmic surface of the plasma membrane (PM), where they are activated by cell surface G protein-coupled receptors. Here we focus on βγ signaling at the Golgi, where βγ activates a signaling cascade, ultimately resulting in vesicle fission from the trans-Golgi network (TGN). To develop a novel molecular tool for inhibiting endogenous βγ in a spatial-temporal manner, we take advantage of a lipid association mutant of the widely used βγ inhibitor GRK2ct (GRK2ct-KERE) and the FRB/FKBP heterodimerization system...
February 3, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27807044/golgi-enzymes-do-not-cycle-through-the-endoplasmic-reticulum-during-protein-secretion-or-mitosis
#14
Julien Villeneuve, Juan Duran, Margherita Scarpa, Laia Bassaganyas, Josse Van Galen, Vivek Malhotra
Golgi-specific sialyltransferase (ST) expressed as a chimera with the rapamycin-binding domain of mTOR, FRB, relocates to the endoplasmic reticulum (ER) in cells exposed to rapamycin that also express invariant chain (Ii)-FKBP in the ER. This result has been taken to indicate that Golgi-resident enzymes cycle to the ER constitutively. We show that ST-FRB is trapped in the ER even without Ii-FKBP upon rapamycin addition. This is because ER-Golgi-cycling FKBP proteins contain a C-terminal KDEL-like sequence, bind ST-FRB in the Golgi, and are transported together back to the ER by KDEL receptor-mediated retrograde transport...
January 1, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27738551/an-improved-reversibly-dimerizing-mutant-of-the-fk506-binding-protein-fkbp
#15
Juan J Barrero, Effrosyni Papanikou, Jason C Casler, Kasey J Day, Benjamin S Glick
FK506-binding protein (FKBP) is a monomer that binds to FK506, rapamycin, and related ligands. The F36M substitution, in which Phe36 in the ligand-binding pocket is changed to Met, leads to formation of antiparallel FKBP dimers, which can be dissociated into monomers by ligand binding. This FKBP(M) mutant has been employed in the mammalian secretory pathway to generate aggregates that can be dissolved by ligand addition to create cargo waves. However, when testing this approach in yeast, we found that dissolution of FKBP(M) aggregates was inefficient...
July 2016: Cellular Logistics
https://www.readbyqxmd.com/read/27664121/molecular-insights-into-substrate-recognition-and-catalytic-mechanism-of-the-chaperone-and-fkbp-peptidyl-prolyl-isomerase-slyd
#16
Esben M Quistgaard, Ulrich Weininger, Yonca Ural-Blimke, Kristofer Modig, Pär Nordlund, Mikael Akke, Christian Löw
BACKGROUND: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date, the interactions of these domains with unfolded proteins have remained rather obscure, with structural information on binding to the FKBP domain being limited to complexes involving various inhibitor compounds or a chemically modified tetrapeptide...
2016: BMC Biology
https://www.readbyqxmd.com/read/27658575/differential-dna-methylation-of-the-meiosis-specific-gene-fkbp6-in-testes-of-yak-and-cattle-yak-hybrids
#17
B Li, H Luo, Q Weng, S Wang, Z Pan, Z Xie, W Wu, H Liu, Q Li
FK506-binding protein 6 (FKBP6) is essential for meiosis during mammalian spermatogenesis. However, the molecular regulation of FKBP6 during spermatogenesis remains unclear. In the present study, we performed molecular characterization of the meiosis-specific gene FKBP6 in yak testes. Yak FKBP6 encodes a polypeptide of 295 amino acid residues with an FK506-binding domain (FKBP_C) and three tetratricopeptide repeat domains. The methylation level of the FKBP6 promoter in testes was significantly higher in cattle-yak with male sterility than in yak, and the FKBP6 promoter was methylated in liver tissues in which FKBP6 is not expressed...
December 2016: Reproduction in Domestic Animals, Zuchthygiene
https://www.readbyqxmd.com/read/27618008/physiological-and-pathogenic-roles-of-prolyl-isomerase-pin1-in-metabolic-regulations-via-multiple-signal-transduction-pathway-modulations
#18
REVIEW
Yusuke Nakatsu, Yasuka Matsunaga, Takeshi Yamamotoya, Koji Ueda, Yuki Inoue, Keiichi Mori, Hideyuki Sakoda, Midori Fujishiro, Hiraku Ono, Akifumi Kushiyama, Tomoichiro Asano
Prolyl isomerases are divided into three groups, the FKBP family, Cyclophilin and the Parvulin family (Pin1 and Par14). Among these isomerases, Pin1 is a unique prolyl isomerase binding to the motif including pSer/pThr-Pro that is phosphorylated by kinases. Once bound, Pin1 modulates the enzymatic activity, protein stability or subcellular localization of target proteins by changing the cis- and trans-formations of proline. Several studies have examined the roles of Pin1 in the pathogenesis of cancers and Alzheimer's disease...
September 7, 2016: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/27424905/an-aluc-based-molecular-tension-probe-for-sensing-intramolecular-protein-protein-interactions
#19
Sung-Bae Kim, Ryo Nishihara, Koji Suzuki
Optical imaging of protein-protein interactions (PPIs) facilitates comprehensive elucidation of intracellular molecular events. The present protocol demonstrates an optical measure for visualizing molecular tension triggered by any PPI in mammalian cells. A unique design of single-chain probes was fabricated, in which a full-length artificial luciferase (ALuc(®)) was sandwiched between two model proteins of interest, e.g., FKBP and FRB. A molecular tension probe comprising ALuc23 greatly enhances the bioluminescence in response to varying concentrations of rapamycin, and named "tension probe (TP)...
2016: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27374865/fk506-binding-protein-51-integrates-pathways-of-adaptation-fkbp51-shapes-the-reactivity-to-environmental-change
#20
Theo Rein
This review portraits FK506 binding protein (FKBP) 51 as "reactivity protein" and collates recent publications to develop the concept of FKBP51 as contributor to different levels of adaptation. Adaptation is a fundamental process that enables unicellular and multicellular organisms to adjust their molecular circuits and structural conditions in reaction to environmental changes threatening their homeostasis. FKBP51 is known as chaperone and co-chaperone of heat shock protein (HSP) 90, thus involved in processes ensuring correct protein folding in response to proteotoxic stress...
September 2016: BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology
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