A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
A group of alicyclic hydrocarbons with the general formula R-C5H9.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.
An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.
A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.
Nocodazole is an antineoplastic agent which exerts its effect by depolymerizing microtubules.
A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Established cell cultures that have the potential to propagate indefinitely.
A group of often glycosylated macrocyclic compounds formed by chain extension of multiple PROPIONATES cyclized into a large (typically 12, 14, or 16)-membered lactone. Macrolides belong to the POLYKETIDES class of natural products, and many members exhibit ANTIBIOTIC properties.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.
Signaling proteins which function as master molecular switches by activating Rho GTPases through conversion of guanine nucleotides. Rho GTPases in turn control many aspects of cell behavior through the regulation of multiple downstream signal transduction pathways.
The 17-valerate derivative of BETAMETHASONE. It has substantial topical anti-inflammatory activity and relatively low systemic anti-inflammatory activity.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
Basic functional unit of plants.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.
A potent androgenic metabolite of TESTOSTERONE. It is produced by the action of the enzyme 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE.
Proteins, generally found in the CYTOPLASM, that specifically bind ANDROGENS and mediate their cellular actions. The complex of the androgen and receptor migrates to the CELL NUCLEUS where it induces transcription of specific segments of DNA.
Tumors or cancer of the PROSTATE.
Compounds that interact with ANDROGEN RECEPTORS in target tissues to bring about the effects similar to those of TESTOSTERONE. Depending on the target tissues, androgenic effects can be on SEX DIFFERENTIATION; male reproductive organs, SPERMATOGENESIS; secondary male SEX CHARACTERISTICS; LIBIDO; development of muscle mass, strength, and power.
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
A cell line derived from cultured tumor cells.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Tumors or cancer of the human BREAST.
A disorder resulting from a defect in the pattern of neuronal migration in which ectopic collections of neurons lie along the lateral ventricles of the brain or just beneath, contiguously or in isolated patches.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.

Generation of CD8(+) T-cell responses to Mycobacterium bovis and mycobacterial antigen in experimental bovine tuberculosis. (1/1373)

Protective immunity against tuberculosis is considered to be essentially cell mediated, and an important role for CD8(+) T lymphocytes has been suggested by several studies of murine and human infections. The present work, using an experimental model of infection with Mycobacterium bovis in cattle, showed that live M. bovis elicits the activation of CD8(+) T cells in vitro. However, a sonic extract prepared from M. bovis (MBSE) and protein purified derivative (PPDb) also induced a considerable degree of activation of the CD8(+) T cells. Analysis of proliferative responses of peripheral blood mononuclear cells, purified CD8(+) T cells, and CD8(+) T-cell clones to M. bovis and to soluble antigenic preparations (MBSE, PPDb) showed that the responses of all three types of cells were always superior for live mycobacteria but that strong responses were also obtained with complex soluble preparations. Furthermore, while cytotoxic capabilities were not investigated, the CD8(+) T cells were found to produce and release gamma interferon in response to antigen (live and soluble), which indicated one possible protective mechanism for these cells in bovine tuberculosis. Finally, it was demonstrated by metabolic inhibition with brefeldin A and cytochalasin D at the clonal level that an endogenous pathway of antigen processing is required for presentation to bovine CD8(+) cells and that presentation is also dependent on phagocytosis of the antigen.  (+info)

Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells. (2/1373)

LY-A strain is a Chinese hamster ovary cell mutant resistant to sphingomyelin (SM)-directed cytolysin and has a defect in de novo SM synthesis. Metabolic labeling experiments with radioactive serine, sphingosine, and choline showed that LY-A cells were defective in synthesis of SM from these precursors, but not syntheses of ceramide (Cer), glycosphingolipids, or phosphatidylcholine, indicating a specific defect in the conversion of Cer to SM in LY-A cells. In vitro experiments showed that the specific defect of SM formation in LY-A cells was not due to alterations in enzymatic activities responsible for SM synthesis or degradation. When cells were treated with brefeldin A, which causes fusion of the Golgi apparatus with the endoplasmic reticulum (ER), de novo SM synthesis in LY-A cells was restored to the wild-type level. Pulse-chase experiments with a fluorescent Cer analogue, N-(4,4-difluoro-5,7-dimethyl-4-bora-3a, 4a-diaza-s-indacene-3-pentanoyl)-D-erythro-sphingosine (C5-DMB-Cer), revealed that in wild-type cells C5-DMB-Cer was redistributed from intracellular membranes to the Golgi apparatus in an intracellular ATP-dependent manner, and that LY-A cells were defective in the energy-dependent redistribution of C5-DMB-Cer. Under ATP-depleted conditions, conversion of C5-DMB-Cer to C5-DMB-SM and of [3H]sphingosine to [3H]SM in wild-type cells decreased to the levels in LY-A cells, which were not affected by ATP depletion. ER-to-Golgi apparatus trafficking of glycosylphosphatidylinositol-anchored or membrane-spanning proteins in LY-A cells appeared to be normal. These results indicate that the predominant pathway of ER-to-Golgi apparatus trafficking of Cer for de novo SM synthesis is ATP dependent and that this pathway is almost completely impaired in LY-A cells. In addition, the specific defect of SM synthesis in LY-A cells suggests different pathways of Cer transport for glycosphingolipids versus SM synthesis.  (+info)

Assembly of very low density lipoprotein: a two-step process of apolipoprotein B core lipidation. (3/1373)

The liver plays a primary role in lipid metabolism. Important functions include the synthesis and incorporation of hydrophobic lipids, triacylglycerols and cholesteryl esters into the core of water-miscible particles called lipoproteins and the secretion of these particles into the circulation for transport to distant tissues. In this article, we present a brief overview of one aspect of the assembly process of very low density lipoproteins, namely, possible mechanisms for combining core lipids with apolipoprotein B. This is a complex process in which apolipoprotein B interacts with core lipids to form very low density lipoproteins by a two-step process that can be dissociated biochemically.  (+info)

Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors. (4/1373)

Protein secretion through the endoplasmic reticulum and Golgi vesicular trafficking system is initiated by the binding of ADP-ribosylation factors (ARFs) to donor membranes, leading to recruitment of coatomer, bud formation, and eventual vesicle release. ARFs are approximately 20-kDa GTPases that are active with bound GTP and inactive with GDP bound. Conversion of ARF-GDP to ARF-GTP is regulated by guanine nucleotide-exchange proteins. All known ARF guanine nucleotide-exchange proteins contain a Sec7 domain of approximately 200 amino acids that includes the active site and fall into two classes that differ in molecular size and susceptibility to inhibition by the fungal metabolite brefeldin A (BFA). To determine the structural basis of BFA sensitivity, chimeric molecules were constructed by using sequences from the Sec7 domains of BFA-sensitive yeast Sec7 protein (ySec7d) and the insensitive human cytohesin-1 (C-1Sec7). Based on BFA inhibition of the activities of these molecules with recombinant yeast ARF2 as substrate, the Asp965-Met975 sequence in ySec7d was shown to be responsible for BFA sensitivity. A C-1Sec7 mutant in which Ser199, Asn204, and Pro209 were replaced with the corresponding ySec7d amino acids, Asp965, Gln970, and Met975, exhibited BFA sensitivity similar to that of recombinant ySec7d (rySec7d). Single replacement in C-1Sec7 of Ser199 or Pro209 resulted in partial inhibition by BFA, whereas replacement of Gln970 in ySec7d with Asn (as found in C-1Sec7) had no effect. As predicted, the double C-1Sec7 mutant with S199D and P209M was BFA-sensitive, demonstrating that Asp965 and Met975 in ySec7d are major molecular determinants of BFA sensitivity.  (+info)

Intracellular trafficking pathways in the assembly of connexins into gap junctions. (5/1373)

Trafficking pathways underlying the assembly of connexins into gap junctions were examined using living COS-7 cells expressing a range of connexin-aequorin (Cx-Aeq) chimeras. By measuring the chemiluminescence of the aequorin fusion partner, the translocation of oligomerized connexins from intracellular stores to the plasma membrane was shown to occur at different rates that depended on the connexin isoform. Treatment of COS-7 cells expressing Cx32-Aeq and Cx43-Aeq with brefeldin A inhibited the movement of these chimera to the plasma membrane by 84 +/- 4 and 88 +/- 4%, respectively. Nocodazole treatment of the cells expressing Cx32-Aeq and Cx43-Aeq produced 29 +/- 16 and 4 +/- 7% inhibition, respectively. In contrast, the transport of Cx26 to the plasma membrane, studied using a construct (Cx26/43T-Aeq) in which the short cytoplasmic carboxyl-terminal tail of Cx26 was replaced with the extended carboxyl terminus of Cx43, was inhibited 89 +/- 5% by nocodazole and was minimally affected by exposure of cells to brefeldin A (17 +/-11%). The transfer of Lucifer yellow across gap junctions between cells expressing wild-type Cx32, Cx43, and the corresponding Cx32-Aeq and Cx43-Aeq chimeras was reduced by nocodazole treatment and abolished by brefeldin A treatment. However, the extent of dye coupling between cells expressing wild-type Cx26 or the Cx26/43T-Aeq chimeras was not significantly affected by brefeldin A treatment, but after nocodazole treatment, transfer of dye to neighboring cells was greatly reduced. These contrasting effects of brefeldin A and nocodazole on the trafficking properties and intercellular dye transfer are interpreted to suggest that two pathways contribute to the routing of connexins to the gap junction.  (+info)

Initiation of galactosaminoglycan biosynthesis. Separate galactosylation and dephosphorylation pathways for phosphoxylosylated decorin protein and exogenous xyloside. (6/1373)

By using various radiolabelled precursors, glycosylation and phosphorylation of decorin in a rat fibroblast cell line was investigated in the presence of increasing concentrations of p-nitrophenyl-O-beta-d-xylopyranoside. Decorin core protein glycanation was suppressed to approximately 25% of the normal level in the presence of 2 mm and 3 mm xyloside. Glycans/saccharides were released from the core protein and size-separated by gel chromatography. The intracellular decorin obtained from cells treated with 2 mm xyloside was substituted with Xyl and also with Gal-Xyl and Gal-Gal-Xyl, but not with longer saccharides. Only the trisaccharide contained an almost fully phosphorylated Xyl. We conclude that galactosylation of endogenous, xylosylated decorin and exogenous xyloside probably follow separate pathways or that xylosides and early decorin glycoforms are kept separated. At the addition of the first glucuronic acid the two pathways seem to merge and dephosphorylation of decorin takes place. Xyloside-primed and secreted galactosaminoglycan chains produced simultanously retained phosphorylated Xyl. Inadequate dephosphorylation could be due to excess substrate or to a short transit.time. As shown previously [Moses, J., Oldberg, A., Eklund, E. & Fransson, L.-A. (1997) Eur. J. Biochem. 248, 767-774], brefeldin A-arrested decorin is substituted with the linkage-region extended with an undersulphated and incomplete galactosaminoglycan chain. In cells treated with this drug, xylosides were unable to prime galactosaminoglycan synthesis and unable to inhibit glycosylation and phosporylation of decorin.  (+info)

Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. (7/1373)

We demonstrate that the major in vivo targets of brefeldin A (BFA) in the secretory pathway of budding yeast are the three members of the Sec7 domain family of ARF exchange factors: Gea1p and Gea2p (functionally interchangeable) and Sec7p. Specific residues within the Sec7 domain are important for BFA inhibition of ARF exchange activity, since mutations in these residues of Gea1p (sensitive to BFA) and of ARNO (resistant to BFA) reverse the sensitivity of each to BFA in vivo and in vitro. We show that the target of BFA inhibition of ARF exchange activity is an ARF-GDP-Sec7 domain protein complex, and that BFA acts to stabilize this complex to a greater extent for a BFA-sensitive Sec7 domain than for a resistant one.  (+info)

Hormonal regulation of oligopeptide transporter pept-1 in a human intestinal cell line. (8/1373)

The intestinal oligopeptide transporter (cloned as Pept-1) has major roles in protein nutrition and drug therapy. A key unstudied question is whether expression of Pept-1 is hormonally regulated. In this experiment, we investigated whether insulin has such a role. We used a human intestinal cell monolayer (Caco-2) as the in vitro model of human small intestine and glycylglutamine (Gly-Gln) as the model substrate for Pept-1. Results showed that addition of insulin at a physiological concentration (5 nM) to incubation medium greatly stimulates Gly-Gln uptake by Caco-2 cells. This stimulation was blocked when genistein, an inhibitor of tyrosine kinase, was added to incubation medium. Studies of the mechanism of insulin stimulation showed the following. 1) Stimulation occurred promptly (30-60 min) after exposure to insulin. 2) There was no significant change in the Michaelis-Menten constant of Gly-Gln transport, but there was a nearly twofold increase in its maximal velocity. 3) Insulin effect persisted even when Golgi apparatus, which is involved in trafficking of newly synthesized Pept-1, was dismantled. 4) However, there was complete elimination of insulin effect by disruption of microtubules involved in trafficking of preformed Pept-1. 5) Finally, with insulin treatment, there was no change in Pept-1 gene expression, but the amount of Pept-1 protein in the apical membrane was increased. In conclusion, the results show that insulin, when it binds to its receptor, stimulates Gly-Gln uptake by Caco-2 cells by increasing the membrane population of Pept-1. The mechanism appears to be increased translocation of this transporter from a preformed cytoplasmic pool.  (+info)

Figure 3. Immunofluorescent localization of procollagen I and Hsp47 in the presence or absence of brefeldin A treatment in CEC. Cells were treated with 2 µg/ml brefeldin A for 30 min, fixed, permeabilized, and stained as described in the text. A. Procollagen I (green) and Hsp47 (red) in brefeldin A-treated cells. B. Prolyl 4-hydroxylase (green) and procollagen I (red) in brefeldin A-treated cells. C. Prolyl 4-hydroxylase (green) and Hsp47 (red) in brefeldin A-treated cells. D. Phase-contrast microscopy of C. Bar, 10 µm.. ...
(His)6-GBF1 is a BFA-resistant ARF-GEF. (A) Fractions enriched in (His)6-GBF1 display a GEF specific for ARFs. Identical volumes (5 μl) of the 50 mM imidazole
brefeldin A esterase: hydrolyzes brefeldin A to brefeldin A acid & also hydrolyzes ethyl valerate; 372 amino acids; amino acid sequence given in first source
In mammalian and yeast cells, the main target of brefeldin A appears to be a guanine nucleotide exchange factor (GEF) called GBF1.[8] GBF1 is a member of the Arf family of GEFs which are recruited to membranes of the Golgi.[9] It is responsible for the regulation of Arf1p GTPase.[9] It does this through converting the inactive GDP-bound form of Arf1p to the active GTP-bound form.[9] The nucleotide exchange occurs at the catalytic Sec7 domain of GBF1. Activated Arf1p then recruits coat protein β-COP, a subunit of the COP-I complex, to cargo-bound receptors on the membrane.[9] Coat protein recruitment is necessary for proper vesicle formation and transport. Brefeldin A reversibly inhibits the function of GBF1 uncompetitively by binding to the complex it forms with GDP-bound Arf1p and preventing conversion to the GTP-bound form.[9] The lack of active Arf1p prevents coat protein recruitment, which then ultimately induces the fusion of neighboring ER and Golgi membranes due to lack of vesicle ...
We examined the actions on ENaC recycling of reagents that alter membrane trafficking and cytoskeletal organization using the restimulation protocol. Treatment with BFA did not affect the first response to forskolin, but it produced a marked inhibition of the subsequent ΔISC. The finding that it was possible to elicit one cycle of forskolin stimulation-recovery suggests that ENaC-containing vesicles available for channel insertion are distal to the Golgi and TGN. The response to restimulation was significantly reduced, however, indicating that ENaC is recycled through BFA-sensitive compartments. Results from a study using BFA-treated toad bladder produced similar findings in response to repeated ADH stimulation; an initial stimulation could be elicited, but subsequent stimulations were abolished by pretreatment with 5 μg/ml BFA (Weng and Wade, 1994). The effect of BFA on ENaC recycling was unexpected in view of its well-documented inhibition of AP-1-dependent trafficking in early compartments ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) has been identified recently as a novel regulator of estrogen signalling in breast cancer cells. Despite being a potential target for new breast cancer treatment, its amino acid sequence suggests no association with any well-characterized protein family and provides little clues as to its molecular function. In this paper, we predicted the structure, function and interactions of BIG3 using a range of bioinformatic tools. Homology search results showed that BIG3 had distinct features from its paralogues, BIG1 and BIG2, with a unique region between the two shared domains, Sec7 and DUF1981. Although BIG3 contains Sec7 domain, the lack of the conserved motif and the critical glutamate residue suggested no potential guaninyl-exchange factor (GEF) activity. Fold recognition tools predicted BIG3 to adopt an α-helical repeat structure similar to that of the armadillo (ARM) family. Using state-of-the-art methods, we predicted interaction sites
We recently reported that brefeldin A-inhibited guanine nucleotide-exchange proteins 3 (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby leading to a reduction of function of the PHB2 growth suppressor in the nuclei of breasts tumor cells. PHB2 nuclear transfer may offer restorative strategies for managing Elizabeth2/Emergency room signs in breasts tumor cells. Introduction Prohibitin 1 and 2 (PHB and buy 808118-40-3 PHB2) proteins are highly conserved in eukaryotic cells and exhibit diverse subcellular localization with different functions [1C3]. These molecules are primarily observed in inner mitochondrial membranes via their buy 808118-40-3 N-terminal transmembrane domain but are also present in several other localizations such as the cytosol, endoplasmic reticulum, nucleus, and plasma membrane [1]. Both proteins form hetero-oligomeric ring structures in the inner mitochondrial membrane and function as chaperones buy 808118-40-3 that maintain mitochondrial integrity and stabilize ...
Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), (10ug), 10 µg.
gi,17538522,ref,NP_501092.1, component of oligomeric Golgi complex 2; brefeldin A-sensitive, LDLC related peripheral Golgi protein, required for normal Golgi function; contains an N myristoylation domain (78.6 kD) (4H802) [Caenorhabditis elegans] gi,2498513,sp,Q21444,COG2_CAEEL Conserved oligomeric Golgi complex component 2 (LDLC protein homolog) gi,1078836,pir,,B53542 brefeldin A-sensitive Golgi protein LDLC - Caenorhabditis elegans gi,807871,emb,CAA84428.1, Cog2 protein [Caenorhabditis elegans] ...
The Golgi apparatus has long been suggested to be important for directing secretion to specific sites on the plasma membrane in response to extracellular signaling events. However, the mechanisms by which signaling events are coordinated with Golgi apparatus function remain poorly understood. Here, we identify a scaffolding function for the Golgi matrix protein GM130 that sheds light on how such signaling events may be regulated. We show that the mammalian Ste20 kinases YSK1 and MST4 target to the Golgi apparatus via the Golgi matrix protein GM130. In addition, GM130 binding activates these kinases by promoting autophosphorylation of a conserved threonine within the T-loop. Interference with YSK1 function perturbs perinuclear Golgi organization, cell migration, and invasion into type I collagen. A biochemical screen identifies 14-3-3zeta as a specific substrate for YSK1 that localizes to the Golgi apparatus, and potentially links YSK1 signaling at the Golgi apparatus with protein transport events, cell
There are six subfamilies of Arf GEFs in eukaryotes (see poster). The GBF/Gea and BIG/Sec7 GEFs function sequentially in the secretory pathway, with GBF/Gea proteins acting at the early Golgi, and BIG/Sec7 proteins at the trans-Golgi and TGN (Donaldson and Jackson, 2011). The cytohesin/Arno, EFA6 and IQSEC/BRAG subfamilies function primarily in endosome-plasma-membrane trafficking pathways at the cell periphery, the latter two using Arf6 as a substrate (Casanova, 2007; Gillingham and Munro, 2007). The FBXO8 GEFs, restricted primarily to vertebrates, contain an F-box in addition to the Sec7 domain (Gillingham and Munro, 2007). Arf activation by GBF/Gea and BIG/Sec7 GEFs is inhibited by the drug brefeldin A, which traps a Sec7-domain-Arf-GDP complex (Mossessova et al., 2003; Peyroche et al., 1999; Renault et al., 2003).. Many GEFs exist in an autoinhibited state in the cytosol, with their activation coupled to membrane recruitment. At the plasma membrane, the Pleckstrin homology (PH) domains of ...
We next analysed the effect of BFA on AtPIN-labelled compartments in maize root cells. As seen on longitudinal sections (Fig. 2F), polar plasma membrane staining with AtPIN was weaker after a 90-minute treatment with BFA (Fig. 2, compare F with E) and almost disappeared after a 150-minute treatment (Fig. 2G) (see also Baluska et al., 2002 and Fig. 3H within). This BFA effect on polar staining was concomitant with the formation of two to four fluorescent areas within the cell (Fig. 2F,G), reminiscent of `BFA compartments (Satiat-Jeunemaitre and Hawes, 1992; Satiat-Jeunemaitre and Hawes 1993) (see also Baluska et al., 2002 and Fig. 3H within). These BFA-induced modifications of plasma membrane staining were also clearly seen on isolated root cells (Fig. 3H,K). At the subcellular level, a third additional BFA effect was observed because there was a clear decrease, or even loss, in the number of the μm-sized intracellular immunolabelled objects (Fig. 3H).. BFA is known to block exocytosis but not ...
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is involved in the maintenance of Golgi structure and function through its interaction with the integral membrane protein giantin. It may also be involved in the hormonal regulation of steroid formation. [provided by RefSeq, Jul 2008 ...
Zinc Finger Protein Containing Five Transmembrane Domains; Null Mutant Exhibits Strongly Fragmented Vacuoles And Sensitivity To Brefeldin A, A Drug Which Is Known To Affect Intracellular Transport
A golgi apparatus, or golgi complex, is the main organelle responsible for mediating the transportation of protein and fat within the cell, according to Scitable, a learning website curated by...
The Golgi apparatus is an organelle found in the cytoplasm of most eukaryotic cells that is involved in the packaging and secretion of substances nece...
The Golgi Cenci Foundation started its activity in November 2009; They have been operating in the city for ten years, first inside the historic building of the Golgi and then, since January 2013, in the new main office in Corso San Martino 10.Since then, three ...
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Dr. Stéphanie Devineau, Unité BFA, équipe Réponses Moléculaires et Cellulaires aux Xénobiotiques (resp. J.M. Dupret) Titre : Crowning ...
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TY - JOUR. T1 - Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells. AU - Wang, E.. AU - Pennington, J. G.. AU - Goldenring, J. R.. AU - Hunziker, W.. AU - Dunn, Kenneth. PY - 2001. Y1 - 2001. N2 - Recent studies showing thorough intermixing of apical and basolateral endosomes have demonstrated that endocytic sorting is critical to maintaining the plasma membrane polarity of epithelial cells. Our studies of living, polarized cells show that disrupting endocytosis with brefeldin-A rapidly destroys the polarity of transferrin receptors in MDCK cells while having no effect on tight junctions. Brefeldin-A treatment induces tubulation of endosomes, but the sequential compartments and transport steps of the transcytotic pathway remain intact. Transferrin is sorted from LDL, but is then missorted from common endosomes to the apical recycling endosome, as identified by its nearly neutral pH, and association with GFP chimeras of Rabs 11a and ...
FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy. MISCELLANEOUS: In the process of transport, SEC12 itself may migrate to the Golgi apparatus and function in subsequent transport events. MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD medium ...
Background: In hepatocytes and alcohol-metabolizing cultured cells, Golgi undergoes ethanol (EtOH)-induced disorganization. Periniclear and organized Golgi is important in liver homeostasis, but how the Golgi remains intact is unknown. Work from our laboratories showed that EtOH-altered cellular function could be reversed after alcohol removal; we wanted to determine whether this recovery would apply to Golgi. Methods: We used alcohol-metabolizing HepG2 (VA-13) cells (cultured with or without EtOH for 72 h) and rat hepatocytes (control and EtOH-fed (Lieber-DeCarli diet). For recovery, EtOH was removed and replenished with control medium (48 hours for VA-13 cells) or control diet (10 days for rats). Results: EtOH-induced Golgi disassembly was associated with de-dimerization of the largest Golgi matrix protein giantin, along with impaired transport of selected hepatic proteins. After recovery from EtOH, Golgi regained their compact structure, and alterations in giantin and protein transport were restored.
The reports of dual-targeted proteins in plants have steadily increased over the past years. The vast majority of these proteins are soluble proteins distributed between compartments of the non-secretory pathway, predominantly chloroplasts and mitochondria. In contrast, dual-targeted transmembrane proteins, especially of the secretory pathway, are rare and the mechanisms leading to their differential targeting remain largely unknown. Here, we report dual-targeting of the Arabidopsis DUF679 Membrane Protein 1 (DMP1) to the tonoplast (TP) and the plasma membrane (PM). In Arabidopsis and tobacco two equally abundant DMP1 isoforms are synthesized by alternative translation initiation: a full length protein, DMP1.1, and a truncated one, DMP1.2, which lacks the N-terminal 19 amino acids including a TP-targeting dileucine motif. Accumulation of DMP1.1 and DMP1.2 in the TP and the PM, respectively, is Brefeldin A-sensitive, indicating transit via the Golgi. However, DMP1.2 interacts with DMP1.1, leading to
Recent studies showed that the phospholipase subunits of Platelet Activating Factor Acetylhydrolase (PAFAH) Ib, α1 and α2 partially localize to the Golgi complex and regulate its structure and function. Using siRNA knockdown of individual subunits, we find that α1 and α2 perform overlapping and unique roles in regulating Golgi morphology, assembly, and secretory cargo trafficking. Knockdown of either α1 or α2 reduced secretion of soluble proteins, but neither single knockdown reduced secretion to the same degree as knockdown of both. Knockdown of α1 or α2 inhibited reassembly of an intact Golgi complex to the same extent as knockdown of both. Transport of VSV-G was slowed but at different steps in the secretory pathway: reduction of α1 slowed trans Golgi network to plasma membrane transport, whereas α2 loss reduced endoplasmic reticulum to Golgi trafficking. Similarly, knockdown of either subunit alone disrupted the Golgi complex but with markedly different morphologies. Finally, ...
Plant cells possess much of the molecular machinery necessary for receptor-mediated endocytosis (RME), but this process still awaits detailed characterization. In order to identify a reliable and well-characterized marker to investigate RME in plant cells, we have expressed the human transferrin rec …
The Golgi complex, also known as the Golgi apparatus or simply the Golgi, is a cytoplasmic organelle. It is found in eukaryote cells, as in animals, plants, and fungi. The complex was discovered by Camillo Golgi in 1898. Golgi, who worked at Pavia, Italy, was ignored. His discovery was said to be dirt on his lenses. Years later, electron microscope pictures showed structures just like in the original Golgi drawings. It is made of several flattened sac-like membranes which look like a stack of pancakes. The main function of the Golgi apparatus is to process and package macromolecules, such as proteins and lipids. They come to the Golgi after being built, and before they go to their destination. In general, what the Golgi does is Much of the enzymatic processing is post-translational modification of proteins. The Golgi complex inspects them for flaws and discards extra material added during their manufacture, wraps them up and then targets them for packaging. The Golgi complex is especially active ...
Endogenous hHK3 localizes to the Golgi complex. The localization of endogenous Hook proteins in Hep2 cells (A, D, G, J, and M) was compared with the Golgi marke
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ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport and phospholipase D activation. Both guanine nucleotide-exchange proteins and GTPase-activating proteins (GAPs) for ARFs have been cloned recently. A zinc finger motif near the amino terminus of the ARF1 GAP was required for stimulation of GTP hydrolysis. ARD1 is an ARF family member that differs from other ARFs by the presence of a 46-kDa amino-terminal extension. We had reported that the ARF domain of ARD1 binds specifically GDP and GTP and that the amino-terminal extension acts as a GAP for the ARF domain of ARD1 but not for ARF proteins. The GAP domain of ARD1, synthesized in Escherichia coli, stimulated hydrolysis of GTP bound to the ARF domain of ARD1. Using ARD1 truncations, it appears that amino acids 101-190 are critical for GAP activity, whereas residues 190-333 are involved in physical interaction between the two domains of ...
ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport and phospholipase D activation. Both guanine nucleotide-exchange proteins and GTPase-activating proteins (GAPs) for ARFs have been cloned recently. A zinc finger motif near the amino terminus of the ARF1 GAP was required for stimulation of GTP hydrolysis. ARD1 is an ARF family member that differs from other ARFs by the presence of a 46-kDa amino-terminal extension. We had reported that the ARF domain of ARD1 binds specifically GDP and GTP and that the amino-terminal extension acts as a GAP for the ARF domain of ARD1 but not for ARF proteins. The GAP domain of ARD1, synthesized in Escherichia coli, stimulated hydrolysis of GTP bound to the ARF domain of ARD1. Using ARD1 truncations, it appears that amino acids 101-190 are critical for GAP activity, whereas residues 190-333 are involved in physical interaction between the two domains of ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Eukaryotic cells perform continuous recycling of the plasma membrane proteins and extracellular matrix molecules from the cell surface back to the cytoplasm (for plant cells, see Low and Chandra, 1994; Robinson et al., 1998). Our recent study (Baluška et al., 2002) provides experimental evidence that cell wall pectins are internalized after in muro de-esterification (Micheli, 2001) and cross-linking with calcium and boron (Matoh and Kobayashi, 1998;Kobayashi et al., 1999). These almost exclusive cell wall pectin epitopes, reactive to JIM5 and RGII antibodies, accumulate abundantly within intracellular BFA-induced compartments, which are obviously formed through aggregation of trans-Golgi networks and putative plant endosomes (Baluška et al., 2002). Here, we report that intracellular BFA compartments accumulate these cell wall pectins in meristematic cells of maize and wheat, but not of zucchini and alfalfa, root apices. Intriguingly, boron deprivation inhibits endocytosis of cell wall pectins. ...
XPLDHTNVTA PQASMMFQYF VKVVPTVYMK VDGEAPLPPQ VLRTNQFSVT RHEKVANGLL GDQGLPGVFV LYELSPMMVK LTEKHRSFTH FLTGVCAIIG GMFTVAGLID SLIYHSARAI QKKIDLGKTT ...
Supplementary MaterialsAdditional file 1: Table S1. group). Group (A & T), dual therapy with Adr (0.25?g/ml) and Tu (0.8?g/ml); Group (A), monotherapy with Adr (0.25?g/ml), and the control group. The colored dots represent over-expressed or under-expressed genes; the black dots represent unchanged genes. em P /em ? ?0.05. (PPTX 80 kb) 13046_2018_935_MOESM3_ESM.pptx (81K) GUID:?DD86D9AB-143A-41D8-8E65-23ABA4296B81 Additional file 4: Figure S3. Expression levels of CHOP, Cl-PARP and Cl-caspase 3 in SGC7901 detected by IF after treatment with monotherapy or dual therapy for 48?h. The concentrations of drugs were the same as those in Additional file 3: Physique S2. (400 ; scale bar, 50?m.) (PPTX 556 kb) 13046_2018_935_MOESM4_ESM.pptx (556K) GUID:?A2B89A2C-2E37-48C3-8062-7981706090A1 Additional file 5: Figure S4. Brefeldin A (BFA) can mimic the effects of Tu on MDR GC cells. a The effects of Tu on glycoproteins-L1CAM and TIMP1. GC cells were treated with Tu (0.8?g/ml) for 48?h before harvest. All ...
The Golgi apparatus is a packaging center Golgi apparatus or Golgi body or Golgi complex is a membrane-bound organelle, associated with the processing of…
We have studied changes in the Golgi morphology in Madin-Darby canine kidney cells as a result of chemically induced DNA damage, and how such morphological change affects synthesis and sorting of sulphated PGs in the cell line ...
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TY - JOUR. T1 - ADP ribosylation factor 6 regulates neuronal migration in the developing cerebral cortex through FIP3/arfophilin-1-dependent endosomal trafficking of N-cadherin. AU - Hara, Yoshinobu. AU - Fukaya, Masahiro. AU - Hayashi, Kanehiro. AU - Kawauchi, Takeshi. AU - Nakajima, Kazunori. AU - Sakagami, Hiroyuki. PY - 2016. Y1 - 2016. N2 - During neural development, endosomal trafficking controls cell shape and motility through the polarized transport of membrane proteins related to cellcell and cellextracellular matrix interactions. ADP ribosylation factor 6 (Arf6) is a critical small GTPase that regulates membrane trafficking between the plasma membrane and endosomes. We herein demonstrated that the knockdown of endogenous Arf6 in mouse cerebral cortices led to impaired neuronal migration in the intermediate zone and cytoplasmic retention of N-cadherin and syntaxin12 in migrating neurons. Rescue experiments with separation-of-function Arf6 mutants identified Rab11 familyinteracting ...
Transition zones are associated with the Golgi stacks. They are close to each other. This makes sense because the communication is more efficient. Vesicles dont need to travel long distances and the existence of the Golgi apparatus itself depends on a continuous process of vesicle incoming. It has been observed that a new transition zone led quickly to the nearby formation of a new Golgi stack. On the contrary, if a transition zone disappears, the associated Golgi cisternae are also lost. Transition zones can fuse with others and one transition zone can be split in two. Their associated Golgi stacks match this behavior. Vesicles budding from the transition zones are COPII coated vesicles ( COPII: coat protein II; Figure 1). Several proteins are involved in the formation of this COPII molecular framework: Sec16, Sar1 GTPases, Sec23/24 and Sec13/31. In this order, they are assembled at the cytosolic surface of the transition zone membranes. Transition zones are the more suitable environments for ...
The glycoside digitonin was used to selectively permeabilize the plasma membrane exposing functionally and morphologically intact ER and Golgi compartments. Permeabilized cells efficiently transported vesicular stomatitis virus glycoprotein (VSV-G) through sealed, membrane-bound compartments in an ATP and cytosol dependent fashion. Transport was vectorial. VSV-G protein was first transported to punctate structures which colocalized with p58 (a putative marker for peripheral punctate pre-Golgi intermediates and the cis-Golgi network) before delivery to the medial Golgi compartments containing alpha-1,2-mannosidase II and processing of VSV-G to endoglycosidase H resistant forms. Exit from the ER was inhibited by an antibody recognizing the carboxyl-terminus of VSV-G. In contrast, VSV-G protein colocalized with p58 in the absence of Ca2+ or the presence of an antibody which inhibits the transport component NSF (SEC18). These studies demonstrate that digitonin permeabilized cells can be used to ...
The stiochiometric phosphorylation of golgin-84 in mitosis together with its binding to active rab1 suggested that it may play a role in Golgi structure and/or membrane trafficking through the Golgi apparatus. To address a possible structural role for golgin-84, GFP-tagged full-length and truncated versions of the protein were expressed in HeLa cells, and effects upon Golgi structure were analyzed by immunofluorescence microscopy (Fig. 5 a). At moderate expression levels, none of the golgin-84 constructs elicited any significant change in Golgi structure (unpublished data). Furthermore, constructs that failed to target to the Golgi apparatus had no effects upon Golgi structure even at very high levels of expression (Fig. 5 a; unpublished data). In contrast, expression at high levels of both full-length and golgin-84 lacking the head region had dramatic effects upon Golgi structure, converting the ribbon into punctate structures dispersed throughout the cytoplasm (Fig. 5 b). EM analysis of the ...
Anti-Golgi complex antibodies (AGAs) are primarily associated with systemic lupus erythematosus and Sjögrens syndrome. Here we report on the immunoreactivity of AGAs against five Golgi autoantigens (giantin, golgin-245, golgin-160, golgin-95/GM130, and golgin-97) and provide data from epitope mapping on the most common Golgi autoantigen, namely giantin. A total of 80 human sera containing AGAs, as defined by indirect immunofluorescence on HEp-2 cells, were analyzed by ELISA using recombinant autoantigens and immunoprecipitation. The proportion of AGA sera that reacted with the five Golgi autoantigens was correlated with the molecular mass of the Golgi antigens. Autoantibodies to giantin, the largest Golgi autoantigen, were the predominant AGAs, being found in 50% of the AGA sera. Epitope mapping of giantin was performed using six recombinant fragments spanning the entire protein. Antigiantin-positive sera with low titer autoantibodies recognized epitopes in the carboxyl-terminal fragments that are
Constitutive Secretion: Advanced Look --, 2.) Exocytosis After leaving the Golgi apparatus, proteins following the constitutive secretion pathway merge with the cell membrane and release their cargo by a process called exocytosis. Clicking on each of the thumbnail images will bring up a larger, labeled version of the described scene.. To see the Flash movie for the following sequence of images, click here.. ...
Arl1 (ARF like protein1) is a poorly understood member of ARF family small GTPases. This thesis presents an original characterization of Arl1 and its effectors. Arl1 was localized to the tans Golgi under EM. Over expression of guanine nucleotide mutants of Arl1 dramatically affects the structure and function of Golgi apparatus. Arl1-GTP was found to interact with GRIP domain of Golgins (Golgin-97, Golgin-245, GCC1 and KIAA0336). The interaction was dependent on the conserved amino acids on both switch II region of Arl1 and the GRIP domain. Collectively, the research presented in this thesis reveals Arl1 is a new regulator of Golgi structure and function and one mechanism of Arl1a??s function is that it recruits and regulates its effectors a?? GRIP domain Golgins to Golgi ...
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COPⅠ囊泡:最初研究者利用三磷酸鳥苷(GTP)衍生物GTPγS(一種富含高爾基體膜的細胞質與抗水解的GTP衍生物)共培養時,發現高爾基體池之間存在一種囊泡轉運結構[9](後來在真核細胞中也證實此結構的存在[10])。除了脂質成分外,參與此囊泡形成的成份還有7種外被體蛋白(即外被體α、β、β′、γ、δ、ε、ζ)。這些外被體蛋白相互作用形成的復合物就是COPⅠ囊泡[11][12]。亞單位α、β′、ε在結構上與網格蛋白及COPⅡ囊泡的外層組分具有較高的一致性,形成復合物的內層組分稱為B亞復合物(主要負責與靶蛋白結合),而亞單位β、γ、δ、ζ 與網格蛋白及COPⅡ囊泡的內層組分相似,形成復合物的內層組分稱為F亞復合物,該亞復合物主要負責與靶蛋白結合,並且直接與COPⅠ囊泡形成的招募者ADP核糖基化因子(英语:ADP ribosylation factor)(ADP ribosylation ...
Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis (By similarity).
Figure 2. Flow cytometric characterization of γδ T cells in our patient demonstrates specific expansion of a homogeneous Vδ2+ T cell population. Flow cytometry performed on frozen PBMC either unstimulated for surface markers or PMA/ionomycin/brefeldin A stimulated for intracellular molecules. (A) FACS used to identify live, singlet lymphocytes (not shown), which were gated on to identify CD3+ T cells in the patient and a representative IFX-treated control (HC). CD3+ cells further gated on to identify Vδ1+/Vδ2+ T cells. The indicated plots display markers specific to the Vδ2+ T cell population with gates based on FMO control (not shown). (B) Mass cytometry used to identify live, singlet, CD3+CD14-CD19-TCRγδ+ cells in the patients PBMC for expression of the indicated markers. (C) viSNE analysis performed using 36 markers to cluster PBMC populations in the patient and 5 age-matched male patients with AS. CD3ε, CD4, CD8α, CD14, CD19, CD56, and TCRγδ antigens were used to gate indicated ...
I make collages by combining paper ephemera, found images, and my own photographic imagery and drawing. Inspired by the Mail Art Movement, I often employ an element of correspondence in my studio practice. Although Im inspired by whatever materials I come across, there is always a feeling of searching or mapping in the work I produce. I was born in rural Breckenridge, MN. I studied photography at Cornish College of the Arts in Seattle, and finished my BFA at Rocky Mountain College of Art + Design (RMCAD), graduating in 2013 from their photography and video art program. ...
talk contribs‎ 307 bytes +307‎ Created page with {{organelle}} ==Definition== The Golgi apparatus (also called the Golgi body or Golgi apparatus) is an organelle found in most eukaryotic cells whose ... ...
We do a complete analysis and explanation behind Hakkers stacks and routines. He had the MENS stack, HUSS routine, Hybrid Stack, and the H4GS routine stack.
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the GBF1 ... Niu TK, Pfeifer AC, Lippincott-Schwartz J, Jackson CL (2005). "Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor ... "Entrez Gene: GBF1 golgi-specific brefeldin A resistance factor 1". Nakajima D, Okazaki N, Yamakawa H, et al. (2003). " ...
... is an anamorph fungus species of the genus of Penicillium which produces Brefeldin A a fungal ... brefeldin a). Formation in Penicillium brefeldianum". Tetrahedron. 39 (21): 3507-13. doi:10.1016/S0040-4020(01)88660-9. v t e. ... brefeldin a). Formation in Penicillium brefeldianum". Tetrahedron. 39 (21): 3507-13. doi:10.1016/S0040-4020(01)88660-9. An, C. ...
Using the drug Brefeldin A to perturb membrane trafficking, she showed that membranes cycle between the endoplasmic reticulum ... Lippincott-Schwartz, J.; Yuan, L.; Tipper, C.; Amherdt, M.; Orci, L.; Klausner, R. D. (1991-11-01). "Brefeldin A's effects on ... Lippincott-Schwartz, J.; Donaldson, J. G.; Klausner, R. D. (1992-03-01). "Brefeldin A: insights into the control of membrane ... "Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi ...
Nassoury, N., Wang, Y., & Morse, D. (2005). Brefeldin a inhibits circadian remodeling of chloroplast structure in the ...
Saito T, Tanaka M, Yamaguchi I (November 1996). "Effect of brefeldin A on influenza A virus-induced apoptosis in vitro". J. Vet ...
The major mechanism of action of Brefeldin A is through inhibition of ARF1. ARF1 has been shown to interact with: CHRM3, COPB1 ...
Treatment with Brefeldin A (BFA) inhibits the cytotoxicity of Modeccin, by disrupting the Golgi apparatus. Brefeldin A blocks ... "Golgi tubule traffic and the effects of brefeldin A visualized in living cells". The Journal of Cell Biology. 139 (5): 1137-55 ...
ARFGEF2: ADP-ribosylation factor guanine nucleotide-exchange factor 2 (brefeldin A-inhibited) ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 1 is a protein that in humans is encoded by the ARFGEF1 gene. ADP- ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ... Togawa A, Morinaga N, Ogasawara M, Moss J, Vaughan M (Apr 1999). "Purification and cloning of a brefeldin A-inhibited guanine ... Shen X, Hong MS, Moss J, Vaughan M (Jan 2007). "BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 2 is a protein that in humans is encoded by the ARFGEF2 gene. ADP- ... Xu KF, Shen X, Li H, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2005). "Interaction of BIG2, a brefeldin A-inhibited guanine ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ...
Podos SD, Reddy P, Ashkenas J, Krieger M (Dec 1994). "LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required ...
Xu KF, Shen X, Li H, Pacheco-Rodriguez G, Moss J, Vaughan M (2005). "Interaction of BIG2, a brefeldin A-inhibited guanine ...
Zeghouf M, Guibert B, Zeeh JC, Cherfils J (December 2005). "Arf, Sec7 and Brefeldin A: a model towards the therapeutic ...
... domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)". Proc. Natl. Acad. Sci. U.S.A. 100 (4): 1627-32 ...
Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ...
... phosphorylation and sulphation by brefeldin A". The Biochemical Journal. 295 (Pt 3): 813-9. doi:10.1042/bj2950813. PMC 1134634 ...
... produces fatty acid, Brefeldin A and the antibiotic Cyanein List of Penicillium species Koman, V.; Betina, ...
Penicillin, cephalosporins, fusafungine, usnic acid, fusidic acid, fumagillin, brefeldin A, verrucarin A, alamethicin, are ...
Skop AR, Bergmann D, Mohler WA, White JG (May 2001). "Completion of cytokinesis in C. elegans requires a brefeldin A-sensitive ...
Brefeldin A is a very common inducer of the unfolded protein response or endoplasmic reticulum stress response (ER stress). ...
"Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of ... "Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of ...
Hsu VW, Shah N, Klausner RD (Jun 1992). "A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like ...
... a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding ...
It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. It may ...
Brefeldin A (BFA) is a fungal metabolite used experimentally to disrupt the secretion pathway as a method of testing Golgi ...
... produces xanthomegin, brefeldin A and janthitrem B MycoBank Straininfo of Penicillium zonatum UniProt ATCC ...
AP-1 complex-associated regulatory protein (Gamma1-adaptin brefeldin A resistance protein) is a protein that in humans is ...
PIN3 is normally localized to the surface of hypocotyl and stem, but is also internalized in the presence of Brefeldin A (BFA ...
... membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46". The ...
2004). "Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 ...
"SAFETY DATA SHEET Brefeldin A" (PDF). Cayman Chemical. 6 February 2015.. *^ a b c d e "Material Safety Data Sheet. Brefeldin A ... Brefeldin A is a lactone antiviral produced by the fungus Penicillium brefeldianum.[1] Brefeldin A inhibits protein transport ... Brefeldin A was initially isolated with hopes to become an antiviral drug[3] but is now primarily used in research to study ... "Brefeldin A Supplier , CAS 20350-15-6 , Tocris Bioscience". Tocris Bioscience. 6 September 2016. Retrieved 2017-05-08.. ...
... brefeldin-A (brefeldin-A) in liquid culture by Eupenicillium brefeldianum, (B. Dodge) Stolk and Scott, ATCC... ... 7-epi-brefeldin A, a co-metabolite of brefeldin A inCurvularia lunata. J Chem Soc Perkin Trans I: 2387-2390.Google Scholar ... Fermentation conditions are described for the production of the antitumor antibiotic 7-(S)-brefeldin-A (brefeldin-A) in liquid ... brefeldin-A Eupenicillium brefeldianum antitumor antibiotic This is a preview of subscription content, log in to check access. ...
1000x Brefeldin A Solution, 1000x Life Sciences:Protein Biology:Antibody and Dye Based Assays ... Invitrogen eBioscience Brefeldin A Solution, 1000x Addition of Brefeldin A during the last hours of in vitro activation of ... Brefeldin A is an inhibitor of intracellular protein transport. *Incubation of cells in culture with Brefeldin A leads to ... Brefeldin A is effective for enhanced detection of a majority of mouse and human intracellular cytokines; however, it is ...
Wood SA, Park JE, and Brown WJ (1991) Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early ... Lippincott-Schwartz J, Yuan L, Tipper C, Amherdt M, Orci L, and Klausner RD (1991) Brefeldin As effects on endosomes, ... Hess MW, Müller M, Debbage PL, Vetterlein M, and Pavelka M (2000) Cryopreparation provides new insight into Brefeldin A-effects ... Klausner RD, Donaldson JG, and Lippincott-Schwartz J (1992) Brefeldin A: insights into the control of membrane traffic and ...
... without Brefeldin A) is a pre-mixed cocktail with optimized concentration of PMA (phorbol 12-myristate-13-acetate) and ... Generally, Brefeldin A is more toxic for longer term incubations, so for shorter stimulations (6 hrs or less) use Brefeldin A. ... The Brefeldin A solution freezes at 4°C . Is the solution still OK? We recommend to thaw in warm water after removing from the ... The Brefeldin A is dissolved in DMSO, which freezes at 18°C, so this is normal. No one has reported any problems with the ...
... hydrolyzes brefeldin A to brefeldin A acid & also hydrolyzes ethyl valerate; 372 amino acids; amino acid sequence given in ... brefeldin A esterase. Subscribe to New Research on brefeldin A esterase hydrolyzes brefeldin A to brefeldin A acid & also ...
Brefeldin A supplier , purchase Brefeldin A , Brefeldin A cost , Brefeldin A manufacturer , order Brefeldin A , Brefeldin A ... with half-maximal inhibition at 2 μM Brefeldin A. Brefeldin A prevents a wide variety of membrane traffic pathways. Brefeldin A ... 3] Brefeldin A induces fusion of the Golgi apparatus with the ER. Brefeldin A abolishes the inhibitory effect of the CERT ... The administration of 25 ng/mL of Brefeldin A completely blocks growth of HF4.9 and HF28RA cells, whereas higher Brefeldin A ...
Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes.. Wood SA1, Park JE, Brown WJ. ... Brefeldin A (BFA) is a fungal metabolite that causes a redistribution of the stacked cisternae of the Golgi complex into the ...
ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited)Imported. ,p>Information which has been ... brefeldin A-inhibited guanine nucleotide-exchange protein 1 isoform X1. Austrofundulus limnaeus ... tr,I3K9S1,I3K9S1_ORENI ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited) OS=Oreochromis ...
Brefeldin A is thus a specific inhibitor of antigen processing for class I-restricted T cell recognition. Its effect on antigen ... Brefeldin A, a specific inhibitor of exocytosis, completely and reversibly inhibited the presentation of viral proteins, but ... The effect of brefeldin A on antigen presentation correlated with its inhibition of intracellular transport of newly ... Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes ...
Indeed, like beta-COP, ARF is dissociated from the Golgi complex by treatment with brefeldin A and brefeldin A prevents ARF ... Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF.. Helms JB1, ... Brefeldin A added to cells causes the rapid and reversible dissociation of a Golgi-associated peripheral membrane protein (M(r ... 12; and D. J. Palmer et al., manuscript submitted), so the primary effect of brefeldin A seems to be on the reaction ...
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 - Q92538 (GBF1_HUMAN) ...
Treatment with 20 microM brefeldin A (BFA) for 60 min caused the disassembly of the Golgi apparatus in tobacco BY-2 cells, and ... Effects of brefeldin A on the formation of the cell plate in tobacco BY-2 cells Eur J Cell Biol. 1995 Mar;66(3):274-81. ... Treatment with 20 microM brefeldin A (BFA) for 60 min caused the disassembly of the Golgi apparatus in tobacco BY-2 cells, and ...
... Plant J. 2006 Dec;48(5 ... In contrast, treatment with brefeldin A, which inhibits recycling from endosomes back to the plasma membrane in plant cells, ...
brefeldin A-inhibited guanine nucleotide-exchange protein;. CA,. calyculin A;. GEP,. guanine nucleotide-exchange protein;. GTP ... Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration ... Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein ... Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein ...
Brefeldin A] [20350-15-6] , Buy and find out price and availability, MSDS, properties of TCIs high quality specialty chemicals ... Brefeldin A: A Macrolide Lactone Antibiotic used as an Inhibitor of Protein Trafficking and Secretion. Brefeldin A (BFA) is a ... Brefeldin A: deciphering an enigmatic inhibitor of secretion (a review) *A. Nebenführ, C. Ritzenthaler, D. G. Robinson, Plant ... Brefeldin A: insights into the control of membrane traffic and organelle structure (a review) *R. D. Klausner, J. G. Donaldson ...
Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells. Robert B. Simon, ... Purpose: To study the mechanism by which an antibiotic brefeldin A (BFA) inhibits proliferation of androgen-responsive ... Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells ... Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells ...
Home » Brefeldin A, a Cytotoxin from an Endophytic Fungal Strain of Eupenicillium brefeldianum Isolated from Arisaema ... Brefeldin A, a Cytotoxin from an Endophytic Fungal Strain of Eupenicillium brefeldianum Isolated from Arisaema erubescens. ... The toxic metabolite was determined as brefeldin A (BFA) based on nuclear magnetic resonance techniques and fast atom ...
Brefeldin A (BFA) was the most successful at inducing lipid accumulation and was used to evaluate secondary screens including ... Phenotypic screening identifies Brefeldin A/Ascotoxin as an inducer of lipid storage in the algae Chlamydomonas reinhardtii ... Brefeldin A (BFA) was the most successful at inducing lipid accumulation and was used to evaluate secondary screens including ...
FM1-43 delivery to the vacuole was largely inhibited by brefeldin A, although overall uptake was stimulated, and brefeldin A ... Brefeldin A (BFA) was kept as a 50 mg/mL stock in methanol, and wortmannin was kept as a 10 mM stock in DMSO at −20°C. ... Driouich, A., Zhang, G.F., and Staehelin, L.A. (1993). Effect of brefeldin A on the structure of the Golgi apparatus and on the ... Uptake of a Fluorescent Marker in Plant Cells Is Sensitive to Brefeldin A and Wortmannin. Neil Emans, Sabine Zimmermann, Rainer ...
Apoptosis, caspase activity, NSC 95397, brefeldin A National Category Medical and Health Sciences Identifiers. URN: urn:nbn:se: ... Conclusion: NSC 95397, brefeldin A, bortezomib and sanguinarine induced caspase-3 activation with modest changes in nuclear ... The most active agents were brefeldin A, emetine, bortezomib and idarubicin, having IC50 values (the concentration of the drug ... The aim of this study was to investigate the apoptosis resulting from NSC 95397, brefeldin A, bortezomib and sanguinarine in ...
Literature References: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity. Produced by Penicillium brefeldianum Dodge: E. Haerri et al., Helv. Chim. Acta 46, 1235 (1963). Also produced by P. decumbens: V. L. Singleton et al., Nature 181, 1072 (1958); P. cyaneum: V. Betina et al., Folia Microbiol. 7, 353 (1962). Structure: H. P. Sigg, Helv. Chim. Acta 47, 1401 (1964). Abs configuration: H. P. Weber et al., ibid. 54, 2763 (1971). Synthesis of (±)-form: E. J. Corey, R. H. Wollenberg, Tetrahedron Lett. 1976, 4705; E. J. Corey et al., ibid. 1977, 2243; R. Baudouy et al., ibid. 2973; P. A. Bartlett, F. R. Green, J. Am. Chem. Soc. 100, 4548 (1978); A. E. Greene et al., ibid. 102, 7583 (1980); M. Honda et al., Tetrahedron Lett. 1981, 2679. Total synthesis of (+)-form: T. Kitahara et al., ibid. 1979, 3021. Biosynthesis: B. E. Cross, P. Hendley, Chem. Commun. 1975, 124; C. R. Hutchinson et al., J. Am. Chem. Soc. 103, 2474, 2477 (1981); M. Sunagawa et al., J. ...
Insights from Brefeldin A-Induced Compartments. František Baluška, Andrej Hlavacka, Jozef Šamaj, Klaus Palme, David G. Robinson ... Insights from Brefeldin A-Induced Compartments. František Baluška, Andrej Hlavacka, Jozef Šamaj, Klaus Palme, David G. Robinson ... Insights from Brefeldin A-Induced Compartments. František Baluška, Andrej Hlavacka, Jozef Šamaj, Klaus Palme, David G. Robinson ... 1995) Effects of brefeldin A on the formation of the cell plate in tobacco BY-2 cells. Eur J Cell Biol 66:274-281. ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) has been identified recently as a novel regulator of ... From: Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) is predicted to interact with its partner through an ...
Home » cDNA » Mouse cDNA » Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A- ... Properties for Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ... MC224976 Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ... "Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), ( ...
The two most widely used reagents are monensin and brefeldin A (BFA). These reagents differ somewhat in their mode of action, ... The Fungal Metabolite Brefeldin A Inhibits Dvl2-Plk1-Dependent Primary Cilium Disassembly. *Uijeong Lee, Sun-Ok Kim, +6 authors ... Brefeldin A, but not monensin, completely blocks CD69 expression on mouse lymphocytes: efficacy of inhibitors of protein ... article{Nylander1999BrefeldinAB, title={Brefeldin A, but not monensin, completely blocks CD69 expression on mouse lymphocytes: ...
Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi ... Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi ... cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment ... Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green ...
Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. R W Doms R W Doms ... Brefeldin A (BFA) has been reported to block protein transport from the ER and cause disassembly of the Golgi complex. We have ... R W Doms, G Russ, J W Yewdell; Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum.. J ... Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. ...
Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. ... S G Miller, L Carnell, H H Moore; Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to ... In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their ... Recent studies using the fungal metabolite brefeldin A (BFA) have provided important insights into the dynamics and the ...
  • In mammalian and yeast cells, the main target of brefeldin A appears to be a guanine nucleotide exchange factor (GEF) called GBF1. (wikipedia.org)
  • Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the GBF1 gene. (wikipedia.org)
  • Brefeldin A reversibly inhibits the function of GBF1 uncompetitively by binding to the complex it forms with GDP-bound Arf1p and preventing conversion to the GTP-bound form. (wikipedia.org)
  • Brefeldin A inhibits protein transport from the endoplasmic reticulum to the golgi complex indirectly by preventing association of COP-I coat to the Golgi membrane. (wikipedia.org)