ADP-Ribosylation Factors: 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 Factor 1: 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 A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Coated Vesicles: Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.Coatomer Protein: 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.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.GTP-Binding Proteins: 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.-.Coat Protein Complex I: 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.Golgi Apparatus: 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)GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Adenosine Diphosphate Ribose: An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.Phospholipase D: An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 5'-O-(3-Thiotriphosphate): Guanosine 5'-(trihydrogen diphosphate), monoanhydride with phosphorothioic acid. A stable GTP analog which enjoys a variety of physiological actions such as stimulation of guanine nucleotide-binding proteins, phosphoinositide hydrolysis, cyclic AMP accumulation, and activation of specific proto-oncogenes.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Nucleoside Diphosphate SugarsAdenosine Diphosphate Sugars: Esters formed between the aldehydic carbon of sugars and the terminal phosphate of adenosine diphosphate.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Deception: The act of deceiving or the fact of being deceived.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Ribose: A pentose active in biological systems usually in its D-form.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.ADP Ribose Transferases: Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Cholera Toxin: An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells, and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Amino Acid Sequence: 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.Actinidia: A plant species of the family ACTINIDIACEAE, order Theales.Virulence Factors, Bordetella: A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Poly(ADP-ribose) Polymerases: Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Botulinum Toxins: Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Adenylate Cyclase: An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC Cyclase Toxin: One of the virulence factors produced by virulent BORDETELLA organisms. It is a bifunctional protein with both ADENYLYL CYCLASES and hemolysin components.Poly Adenosine Diphosphate Ribose: A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.Phosphatidylinositol 4,5-Diphosphate: A phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)Bacterial Toxins: Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.Kinetics: The rate dynamics in chemical or physical systems.Adaptor Proteins, Vesicular Transport: A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.rhoA GTP-Binding Protein: A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC Proteins: Proteins prepared by recombinant DNA technology.Azaguanine: One of the early purine analogs showing antineoplastic activity. It functions as an antimetabolite and is easily incorporated into ribonucleic acids.Intracellular Membranes: 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.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Biological Transport: 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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.NAD+ NucleosidaseCloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Tankyrases: A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Mitochondrial ADP, ATP Translocases: A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
(1/429) Identification of a new Pyk2 target protein with Arf-GAP activity.

Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap.  (+info)

(2/429) GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro.

Recent cloning of a rat brain phosphatidylinositol 3,4, 5-trisphosphate binding protein, centaurin alpha, identified a novel gene family based on homology to an amino-terminal zinc-binding domain. In Saccharomyces cerevisiae, the protein with the highest homology to centaurin alpha is Gcs1p, the product of the GCS1 gene. GCS1 was originally identified as a gene conditionally required for the reentry of cells into the cell cycle after stationary phase growth. Gcs1p was previously characterized as a guanosine triphosphatase-activating protein for the small guanosine triphosphatase Arf1, and gcs1 mutants displayed vesicle-trafficking defects. Here, we have shown that similar to centaurin alpha, recombinant Gcs1p bound phosphoinositide-based affinity resins with high affinity and specificity. A novel GCS1 disruption strain (gcs1Delta) exhibited morphological defects, as well as mislocalization of cortical actin patches. gcs1Delta was hypersensitive to the actin monomer-sequestering drug, latrunculin-B. Synthetic lethality was observed between null alleles of GCS1 and SLA2, the gene encoding a protein involved in stabilization of the actin cytoskeleton. In addition, synthetic growth defects were observed between null alleles of GCS1 and SAC6, the gene encoding the yeast fimbrin homologue. Recombinant Gcs1p bound to actin filaments, stimulated actin polymerization, and inhibited actin depolymerization in vitro. These data provide in vivo and in vitro evidence that Gcs1p interacts directly with the actin cytoskeleton in S. cerevisiae.  (+info)

(3/429) EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization.

We have identified a human cDNA encoding a novel protein, exchange factor for ARF6 (EFA6), which contains Sec7 and pleckstrin homology domains. EFA6 promotes efficient guanine nucleotide exchange on ARF6 and is distinct from the ARNO family of ARF1 exchange factors. The protein localizes to a dense matrix on the cytoplasmic face of plasma membrane invaginations, induced on its expression. We show that EFA6 regulates endosomal membrane recycling and promotes the redistribution of transferrin receptors to the cell surface. Furthermore, expression of EFA6 induces actin-based membrane ruffles that are inhibited by co-expression of dominant-inhibitory mutant forms of ARF6 or Rac1. Our results demonstrate that by catalyzing nucleotide exchange on ARF6 at the plasma membrane and by regulating Rac1 activation, EFA6 coordinates endocytosis with cytoskeletal rearrangements.  (+info)

(4/429) Characterization of the regulation of phospholipase D activity in the detergent-insoluble fraction of HL60 cells by protein kinase C and small G-proteins.

Phospholipase D (PLD) activity has been shown to be GTP-dependent both in vivo and in vitro. One protein that confers GTP sensitivity to PLD activity in vitro is the low-molecular-mass G-protein ADP-ribosylation factor (Arf). However, members of the Rho family and protein kinase C (PKC) have also been reported to activate PLD in various cell systems. We have characterized the stimulation of PLD in HL60 cell membranes by these proteins. The results demonstrate that a considerable proportion of HL60 PLD activity is located in a detergent-insoluble fraction of the cell membrane that is unlikely to be a caveolae-like domain, but is probably cytoskeletal. This PLD activity required the presence of Arf1, a Rho-family member and PKC for efficient catalysis of the lipid substrate, suggesting that the activity represents PLD1. We show that recombinant human PLD1b is regulated in a similar manner to HL60-membrane PLD, and that PKCalpha and PKCdelta are equally effective PLD activators. Therefore maximum PLD activity requires Arf, a Rho-family member and PKC, emphasizing the high degree of regulation of this enzyme.  (+info)

(5/429) Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis.

The crystal structure of the complex of ARF1 GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 A resolution. The ARFGAP molecule binds to switch 2 and helix alpha3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.  (+info)

(6/429) Expression and distribution of adenosine diphosphate-ribosylation factors in the rat kidney.

BACKGROUND: Adenosine diphosphate (ADP)-ribosylation factors (ARFs) are small guanosine triphosphatases involved in membrane traffic regulation. Aiming to explore the possible involvement of ARF1 and ARF6 in the reabsorptive properties of the nephron, we evaluated their distribution along the different renal epithelial segments. METHODS: ARFs were detected by immunofluorescence and immunogold cytochemistry on renal sections, using specific anti-ARF antibodies. RESULTS: ARF1 was detected in proximal and distal tubules, thick ascending limbs of Henle's loops, and cortical and medullary collecting ducts. By immunofluorescence, labeling was mostly localized to the cell cytoplasm, particularly in Golgi areas. By electron microscopy, the Golgi apparatus and the endosomal compartment of proximal and distal tubular cells were labeled. ARF6 immunofluorescence was observed in brush border membranes and the cytoplasm of proximal convoluted tubular cells, whereas it was restricted to the apical border of proximal straight tubules. ARF6 immunogold labeling was detected over microvilli and endocytic compartments of proximal tubular cells. CONCLUSIONS: This study demonstrates the following: (a) the heterogeneous distributions of ARF1 and ARF6 along the nephron, (b) the existence of cytosolic and membrane-bound forms for both ARFs, and (c) their association with microvilli and endocytic compartments, suggesting an active participation in renal reabsorption.  (+info)

(7/429) Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors.

Activation of ADP-ribosylation factors (ARFs), approximately 20-kDa guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking, depends on guanine nucleotide-exchange proteins (GEPs), which accelerate replacement of bound GDP with GTP. Two major families of ARF GEPs are known: approximately 200-kDa molecules that are inhibited by brefeldin A (BFA), a fungal metabolite that blocks protein secretion and causes apparent disintegration of Golgi structure, and approximately 50-kDa GEPs that are insensitive to BFA. We describe here two human brain cDNAs that encode BFA-inhibited GEPs. One is a approximately 209-kDa protein 99.5% identical in deduced amino acid sequence (1, 849 residues) to a BFA-inhibited ARF GEP (p200) from bovine brain. The other smaller protein, which is approximately 74% identical (1, 785 amino acids), represents a previously unknown gene. We propose that the former, p200, be named BIG1 for (brefeldin A-inhibited GEP1) and the second, which encodes a approximately 202-kDa protein, BIG2. A protein containing sequences found in BIG2 had been purified earlier from bovine brain. Human tissues contained a 7.5-kilobase BIG1 mRNA and a 9.4-kilobase BIG2 transcript. The BIG1 and BIG2 genes were localized, respectively, to chromosomes 8 and 20. BIG2, synthesized as a His6 fusion protein in Sf9 cells, accelerated guanosine 5'-3-O-(thio)triphosphate binding by recombinant ARF1, ARF5, and ARF6. It activated native ARF (mixture of ARF1 and ARF3) more effectively than it did any of the nonmyristoylated recombinant ARFs. BIG2 activity was inhibited by BFA in a concentration-dependent manner but not by B17, a structural analog without effects on Golgi function. Although several clones for approximately 50-kDa BFA-insensitive ARF GEPs are known, these new clones for the approximately 200-kDa BIG1 and BIG2 should facilitate characterization of this rather different family of proteins as well as the elucidation of mechanisms of regulation of BFA-sensitive ARF function in Golgi transport.  (+info)

(8/429) Structural elements of ADP-ribosylation factor 1 required for functional interaction with cytohesin-1.

ADP-ribosylation factor 1 (ARF1) is a 20-kDa guanine nucleotide-binding protein involved in vesicular trafficking. Conversion of inactive ARF-GDP to active ARF-GTP is catalyzed by guanine nucleotide exchange proteins such as cytohesin-1. Cytohesin-1 and its Sec7 domain (C-1Sec7) exhibit guanine nucleotide exchange protein activity with ARF1 but not ARF-like protein 1 (ARL1), which is 57% identical in amino acid sequence. With chimeric proteins composed of ARF1 (F) and ARL1 (L) sequences we identified three structural elements responsible for this specificity. Cytohesin-1 increased [35S]guanosine 5'-(gamma-thio)triphosphate binding to L28/F (first 28 residues of L, remainder F) and to a much lesser extent F139/L, and mut13F139/L (F139/L with random sequence in the first 13 positions) but not Delta13ARF1 that lacks the first 13 amino acids; therefore, a nonspecific ARF N terminus was required for cytohesin-1 action. The N terminus was not, however, required for that of C-1Sec7. Both C-1Sec7 and cytohesin-1 effectively released guanosine 5'-(gamma-thio)triphosphate from ARF1, but only C-1Sec7 displaced the nonhydrolyzable GTP analog bound to mut13F139/L, again indicating that structure in addition to the Sec7 domain is involved in cytohesin-1 interaction. Some element(s) of the C-terminal region is also involved, because replacement of the last 42 amino acids with ARL sequence in F139L decreased markedly the interaction with cytohesin-1. Participation of both termini is consistent with the crystallographic structure of ARF in which the two terminal alpha-helices are in close proximity. ARF1 residues 28-50 are also important in the interaction with cytohesin-1; replacement of Lys-38 with Gln, the corresponding residue in ARL1, abolished the ability to serve as substrate for cytohesin-1 or C-1Sec7. These studies have defined multiple structural elements in ARF1, including switch 1 and the N and C termini, that participate in functional interactions with cytohesin-1 (or its catalytic domain C-1Sec7), which were not apparent from crystallographic analysis.  (+info)

*  GPLD1
2005). "Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of ... 2005). "Characterization of primate trypanosome lytic factors". Mol. Biochem. Parasitol. 138 (1): 9-20. doi:10.1016/j. ... 53 (1): 21-38. PMID 11939716. Jaworek J, Bonio J, Leja-Szpa A, et al. (2002). "Sensory nerves in central and peripheral control ... 325 (1-2): 59-70. doi:10.1016/S0009-8981(02)00248-6. PMID 12367767. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). " ...
*  ADP ribosylation factor
ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family ... The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular ... Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP- ... Amor JC, Harrison DH, Kahn RA, Ringe D (1994). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature. ...
*  ARF1
Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6 ... ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene. ADP-ribosylation factor 1 (ARF1) is a member ... 1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding ... "Entrez Gene: ARF1 ADP-ribosylation factor 1". Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September ...
"Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Letters. 430 (3): 231-5. ... "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Letters. 430 (3): 231-5. ... a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral". The Journal of Biological Chemistry. 275 ( ... 4 (1): 73-8. doi:10.1038/ncb720. PMID 11744922. Clough RR, Sidhu RS, Bhullar RP (Aug 2002). "Calmodulin binds RalA and RalB and ...
*  Phospholipase D1
Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric ... ADP-ribosylation factor regulates hPLD2". J. Biol. Chem. 273 (21): 12846-52. doi:10.1074/jbc.273.21.12846. PMID 9582313. Kim JH ... "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene ... "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. 430 (3): 231-5. doi: ...
*  CYTH1
Pacheco-Rodriguez G, Meacci E, Vitale N, Moss J, Vaughan M (1998). "Guanine nucleotide exchange on ADP-ribosylation factors ... "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange ... "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange ... Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909-14. doi ...
*  Exomer
... binds to 2 molecules of ADP-ribosylation factor 1 (Arf1) as shown in this figure. A hinge region of exomer is thought to ...
*  ARF6
ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety ... Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6 ... "ADP-ribosylation factor 6 as a target of guanine nucleotide exchange factor GRP1". J. Biol. Chem. 274 (38): 27099-104. doi: ... Amor JC, Harrison DH, Kahn RA, Ringe D (1995). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature. ...
*  ARL1
ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, ... ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1 gene. The protein encoded by this ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both ...
*  ARF3
ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene. ADP-ribosylation factor 3 (ARF3) is a member ... "Entrez Gene: ARF3 ADP-ribosylation factor 3". Kanoh H, Williger BT, Exton JH (February 1997). "Arfaptin 1, a putative cytosolic ... Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (1992). "Characterization of the human gene encoding ADP-ribosylation factor 1, a ... Boman AL, Zhang Cj, Zhu X, Kahn RA (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane ...
*  TMED10
2002). "Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23". EMBO J. 20 ( ... 200 (1-2): 149-56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. Gommel D, Orci L, Emig EM, et al. (1999). "p24 and p23, the ... 138 (1-2): 171-4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). " ... 1 (1): 139-53. doi:10.1016/S1534-5807(01)00004-1. PMID 11703931. Gommel DU, Memon AR, Heiss A, et al. ( ...
*  CYTH3
1998). "Nerve growth factor- and epidermal growth factor-stimulated translocation of the ADP-ribosylation factor-exchange ... 1998). "ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of ... and it may have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ... guanine nucleotide-exchange proteins for ADP-ribosylation factors". J. Biol. Chem. 275 (5): 3221-30. doi:10.1074/jbc.275.5.3221 ...
ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene. The protein encoded by ... "Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1". Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S ... It is related to the ADP-ribosylation factor (ARF) and ARF-like (ARL) genes. The gene is located in a gene cluster that ... 1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide ...
ADP-ribosylation factor GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARFGAP1 gene. Two transcript ... which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein ...
*  PIP5K1A
2000). "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible ... Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha is an enzyme that in humans is encoded by the PIP5K1A gene. GRCh38: ... 2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315-21. doi:10.1038/nature04727 ...
ADP-ribosylation factor GTPase-activating protein 3 is a protein that in humans is encoded by the ARFGAP3 gene. The protein ... "Entrez Gene: ARFGAP3 ADP-ribosylation factor GTPase activating protein 3". Human ARFGAP1 genome location and ARFGAP1 gene ... which associates with the Golgi apparatus and which is thought to interact with ADP-ribosylation factor 1 (ARF1). The encoded ... 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven ...
*  TRIM23
This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its ... Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M (Jul 1998). "Localization of ADP-ribosylation factor domain protein 1 (ARD1) ... Vitale N, Moss J, Vaughan M (Oct 1997). "Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor ... Vitale N, Moss J, Vaughan M (Jan 1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor ...
*  List of MeSH codes (D12.776.476)
... adp-ribosylation factor 1 MeSH D12.776.476.525.400.025 -- rab1 gtp-binding proteins MeSH D12.776.476.525.400.050 -- rab2 gtp- ... tnf receptor-associated factor 2 MeSH D12.776.476.024.500.875 -- tnf receptor-associated factor 3 MeSH D12.776.476.024.500.937 ... tnf receptor-associated factor 5 MeSH D12.776.476.024.500.968 -- tnf receptor-associated factor 6 MeSH D12.776.476.075.405.200 ... interferon-stimulated gene factor 3, gamma subunit MeSH D12.776.476.024.389.124 -- interferon regulatory factor-1 MeSH D12.776. ...
*  CYTH2
Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6 ... Lee SY, Pohajdak B (2000). "N-terminal targeting of guanine nucleotide exchange factors (GEF) for ADP ribosylation factors (ARF ... Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (2001). "beta-Arrestin-mediated ADP-ribosylation factor ... "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45 ...
*  NAT5
1 (3): 287-92. doi:10.1093/embo-reports/kvd058. PMC 1083732 . PMID 11256614. Deloukas P, Matthews LH, Ashurst J, et al. (2002 ... 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem ...
"Entrez Gene: ARFIP1 ADP-ribosylation factor interacting protein 1 (arfaptin 1)". Tsai SC, Adamik R, Hong JX, et al. (1998). " ... a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J Biol Chem. 272 (9): 5421-9 ... Arfaptin-1 is a protein that in humans is encoded by the ARFIP1 gene. ARFIP1 has been shown to interact with ARF3. GRCh38: ... 537 (1-3): 91-5. doi:10.1016/S0014-5793(03)00098-X. PMID 12606037. Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete ...
*  ARL6IP1
ADP-ribosylation factor-like protein 6-interacting protein 1 is a protein that in humans is encoded by the ARL6IP1 gene. GRCh38 ... ARL6IP1 ADP-ribosylation factor-like 6 interacting protein 1". Human ARL6IP1 genome location and ARL6IP1 gene details page in ... "A novel ADP-ribosylation like factor (ARL-6), interacts with the protein-conducting channel SEC61beta subunit". FEBS Lett. 459 ... ADP-ribosylation-like factor-6 interacting protein (ARL6)". Genomics. 68 (3): 351-4. doi:10.1006/geno.2000.6278. PMID 10995579 ...
*  Centaurin, alpha 1
... an ADP-ribosylation factor 6 GTPase activating protein, inhibits beta 2-adrenoceptor internalization". Molecular Pharmacology. ... 5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating ... membrane trafficking induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin ... 128 (1): 9-13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, ...
*  List of MeSH codes (D08)
... adp-ribosylation factors MeSH D08.811.277.040.330.300.400.100.100 --- ADP-ribosylation factor 1 MeSH D08.811.277.040.330.300. ... factor ixa MeSH D08.811.277.656.300.760.315 --- factor xa MeSH D08.811.277.656.300.760.320 --- factor xia MeSH D08.811.277.656. ... peptide elongation factor g MeSH D08.811.277.040.330.300.100.700 --- peptide elongation factor tu MeSH D08.811.277.040.330.300. ... adp-ribosyl cyclase MeSH D08.811.913.400.725.115.680 --- pertussis toxin MeSH D08.811.913.400.725.115.690 --- poly(adp-ribose) ...
"Entrez Gene: ARFGEF1 ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited)". Padilla PI, Chang MJ ... ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene ... "Isolation of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (ARF) 1 and ARF3 that ... "Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors". The ...
... belongs to an ADP-ribosylation factor GTPase-activating (ARF-GAP) protein family involved in membrane traffic and actin ... phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton". The Journal of ... 128 (1): 9-13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, ... Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 is an enzyme that in humans is encoded by the AGAP1 gene. ...
ADP-ribosylation factor-like tumour-suppressor protein 1 | definition of ADP-ribosylation factor-like tumour-suppressor protein...  ADP-ribosylation factor-like tumour-suppressor protein 1 | definition of ADP-ribosylation factor-like tumour-suppressor protein...
Looking for online definition of ADP-ribosylation factor-like tumour-suppressor protein 1 in the Medical Dictionary? ADP-ribosylation factor-like tumour-suppressor protein 1 explanation free. What is ADP-ribosylation factor-like tumour-suppressor protein 1? Meaning of ADP-ribosylation factor-like tumour-suppressor protein 1 medical term. What does ADP-ribosylation factor-like tumour-suppressor protein 1 mean?
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ARFGAP1 recombinant protein | ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP 001268411.1  ARFGAP1 recombinant protein | ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP 001268411.1
Buy ARFGAP1 recombinant protein, ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP_001268411.1 (MBS1301288) product datasheet at MyBioSource, Recombinant Proteins
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Arl2 - ADP-ribosylation factor-like protein 2 - Mus musculus (Mouse) - Arl2 gene & protein  Arl2 - ADP-ribosylation factor-like protein 2 - Mus musculus (Mouse) - Arl2 gene & protein
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle.
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ADP-ribosylation factor-like protein 3  ADP-ribosylation factor-like protein 3
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit ...
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SYT1 - Arf guanine nucleotide exchange factor SYT1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) -...  SYT1 - Arf guanine nucleotide exchange factor SYT1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) -...
Guanine nucleotide exchange factor for Arf GTPases, stimulating the nucleotide exchange from the GDP-bound to the GTP-bound form. Catalyzes both the GDP release by and the GTP binding to ARF2. Has no exhange activity on Rab GTPases. Involved in vesicular transport.
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WikiGenes - ARL6IP6 - ADP-ribosylation factor-like 6 interacting...  WikiGenes - ARL6IP6 - ADP-ribosylation factor-like 6 interacting...
The world's first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
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ARL5C (ADP-ribosylation factor-like 5C) - KOMP (Knockout Mouse Project)  ARL5C (ADP-ribosylation factor-like 5C) - KOMP (Knockout Mouse Project)
The KOMP Repository is located at the University of California Davis and Children's Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
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arl15a, ADP-ribosylation factor-like 15a - Creative Biogene  arl15a, ADP-ribosylation factor-like 15a - Creative Biogene
Creative Biogene offers challenging job opportunities for people looking for career growth in an entrepreneurial environment that recognizes individual contributions ...
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Effect of protein kinase a activity on the association of ADP-ribosylation factor 1 to Golgi membranes  Effect of protein kinase a activity on the association of ADP-ribosylation factor 1 to Golgi membranes
Ver más] The small GTP-binding protein ADP-ribosylation factor 1 (ARF1) is an essential component of the molecular machinery that catalyzes the formation of membranebound transport intermediates. By using an in vitro assay that reproduces recruitment of cytosolic proteins onto purified, high salt-washed Golgi membranes, we have analyzed the role of cAMP-dependent protein kinase A (PKA) on ARF1 incorporation. Addition to this assay of either pure catalytic subunits of PKA (C-PKA) or cAMP increased ARF1 binding. By contrast, ARF1 association was inhibited following C-PKA inactivation with either PKA inhibitory peptide or RIIa as well as after cytosol depletion of C-PKA. C-PKA also stimulated recruitment and activation of a recombinant form of human ARF1 in the absence of additional cytosolic components. The binding step could be dissociated from the activation reaction and found to be independent of guanine nucleotides and saturable. This step was stimulated ...
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ARL4A acts with GCC185 to modulate Golgi complex organization | Journal of Cell Science  ARL4A acts with GCC185 to modulate Golgi complex organization | Journal of Cell Science
ADP-ribosylation factor-like protein 4A (ARL4A) is a developmentally regulated member of the ARF/ARL GTPase family. The primary structure of ARL4A is very similar to that of other ARF/ARL molecules, but its function remains unclear. The trans-Golgi network golgin GCC185 is required for maintenance of Golgi structure and distinct endosome-to-Golgi transport. We show here that GCC185 acts as a new effector for ARL4 to modulate Golgi organization. ARL4A directly interacts with GCC185 in a GTP-dependent manner. Sub-coiled-coil regions of the CC2 domain of GCC185 are required for the interaction between GCC185 and ARL4A. Depletion of ARL4A reproduces the GCC185-depleted phenotype, causing fragmentation of the Golgi compartment and defects in endosome-to-Golgi transport. GCC185 and ARL4A localize to the Golgi independently of each other. Deletion of the ARL4A-interacting region of GCC185 results in inability to maintain Golgi structure. Depletion of ARL4A impairs ...
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Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1  Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
This gene encodes a member of an ADP-ribosylation factor GTPase-activating protein family involved in membrane trafficking and cytoskeleton dynamics. This gene functions as a direct regulator of the adaptor-related protein complex 3 on endosomes. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011 ...
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Short coiled-coil protein  Short coiled-coil protein
This gene encodes a short coiled-coiled domain-containing protein that localizes to the Golgi apparatus. The encoded protein interacts with ADP-ribosylation factor-like proteins. Pseudogenes of this gene are found on chromosomes 1 and 14. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2009 ...
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OriGene - ARL2 (NM 001667) cDNA Clone  OriGene - ARL2 (NM 001667) cDNA Clone
ARL2 - ARL2 (untagged)-Human ADP-ribosylation factor-like 2 (ARL2), transcript variant 1 available for purchase from OriGene - Your Gene Company.
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OriGene - ARF1 (NM 001658) cDNA Clone  OriGene - ARF1 (NM 001658) cDNA Clone
ARF1 - ARF1 (untagged)-Human ADP-ribosylation factor 1 (ARF1), transcript variant 4 available for purchase from OriGene - Your Gene Company.
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The small GTPASE - ARF like protein 1 (ARL1) is a new regulator of golgi structure and function | ScholarBank@NUS  The small GTPASE - ARF like protein 1 (ARL1) is a new regulator of golgi structure and function | [email protected]
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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OriGene - Arl2bp (NM 001024906) cDNA Clone  OriGene - Arl2bp (NM 001024906) cDNA Clone
Arl2bp - Arl2bp (untagged ORF) - Rat ADP-ribosylation factor-like 2 binding protein (Arl2bp), (10 ug) available for purchase from OriGene - Your Gene Company.
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microRNAs in the onset and development of cardiovascular disease | Clinical Science  microRNAs in the onset and development of cardiovascular disease | Clinical Science
Abbreviations: ABC, ATP-binding cassette transporter; ANGPTL3, angiopoietin-like 3; apo, apolipoprotein; ARL7, ADP-ribosylation factor-like 7; CAD, coronary artery disease; CXCR4, CXC receptor 4; EC, endothelial cell; FOXA2, forkhead box A2; GPAM, glycerol-3-phosphate acyltransferase 1; HDL, high-density lipoprotein; HDL-C, HDL-cholesterol; HMGCR, 3-hydroxy-3-methylglutaryl-CoA reductase; IL, interleukin; LDL, low-density lipoprotein; LDLR, LDL receptor; LNA, locked nucleic acid; LOX-1, oxidized LDL receptor 1; LPL, lipoprotein lipase; LPS, lipopolysaccharide; LXR, liver X receptor; Mct1, monocarboxylate transporter 1; MI, myocardial infarction; miRNA, microRNA; Mtpn, myotrophin; NFAT, nuclear factor of activated T-cells; NF-κB, nuclear factor κB; p27Kip1, cyclin-dependent kinase inhibitor 1B; p57Kip2, cyclin-dependent kinase inhibitor 1C; oxLDL, oxidized LDL; PEPCK, phosphoenolpyruvate carboxykinase; PI3K, phosphoinositide ...
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Anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p))  Anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p))
Top performende anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p)) vergleichen & kaufen.
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What rhymes with adp-ribosylation factor 1?  What rhymes with adp-ribosylation factor 1?
... Lookup it up at - the most comprehensive rhyming words dictionary on the web!
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Acetylcholine ??4??2 Nicotinic Receptors  Acetylcholine ??4??2 Nicotinic Receptors
The tiny G protein Arf1 regulates Golgi traffic and it is activated by two related types of guanine nucleotide exchange factor (GEF). We validate this using the Arf1 orthologue (Arf79F) as well as the related course II Arf (Arf102F) which demonstrated a similar design of effector binding. Applying the technique towards the Arf-like G proteins Arl1 we discovered that it binds right to Sec71 the ortholog of BIG1 TNFSF14 and BIG2 via an N-terminal area. We display that in mammalian cells Arl1 is essential for Golgi recruitment of BIG2 and BIG1 however not GBF1. Thus Arl1 works to immediate a trans-Golgi-specific Arf1 GEF and therefore active Arf1 towards the trans part from the Golgi. Intro The members from the ADP ribosylation element (Arf) category of little G proteins are crucial regulators of membrane visitors and cytoskeletal systems (D'Souza-Schorey and Chavrier 2006 Biopterin Gillingham and Munro 2007 Donaldson and Jackson 2011 Distinct through the other ...
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The small GTPase Arf1 modulates mitochondrial morphology and function | The EMBO Journal  The small GTPase Arf1 modulates mitochondrial morphology and function | The EMBO Journal
In addition, the arf1‐11∆arf2 mutation results in aggregated Fzo1, which is removed by overexpression of Cdc48. We identified Cdc48 as an interactor of Arf1‐GTP. Thus, a third function could be the recruitment of the AAA‐ATPase Cdc48 to mitochondria to remove Fzo1 and potentially other mitochondrial outer membrane proteins. In the wild‐type situation, Arf1 would promote recruitment of Cdc48 to mitochondria to maintain proper Fzo1 homeostasis, whereas in the mutant situation aberrant Fzo1 would accumulate because Cdc48 is recruited less efficiently. Cdc48 has a known role in the quality control of mitochondrial outer membrane proteins in yeast and worms and promotes degradation of Fzo1 (Heo et al, 2010). Consistently, the mammalian Cdc48 homologue p97 promotes ubiquitylation and proteasome‐dependent degradation of the mitofusins Mfn1 and Mfn2 (Tanaka et al, 2010). Our data are in agreement with the recently reported role of Cdc48/p97/VCP in the retro‐translocation of mitochondrial ...
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Table of Contents - January 02, 2017, 216 (1) | JCB  Table of Contents - January 02, 2017, 216 (1) | JCB
Rafiq et al. demonstrate that the small G protein ARF1 and its activator, cytohesin 2 (ARNO), are required for podosome formation in macrophage-like cells and fibroblasts. Inhibition of ARNO-ARF1 signaling results in increased RhoA activity and disassembly of podosomes in a myosin-IIA-dependent fashion. In fibroblasts that normally do not form podosomes, constitutively active ARF1 induces actin-rich puncta associated with sites of matrix degradation, putative precursors of podosomes. ...
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Endosomal membrane dynamics underlying cell spreading: A role for the small GTPase Arf6 - Academic Commons  Endosomal membrane dynamics underlying cell spreading: A role for the small GTPase Arf6 - Academic Commons
Cell migration is an orchestrated and highly coordinated multi-step process that is central to the development and maintenance of multicellular organisms. Dysregulated migration however, is associated with pathological states such as tumor formation and metastasis; thus a clear understanding of the molecular mechanisms that drive this process is critical to the development of counteracting therapeutics. Cell migration and adhesion-dependent cell spreading share a number of features. For example, both processes rely on the activation of mechanisms for the coordinated spatial and temporal assembly/disassembly of focal adhesions, as well as mechanisms controlling actin rearrangements and directed vesicular trafficking. Actin remodeling and vesicular trafficking events are in turn, implicated functions of a variety of small GTPases of the Ras superfamily, which include the Rho and Arf subfamilies. Thus towards efforts of further characterizing the molecular pathways that drive cell spreading, I pursued aims
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British Library EThOS: Characterisation of the human Arl4 and Arl8 families of small GTPases  British Library EThOS: Characterisation of the human Arl4 and Arl8 families of small GTPases
Two closely related human Arls, Arl8a and Arl8b, were found to localise to lysosomes in mammalian cells. conventionally, membrane binding of Arf and Arl proteins is mediated by both an N-terminal myristoyl group and an N-terminal amphipathic helix that are inserted into the lipid bilayer upon activation of the GTPase. Arl8 GPTases lack myristolylation sites, and examination of the N-terminus of Arl8b revealed that it contains an acetyl group instead, and this acetylated methionine is necessary for its lysosomal location. Lysosomes of cells overexpressing Arl8b move more frequently, suggesting a role for Arl8a and Arl8b as positive regulators of lysosomal transport. Arl4a, Arl4c and Arl4d are very similar in sequence and were found to act in a pathway upstream of Arf6, Arf6 is a regulator of key processes at the plasma membrane, such as endocytosis, actin dynamics and cell adhesion. One of the major activators of Arf6 is the exchange factor ARNO ('Arf nucleotide binding site opener'). In ...
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  • PARP-1 dissociates Smad complexes from DNA by ADP-ribosylating Smad3 and Smad4, which attenuates Smad-specific gene responses and TGF-β-induced epithelial-mesenchymal transition. (
  • In an unbiased proteomic screen, we identified poly(ADP-ribose) polymerase-1 (PARP-1) as a Smad-interacting partner. (
  • Production and auto-induction of transforming growth factor-alpha in human keratinocytes. (
  • Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice. (