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.
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.
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)
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.
TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to 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.
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
The sequence at the 3' end of messenger RNA that does not code for product. This region contains transcription and translation regulating sequences.
A republic in western Africa, south of NIGER between BENIN and CAMEROON. Its capital is Abuja.
The sequence at the 5' end of the messenger RNA that does not code for product. This sequence contains the ribosome binding site and other transcription and translation regulating sequences.
The parts of the messenger RNA sequence that do not code for product, i.e. the 5' UNTRANSLATED REGIONS and 3' UNTRANSLATED REGIONS.
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.
Exclusive legal rights or privileges applied to inventions, plants, etc.
A genus of protozoa parasitic to birds and mammals. T. gondii is one of the most common infectious pathogenic animal parasites of man.
A specific HLA-B surface antigen subtype. Members of this subtype contain alpha chains that are encoded by the HLA-B*40 allele family.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
The acquired form of infection by Toxoplasma gondii in animals and man.
A dye used to stain proteins in electrophoretic techniques. It is used interchangeably with its acid form.
The study of the composition, chemical structures, and chemical reactions of the NERVOUS SYSTEM or its components.
Tumors or cancer of the OVARY. These neoplasms can be benign or malignant. They are classified according to the tissue of origin, such as the surface EPITHELIUM, the stromal endocrine cells, and the totipotent GERM CELLS.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
A malignant epithelial tumor with a glandular organization.
Ubiquitously expressed integral membrane glycoproteins found in the LYSOSOME.
The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE.
A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.
A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in calcium-dependent EXOCYTOSIS. This enzyme was formerly listed as EC 3.6.1.47.
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.
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.
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)
Publications in any medium issued in successive parts bearing numerical or chronological designations and intended to be continued indefinitely. (ALA Glossary of Library and Information Science, 1983, p203)
The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.
Databases devoted to knowledge about specific genes and gene products.
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
A sequential pattern of amino acids occurring more than once in the same protein sequence.
The technique of spraying a tissue specimen with a thin coat of a heavy metal such as platinum. The specimen is sprayed from an oblique angle, which results in the uneven deposition of the coating. The varying thicknesses create a shadow effect and give a three-dimensional appearance to the specimen.
The portion of an interactive computer program that issues messages to and receives commands from a user.
Collections of illustrative plates, charts, etc., usually with explanatory captions.
The cells found in the body fluid circulating throughout the CARDIOVASCULAR SYSTEM.
The first cervical vertebra.
A multistage process that includes cloning, physical mapping, subcloning, sequencing, and information analysis of an RNA SEQUENCE.
Progenitor cells from which all blood cells derive.
Methods to identify and characterize cancer in the early stages of disease and predict tumor behavior.
New abnormal growth of tissue. Malignant neoplasms show a greater degree of anaplasia and have the properties of invasion and metastasis, compared to benign neoplasms.
Tumors or cancer of the human BREAST.
Tumors or cancer of the PROSTATE.
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.-.
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.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
Rapid methods of measuring the effects of an agent in a biological or chemical assay. The assay usually involves some form of automation or a way to conduct multiple assays at the same time using sample arrays.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
The genetic complement of an insect (INSECTS) as represented in its DNA.
Proteins found in any species of bacterium.

Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. (1/266)

COPI-coated vesicle budding from lipid bilayers whose composition resembles mammalian Golgi membranes requires coatomer, ARF, GTP, and cytoplasmic tails of putative cargo receptors (p24 family proteins) or membrane cargo proteins (containing the KKXX retrieval signal) emanating from the bilayer surface. Liposome-derived COPI-coated vesicles are similar to their native counterparts with respect to diameter, buoyant density, morphology, and the requirement for an elevated temperature for budding. These results suggest that a bivalent interaction of coatomer with membrane-bound ARF[GTP] and with the cytoplasmic tails of cargo or putative cargo receptors is the molecular basis of COPI coat assembly and provide a simple mechanism to couple uptake of cargo to transport vesicle formation.  (+info)

Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. (2/266)

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)

Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. (3/266)

The Saccharomyces cerevisiae maltose transporter is a 12-transmembrane segment protein that under certain physiological conditions is degraded in the vacuole after internalization by endocytosis. Previous studies showed that endocytosis of this protein is dependent on the actin network, is independent of microtubules, and requires the binding of ubiquitin. In this work, we attempted to determine which coat proteins are involved in this endocytosis. Using mutants defective in the heavy chain of clathrin and in several subunits of the COPI and the COPII complexes, we found that clathrin, as well as two cytosolic subunits of COPII, Sec23p and Sec24p, could be involved in internalization of the yeast maltose transporter. The results also indicate that endocytosis of the maltose transporter and of the alpha-factor receptor could have different requirements.  (+info)

Inhibition of secretion by 1,3-Cyclohexanebis(methylamine), a dibasic compound that interferes with coatomer function. (4/266)

We noted previously that certain aminoglycoside antibiotics inhibit the binding of coatomer to Golgi membranes in vitro. The inhibition is mediated in part by two primary amino groups present at the 1 and 3 positions of the 2-deoxystreptamine moiety of the antibiotics. These two amines appear to mimic the epsilon-amino groups present in the two lysine residues of the KKXX motif that is known to bind coatomer. Here we report the effects of 1, 3-cyclohexanebis(methylamine) (CBM) on secretion in vivo, a compound chosen for study because it contains primary amino groups that resemble those in 2-deoxystreptamine and it should penetrate lipid bilayers more readily than antibiotics. CBM inhibited coatomer binding to Golgi membranes in vitro and in vivo and inhibited secretion by intact cells. Despite depressed binding of coatomer in vivo, the Golgi complex retained its characteristic perinuclear location in the presence of CBM and did not fuse with the endoplasmic reticulum (ER). Transport from the ER to the Golgi was also not blocked by CBM. These data suggest that a full complement of coat protein I (COPI) on membranes is not critical for maintenance of Golgi integrity or for traffic from the ER to the Golgi but is necessary for transport through the Golgi to the plasma membrane.  (+info)

Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes. (5/266)

The Nef protein of primate lentiviruses downregulates the cell surface expression of CD4 through a two-step process. First, Nef connects the cytoplasmic tail of CD4 with adaptor protein complexes (AP), thereby inducing the formation of CD4-specific clathrin-coated pits that rapidly endocytose the viral receptor. Second, Nef targets internalized CD4 molecules for degradation. Here we show that Nef accomplishes this second task by acting as a connector between CD4 and the beta subunit of COPI coatomers in endosomes. A sequence encompassing a critical acidic dipeptide, located nearby but distinct from the AP-binding determinant of HIV-1 Nef, is responsible for beta-COP recruitment and for routing to lysosomes. A novel class of endosomal sorting motif, based on acidic residues, is thus revealed, and beta-COP is identified as its downstream partner.  (+info)

p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. (6/266)

COPI-coated vesicles that bud off the Golgi complex contain two major transmembrane proteins, p23 and p24. We have localized the protein at the Golgi complex and at COPI-coated vesicles. Transport from the intermediate compartment (IC) to the Golgi can be blocked at 15 degrees C, and under these conditions p24 accumulates in peripheral punctated structures identified as IC. Release from the temperature block leads to a redistribution of p24 to the Golgi, showing that p24, similar to p23, cycles between the IC and Golgi complex. Immunoprecipitations of p24 from cell lysates and from detergent-solubilized Golgi membranes and COPI-coated vesicles show that p24 and p23 interact with each other to form a complex. Transient transfection of p23 in HeLa cells shows that p23 and p24 colocalize in structures induced by the overexpression of p23. Taken together p24 interacts with p23 and constitutively cycles between the organelles of the early secretory pathway.  (+info)

Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation. (7/266)

Physiological conditions that impinge on constitutive traffic and affect organelle structure are not known. We report that osmotically induced cell volume changes, which are known to occur under a variety of conditions, rapidly inhibited endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells. Both ER export and ER Golgi intermediate compartment (ERGIC)-to-Golgi trafficking steps were blocked, but retrograde transport was active, and it mediated ERGIC and Golgi collapse into the ER. Extensive tubulation and relatively rapid Golgi resident redistribution were observed under hypo-osmotic conditions, whereas a slower redistribution of the same markers, without apparent tubulation, was observed under hyperosmotic conditions. The osmotic stress response correlated with the perturbation of COPI function, because both hypo- and hyperosmotic conditions slowed brefeldin A-induced dissociation of betaCOP from Golgi membranes. Remarkably, Golgi residents reemerged after several hours of sustained incubation in hypotonic or hypertonic medium. Reemergence was independent of new protein synthesis but required PKC, an activity known to mediate cell volume recovery. Taken together these results indicate the existence of a coupling between cell volume and constitutive traffic that impacts organelle structure through independent effects on anterograde and retrograde flow and that involves, in part, modulation of COPI function.  (+info)

GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. (8/266)

A site-directed photocross-linking approach was employed to determine components that act downstream of ADP-ribosylation factor (ARF). To this end, a photolabile phenylalanine analog was incorporated at various positions of the putative effector region of the ARF molecule. Depending on the position of incorporation, we find specific and GTP-dependent interactions of ARF with two subunits of the coatomer complex, beta-COP and gamma-COP, as well as an interaction with a cytosolic protein (approximately 185 kDa). In addition, we observe homodimer formation of ARF molecules at the Golgi membrane. These data suggest that the binding site of ARF to coatomer is at the interface of its beta- and gamma-subunits, and this is in close proximity to the second site of interaction of coatomer with the Golgi membrane, the binding site within gamma-COP for cytosolic dibasic/diphenylalanine motifs.  (+info)

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
COPE Full-Length MS Protein Standard (NP_009194), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. It is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least the alpha, beta, beta, gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.
Coatomer subunit beta-1; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (948 aa ...
Among all retroviruses, foamy viruses (FVs) are unique in that they regularly mature at intracytoplasmic membranes. The envelope glycoprotein of FV encodes an endoplasmic reticulum (ER) retrieval signal, the dilysine motif (KKXX), that functions to localize the human FV (HFV) glycoprotein to the ER. This study analyzed the function of the dilysine motif in the context of infectious molecular clones of HFV that encoded mutations in the dilysine motif. Electron microscopy (EM) demonstrated virion budding both intracytoplasmically and at the plasma membrane for the wild-type and mutant viruses. Additionally, mutant viruses retained their infectivity, but viruses lacking the dilysine signal budded at the plasma membrane to a greater extent than did wild-type viruses. Interestingly, this relative increase in budding across the plasma membrane did not increase the overall release of viral particles into cell culture media as measured by protein levels in vital pellets or infectious virus titers. We ...
plant Sar1 (ER marker) , Q8VYP7, AS08 326, Sar1 belongs to a small GTPase superfamily and GTP binging activity. This protein is involved in intracellular protein transport. There are two different non-clathrin-coated vesicle
COPB antibody [maD] (coatomer protein complex subunit beta 1) for ELISA, ICC/IF, WB. Anti-COPB mAb (GTX26323) is tested in Human, Monkey, Rat, Hamster samples. 100% Ab-Assurance.
The gene that encodes ARCN1 maps in a region, which includes the mixed lineage leukemia and Friend leukemia virus integration 1 genes, where multiple…
Characterisation of a delta-COP homologue in the malaria parasite, Plasmodium falciparum.: The mature human erythrocyte is a simple haemoglobin-containing cell
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Coatomer subunit gamma ; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (899 aa ...
Microinjection of the slowly hydrolyzable GTP analogue GTP(gamma)S or the ectopic expression of a GTP restricted mutant of the small GTPase arf1 (arf1[Q71L]) leads to the rapid accumulation of COPI coated vesicles and buds in living cells. This effect is blocked at 15 degrees C and by microinjection of antibodies against (beta)-COP. Anterograde and retrograde membrane protein transport markers, which have been previously shown to be incorporated into COPI vesicles between the endoplasmic reticulum and Golgi complex, are depleted from the GTP(gamma)S or arf1[Q71L] induced COPI coated vesicles and buds. In contrast, in control cells 30 to 60% of the COPI carriers co-localize with these markers. These in vivo data corroborate recent in vitro work, suggesting that GTP(gamma)S and arf1[Q71L] interfere with the sorting of membrane proteins into Golgi derived COPI vesicles, and provide the first in vivo evidence for a role of GTP hydrolysis by arf1 in the sorting of cargo into COPI coated vesicles and ...
Recently, Lanoix et al. 1999 have analyzed the resident protein (glycosyltransferase) content of an uncoated membrane fraction produced from Golgi membranes in vitro (in the presence of GTP) that is thought to be derived from COPI-coated vesicles, and compared this with bona fide COPI-coated vesicles prepared with GTPγS. They report (Table IV in Lanoix et al., 1999) a 9.6-fold higher concentration (protein/phospholipid) of NAGT I and a 4.8-fold higher concentration of Man II, in the uncoated (GTP) vesicles than in the starting Golgi fraction and an exclusion of residents in the GTPγS -prepared coated vesicles. There was no corresponding enrichment in anterograde-directed cargo in the GTP-produced uncoated vesicles (1.7-fold for pIgR) or in bona fide COP I-coated vesicles made with GTPγS (1.2-fold). In contradiction to this, Nickel et al. 1998 analyzed bona fide coated COPI vesicles produced in the presence of GTP versus GTPγS, and report that anterograde-directed cargo is up to 50-fold more ...
Calcium-regulated non-lysosomal thiol-protease. Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex (By similarity ...
Membrane, Proteins, Endoplasmic Reticulum, Reticulum, Secretory Pathway, Yeast, Gtpase, Coated Vesicles, Copi, Copi-coated Vesicles, and Clathrin
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Vesicular transport shuttles proteins and membranes among the different organellar compartments within the cell. Coat proteins act as the core machinery that in...
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ウサギ・ポリクローナル抗体 ab2913 交差種: Rat,Hu,NHuPrm 適用: WB,IP,ICC…alpha COP I抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
DRTS_LEIAM (P16126 ), DRTS_LEIMA (P07382 ), DRTS_MAIZE (O81395 ), DRTS_ORYSJ (Q2QRX6 ), DRTS_PARTE (Q27828 ), DRTS_PLABA (Q27713 ), DRTS_PLACH (P20712 ), DRTS_PLAFK (P13922 ), DRTS_PLAVI (O02604 ), DRTS_PLAVN (P46103 ), DRTS_SOYBN (P51820 ), DRTS_TOXGO (Q07422 ), DRTS_TRYBB (Q27783 ), DRTS_TRYCR (Q27793 ), DYR10_ECOLX (Q04515 ), DYR13_ECOLX (Q59408 ), DYR15_ECOLX (P78218 ), DYR1_ECOLX (P00382 ), DYR1_HALMA (Q5V3R2 ), DYR2_HALMA (Q5V600 ), DYR3_SALTM (P12833 ), DYR5_ECOLX (P11731 ), DYR6_PROMI (P95524 ), DYR7_ECOLX (P27422 ), DYR8_ECOLX (P0ABQ7 ), DYR8_SHISO (P0ABQ8 ), DYR9_ECOLX (Q59397 ), DYRA_HALVD (P15093 ), DYRA_STAAU (P13955 ), DYRB_HALVO (Q9UWQ4 ), DYR_AEDAL (P28019 ), DYR_BACSU (P11045 ), DYR_BOVIN (P00376 ), DYR_BPT4 (P04382 ), DYR_BUCAI (P57243 ), DYR_BUCAP (Q8K9Z8 ), DYR_BUCBP (Q89AV2 ), DYR_CAEEL (Q93341 ), DYR_CANAX (P22906 ), DYR_CHICK (P00378 ), DYR_CITFR (P31073 ), DYR_CRYNJ (Q07801 ), DYR_DROME (P17719 ), DYR_ECOL6 (P0ABQ5 ), DYR_ECOLI (P0ABQ4 ), DYR_ENTFC (P00380 ), DYR_HAEIN ...
p,Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 Å. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit α-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within α-COP itself, mediates α-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that α-COP ...
Author: Rein, U. et al.; Genre: Journal Article; Published in Print: 2002-04-29; Open Access; Keywords: Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport|br/|; Title: ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
Steroids and SARMs are indispensable when it comes to muscle growth. Besides, they bring no side effects at all! Or not? Lets find out together.
TY - JOUR. T1 - Tethering assays for COPI vesicles mediated by golgins. AU - Satoh, Ayano. AU - Malsam, Jörg. AU - Warren, Graham. N1 - Funding Information: We thank all members of the Warren, Mellman, and Toomre laboratories for helpful comments and discussions, and Marino Zerial for generous provision of purified EEA1. This work was supported by the NIH and the Ludwig Institute for Cancer Research. A.S. was supported by the American Heart Association.. PY - 2005. Y1 - 2005. N2 - A method is described that allows the attachment of COPI vesicles and Golgi membranes to glass slides that can then be analyzed using electron microscopy (EM) and immuno-EM methods. Subpopulations of COPI vesicles can be bound selectively using recombinant golgins. Alternatively, COPI vesicles can be attached to prebound Golgi membranes. Marking these vesicles selectively with biotin allows their site of attachment to be identified.. AB - A method is described that allows the attachment of COPI vesicles and Golgi ...
In addition to the better characterized COPI-dependent retrograde Golgi-to-ER pathway, a second COPI-independent pathway has also been identified. This pathway is RAB6 dependent and transports cargo such as glycosylation enzymes and Shiga and Shiga-like toxin through tubular carriers rather than vesicles (White et al, 1999; Girod et al, 1999; reviewed in Heffernan and Simpson, 2014). In the absence of a COPI coat, the membrane curvature necessary to initiate tubulation may be provided through the action of phospholipase A, which hydrolyzes phospholipids at the sn2 position to yield lysophospholipids. This activity is countered by lysophospholipid acyltransferases, and the balance of these may influence whether transport tubules or transport vesicles form (de Figuiredo et al, 1998; reviewed in Bechler et al, 2012). RAB6-dependent tubules also depend on the dynein-dynactin motor complex and the hoomodimeric Bicaudal proteins (Matanis et al, 2002; Yamada et al, 2013; reviewed in Heffernan and ...
Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. Amino acid differences in be
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
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Coat protein complex I (COPI) vesicles are involved in transport processes within the early secretory pathway (Bethune et al., 2006). For their biogenesis, the small GTPase ADP ribosylation factor 1 (Arf1) in its GDP-bound form is recruited to the Golgi membrane by dimeric transmembrane proteins of the p24 family (Gommel et al., 2001) or by interaction with membrin (Honda et al., 2005). The membrane-associated Arf guanine nucleotide exchange factor GBF1 catalyzes exchange of the bound GDP to GTP (Zhao et al., 2006). Arf1-GTP dissociates from the p24 proteins and is inserted into the Golgi membrane (Franco et al., 1996; Antonny et al., 1997) as a dimer (Beck et al., 2008) to recruit the heptameric protein complex coatomer (Palmer et al., 1993). Coatomer polymerization leads to the formation of a COPI-coated vesicle (Bremser et al., 1999; Reinhard et al., 1999). Arf GTPase-activating proteins (GAPs) catalyze hydrolysis of the GTP bound to Arf1 followed by dissociation of the coat (Tanigawa et al., ...
Daria Sicari, Aeid Igbaria, Eric Chevet. Control of Protein Homeostasis in the Early Secretory Pathway Current Status and Challenges. Cells, MDPI, 2019, 8 (11), pp.E1347. ⟨10.3390/cells8111347⟩. ⟨hal-02365417⟩ ...
Pasul 1. Aprinzi cuptorul, speli cartofii cu apă călduţă (nu îi cureţi de coajă), îi ştergi de apă, îi înţepi pe fiecare în parte în două locuri (opuse) cu o furculiţă, îi pui pe o coală de hârtie de copt, pe o tavă nu prea adâncă şi îi pui la cuptor, la foc puternic, vreo 15 minute şi la foc mediu spre mic până sunt gata. Când sunt gata? Atunci când sunt pătrunşi în momentul în care îi verifici cu furculiţa.. Pasul 2. În paralel, pui ouăle la fiert.. Pasul 3. Cât s-au copt cartofii şi au fiert ouăle, pregăteşti celelalte ingrediente. Adică: cureţi ceapa roşie şi ceapa verde, speli puţin măslinele de urmele de zeamă în care fuseseră murate, fărâmi telemeaua de capră şi toci cele două feluri de ceapă. Pe cea roşie - rondele, iar pe cea verde - mărunţel.. Pasul 4. După ce s-au copt, laşi cartofii să se răcorească puţin, îi tai repede în jumătăţi sau în sferturi, după cât de mari sunt. Îi stropeşti imediat cu două-trei ...
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 ...
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] ...
Jain Goyal, M., Zhao, X., Bozhinova, M., Andrade-López, K., de Heus, C., Schulze-Dramac, S., Müller-McNicoll, M., Klumperman, J. and Béthune, J. (2020) A paralog-specific role of COPI vesicles in the neuronal differentiation of mouse pluripotent cells. Life Science Alliance, 3, e202000714.. Rafiee, M.R., Sigismondo, G., Kalxdorf, M., Forster, L., Brugger, B., Béthune, J. and Krijgsveld, J. (2020) Protease-resistant streptavidin for interaction proteomics. Molecular systems biology, 16, e9370.. Adolf, F., Rhiel, M., Hessling, B., Gao, Q., Hellwig, A., Béthune, J. and Wieland, F.T. (2019) Proteomic Profiling of Mammalian COPII and COPI Vesicles. Cell reports, 26, 250-265 e255.. Béthune, J., Jansen, R.P., Feldbrugge, M. and Zarnack, K. (2019) Membrane-Associated RNA-Binding Proteins Orchestrate Organelle-Coupled Translation. Trends in cell biology, 29, 178-188.. Egetemaier, S. and Béthune, J. (2019). Proteomik-Analyse von dynamischen Proteinkomplexen. Biospektrum (Springer Verlag) 01.19, ...
The nucleotide sequences of the nucleoprotein (NP) genes of fowl plague virus (FPV) and of a temperature-sensitive (ts) mutant (ts81) derived therefrom have been determined. The ts81-NP nucleotide sequence possesses a single nucleotide substitution in comparison to the wild type. This causes an amin …
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 ...
1FQE: Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin.
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
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
Im currently cutting for the next two months and need some input on what natural bulking stack would help me achieve the best goals possible. I was
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 ...
SCYL1 binds COP1 vesicles that mediate retrograde Golgi-to ER transport, through an SCYL1-specific RKLD motif at the extreme C terminus [2]. Knockdown of SCYL1 disrupts Golgi morphology and blocks retrograte COPI-mediated transport from Golgi to ER [3]. The Golgi-localized Gorab protein (aka NTKL-BP1, SCYL-BP1) was found as a interactor of mouse Scyl1 by Y2H and coIP [4]. The yeast SCYL1, Cex1, also has several trafficking-associated physical and genetic interactors, including YPT6 (Golgi fusion of late endosome vesicles), COG5 and COG6 (fusion of vesicles to Golgi), several COPI complex members (COP1, SEC27, SEC29, RET2, UBP5 and BRE5 (ER-Golgi transport), and RGP1 and RIC1 (Golgi-to-ER transport) (BioGrid). SCYL2 appears to act a a different point in trafficking - the endocytosis and trafficking of surface proteins. Human SCYL2 (aka CVAK104) binds clathrin and the plasma membrane adaptor complex, AP2 [5]. Yeast SCYL2 (Cex1) was also found in a genetic screen for modifiers of a clathrin mutant ...
View Notes - Lecture 13 11 from BICD 110 at UCSD. Lecture 13 11/02/07 Golgi Structure/Function, Lysosome, Exocytosis Glycosylation Protects lysosome membrane proteins from autodegradation
The mammalian Golgi complex is composed of stacks of flattened cisternae linked through tubules to form a contiguous juxtanuclear ribbon. The stacked cisternae reflect the compartmentalization of Golgi enzymes for the processing of transiting cargo (Mellman and Simons, 1992; Puthenveedu and Linstedt, 2005). Cargo movement through the stack has been variously suggested to occur in vesicles, in maturing cisternae, or by tubular connections between cisternae (Malhotra et al., 1989; Mollenhauer and Morre, 1991; Glick et al., 1997; Allan and Balch, 1999; Pelham and Rothman, 2000; Trucco et al., 2004). Although not exclusive of other processes, maturation has gained recent support (Emr et al., 2009). This model starts with the creation of cargo-containing cis-Golgi cisternae. The cargo stays within these cisternae and is sequentially processed when the cis enzymes are replaced with medial enzymes, which are subsequently replaced with trans enzymes. As cisternae progress through the Golgi stack, this ...
chains in the Genus database with same CATH superfamily 3UAI C; 2RFK C; 2EY4 C; 3MQK C; 2HVY B; 2V3M A; 2EQN A; 3U28 C; #chains in the Genus database with same CATH topology 3SUF A; 2AEI H; 5DP8 A; 3WY8 A; 1OWI A; 2ZU5 A; 3KHV A; 4Y11 E; 1SGF G; 1NBM D; 3Q3X A; 1C2H A; 4IN1 A; 3RM0 H; 1ZZZ A; 3KQE A; 1GHY H; 1MMJ N; 1TOC B; 3N7E A; 3M5M A; 2R3Y A; 1TPP A; 2P3T B; 5C0U A; 1SOT A; 1GBH A; 2PKS B; 3QX5 H; 3FO8 D; 1ZMN A; 3IIT A; 1C5P A; 4KEL A; 5L2Z H; 1K0H A; 1QGF A; 2THF B; 3GDU A; 5F8Z A; 2KM0 A; 2A4Q A; 1P9S A; 1TMB H; 2ZGX H; 3S9C A; 2ZC9 H; 1O5F H; 1FY1 A; 2BD4 A; 1KLJ H; 3MU8 A; 2OUA A; 3SGB E; 4O9V A; 3K6Z A; 3NK8 A; 4X6M A; 3BIU H; 5JB8 S; 1HDT H; 3URE A; 2DE8 A; 1QRX A; 1OKX A; 4Y8Z A; 1CU1 A; 1EOL A; 1F92 A; 4M7G A; 4B76 A; 1YPL H; 1K22 H; 4I31 A; 1O2K A; 3PLP A; 2FM2 A; 4B73 A; 4I7Y H; 1O5C B; 1OWJ A; 1DFP A; 5IDK A; 4Y8Y A; 4I33 A; 3ZVB A; 1W0Z U; 3RXC A; 1ZGV A; 1XUF A; 1KMH B; 1O2W A; 2C4F H; 4TY6 A; 8KME 2; 1CSO E; 2VID A; 4SGA E; 2DE9 A; 1CE5 A; 5A2M H; 2B8O H; 3M36 A; 4Q7X A; 5T6G ...
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.
Regarding the biogenesis of peroxisomes various concepts have been postulated. Based on morphological data that demonstrated close spatial relationships between peroxisomes and the ER, Novikoff and Novikoff (44) favored the idea that new peroxisomes are formed by budding and fission from the ER. However, a series of biochemical studies initiated by de Duve and coworkers (36, 51) in the early 1970s, focusing on the biogenetic route of catalase as a peroxisomal marker, did not reveal an ER involvement in the import of catalase. Subsequent findings of Goldman and Blobel (19) and particularly the group of Lazarow and coworkers (52, 54) confirmed this view demonstrating that peroxisomal matrix proteins, such as catalase, urate oxidase, and enzymes of the peroxisomal β-oxidation pathway, are synthesized on free polyribosomes and thus are imported posttranslationally. Accordingly, Goldman and Blobel (19) postulated a model in which peroxisomal matrix proteins are found in nascent peroxisomes, whereas ...
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 COPI is a comprehensive oral proficiency assessment that provides reliable, valid results to help inform instruction and gauge student progress.. The COPI is designed to assess the oral proficiency of upper high school students, college students, and professionals who are native or near-native English speakers learning the target language. The COPI provides language professionals with a computerized, time-efficient tool to assess their students language proficiency. The COPIs computerized delivery uses up-to-date technology, and its semi-adaptive design adjusts test difficulty level to students proficiency levels. Performance on the COPI is rated according to the ACTFL Proficiency Guidelines-Speaking.. The COPI is available in two formats (USB or CD) and includes the following components:. COPI Test Administration Program ...
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. This review offers a summary of vesicular trafficking with an emphasis on the ARF1 and SAR1 expression patterns at early growth stages and in the de-etiolation process.
Newly synthesized proteins and lipids are transported across the Golgi complex via different mechanisms whose respective roles are not completely clear. We previously identified a non-vesicular intra-Golgi transport pathway for glucosylceramide (GlcCer)--the common precursor of the different series of glycosphingolipids-that is operated by the cytosolic GlcCer-transfer protein FAPP2 (also known as PLEKHA8) (ref. 1). However, the molecular determinants of the FAPP2-mediated transfer of GlcCer from the cis-Golgi to the trans-Golgi network, as well as the physiological relevance of maintaining two parallel transport pathways of GlcCer--vesicular and non-vesicular--through the Golgi, remain poorly defined. Here, using mouse and cell models, we clarify the molecular mechanisms underlying the intra-Golgi vectorial transfer of GlcCer by FAPP2 and show that GlcCer is channelled by vesicular and non-vesicular transport to two topologically distinct glycosylation tracks in the Golgi cisternae and the trans-Golgi
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Complete information for ARF6 gene (Protein Coding), ADP Ribosylation Factor 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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 ...
Complete information for ARL6IP6 gene (Protein Coding), ADP Ribosylation Factor Like GTPase 6 Interacting Protein 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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…
Fluorescent and time lapse microscopy, advantages of multiplex analysis and the Golgi apparatus. Please donwload this free white paper for more inform
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 product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. ...
Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene. It is one of seven proteins in the COPI ... "Entrez Gene: COPG coatomer protein complex, subunit gamma". Bermak, Jason C; Li Ming; Bullock Clayton; Weingarten Paul; Zhou ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex" (PDF). J. Cell ...
Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene. In eukaryotic cells, protein transport between ... "Entrez Gene: COPA coatomer protein complex, subunit alpha". Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell ...
Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene. COPG2 has been shown to interact with ... "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2". Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (Feb 2002). " ... Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
Coatomer subunit zeta-1 is a protein that in humans is encoded by the COPZ1 gene. COPZ1 has been shown to interact with COPG. ... "Entrez Gene: COPZ1 coatomer protein complex, subunit zeta 1". Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (November ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex" (PDF). J. Cell ... Overview of all the structural information available in the PDB for UniProt: P61923 (Human Coatomer subunit zeta-1) at the PDBe ...
"The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon". J. Biol. Chem. 272 (46): 29200 ... Coatomer subunit beta' is a protein that in humans is encoded by the COPB2 gene. The Golgi coatomer complex (see MIM 601924) ... "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)". Eugster A, Frigerio G, Dale M, Duden R (August 2000 ... "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ...
... is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to ... 1994). "Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum". Cell. 79 (7): 1199-207. ... Luminal proteins: Proteins found in the lumen of the Golgi complex that need to be transported to the lumen of the ER contain ... 1996). "A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding". J Cell Biol. 135 (5 ...
Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene. COPI coatomer, a protein complex GRCh38: ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein ...
Though PCTV does not require COPII coatomer proteins for budding from the ER, association with the coatomer is necessary for ... Without the fully functional sar1B protein, the COPll coatomer proteins engulf pre-chylomicrons exiting the ER but are unable ... Sar1B is a GTPase and one of the five proteins of the COPll coatomer. A mutation in the sar1B gene and subsequently the sar1B ... Before the PCTV leaves the ER, it is incorporated into a COPII coatomer of five proteins. The PCTV undergoes a similar ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... ARF6+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH) Human ARF6 genome location and ARF6 ... D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L (1997). "A role for POR1, a Rac1-interacting protein, in ARF6 ... ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... 2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... The gene products include 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ... ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene. ADP-ribosylation factor 4 (ARF4) is a member ... Shin OH, Ross AH, Mihai I, Exton JH (1999). "Identification of arfophilin, a target protein for GTP-bound class II ADP- ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 ( ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction ... AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
... is a coatomer, a type of vesicle coat protein that transports proteins from the rough endoplasmic reticulum to the Golgi ... COPII's coat is composed of five proteins: Sar1, Sec23, Sec24, Sec13, and Sec31. These proteins dimerize to form larger protein ... Embo) Crystal structures of CopII Conformation of the CopII protein complexed with the snare protein Bet1 (PDB: 1PCX​). ... The coat consists of large protein subcomplexes that are made of four different protein subunits. ...
Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles.. Nature. 1991-01-17 ... 運輸囊泡(Transport vesicles)在真核生物中,通過在不同細胞器及細胞表面進行轉運發揮它的作用。目前已知的運輸囊泡有網格蛋白囊泡、外被體蛋白(英语:Coat protein)Ⅰ(coat protein、COPI(英语:COPI)囊泡)和 ... Lee, C; Goldberg, J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle
Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. PMID ... "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. PMC 1847948. PMID ... Koatomerna podjedinica gama-2 je protein koji je kod ljudi kodiran COPG2 genom.[1][2][3] ...
... a human gene that encodes the protein coatomer subunit epsilon COPE (film), a 2007 psychological thriller/horror independent ...
... a human gene that encodes the coatomer subunit alpha protein Controlling Profitability Analysis, Profitability Analysis (SAP) ...
They are also common in membrane coat proteins known as coatomers, such as clathrin, and in regulatory proteins that form ... The protein-protein interaction capacity of alpha solenoid proteins also makes them well suited to function as regulatory ... extended protein-protein interaction surfaces or to form deep concave areas for binding globular proteins. Because they are ... "When protein folding is simplified to protein coiling: the continuum of solenoid protein structures". Trends in Biochemical ...
Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ... Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These ...
Components of COPI (cop one) a coatomer, and TSET (T-set) a membrane trafficking complex have similar heterotetramers of the AP ... In the AP complexes, there are two large proteins (∼100 kD) and two smaller proteins. One of the large proteins is termed β ( ... PTBs are protein domains that include NUMB, DAB1 and DAB2. Epsin and AP180 in the ANTH domain are other adaptor proteins that ... The individual proteins of the COPII complex are called SEC proteins, because they are encoded by genes identified in secretory ...
The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: COPI ( ... Coatomer+Protein at the US National Library of Medicine Medical Subject Headings (MeSH) Boehm, Markus; Bonifacino, Juan S. ( ... COP II is a coatomer that coats the vesicles transporting proteins from the ER to the golgi complex. This pathway is referred ...
1999). "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ... Retinol binding protein 1, cellular, also known as RBP1, is a protein that in humans is encoded by the RBP1 gene. RBP1 is the ... "The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane ... Alteration of relative protein amounts is linked to the state of differentiation". Biochem. J. 287. ( Pt 2) (2): 383-9. doi: ...
The coatomer subunit delta (delta-COP) is a cytosolic protein complex that binds to motifs and associates with vesicles ... Role of Mammalian Vacuolar Protein-sorting Proteins in Endocytic Trafficking of a Non-ubiquitinated G Protein-coupled Receptor ... There is no evidence of post-translational modifications of the TMEM267 protein found in tissues. According to protein sequence ... The protein was identified as a member of a large group of proteins that comprise a filter in mammalian cells which allow ...
2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... Scyl1 localizes to the cis-Golgi and ER-Golgi Intermediate Compartment (ERGIC). Scyl1 binds to Coatomer I (COPI) and ... This gene encodes a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. The protein has a ... The FL protein contains HEAT repeats and a C-terminal coiled coil domain that also contains multiple dibasic motifs, and ends ...
... is a protein located on chromosome 11. Also known as ARCN1, it plays a role in eukaryotic cell biology. It is part of ... the COPI coatomer complex. Xu X, Kedlaya R, Higuchi H, et al. (2010). "Mutation in archain 1, a subunit of COPI coatomer ...
2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs ... 2004). "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex". J. Biol. Chem. 278 (52): 52689- ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355-64. doi: ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347-55. doi: ...
The proteins lining the inner pore make up the NUP62 complex. On the nucleoplasm side, extra proteins associated with the ring ... the ancestral coatomer elements (ACE). To date, two classes of ACEs have been identified. ACE1 is a 28-helix domain found in ... Different sets of proteins associate on either ring, and some transmembrane proteins anchor the assembly to the lipid bilayer. ... Karyopherins can serve as an importin (transporting proteins into the nucleus) or an exportin (transporting proteins out of the ...
... including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ... The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively ... ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene. ADP-ribosylation factor 1 (ARF1) is a member ...
Two examples of adaptor proteins are AP180[3] and epsin.[4][5][6] AP180 is used in synaptic vesicle formation. It recruits ... Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by ... Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis ... In a cell, a triskelion floating in the cytoplasm binds to an adaptor protein, linking one of its feet to the membrane at a ...
The protein ELKS binds to the cell adhesion protein, β-neurexin, and other proteins within the complex such as Piccolo and ... It is stabilized by proteins within the active zone and bound to the presynaptic membrane by SNARE proteins. These vesicles are ... In the periactive zone, scaffolding proteins such as intersectin 1 recruit proteins that mediate endocytosis such as dynamin, ... Neuroligin then interacts with proteins that bind to postsynaptic receptors. Protein interactions like that seen between ...
"GPCR-G Protein-β-Arrestin Super-Complex Mediates Sustained G Protein Signaling". Cell. 166 (4): 907-919. doi:10.1016/j.cell. ... A mature pit will be cleaved from the plasma membrane through the use of membrane binding and fission proteins such as dynamin ... Glass JJ, Yuen D, Rae J, Johnston AP, Parton RG, Kent SJ, De Rose R (April 2016). "Human immune cell targeting of protein ... The cargo ligand and receptor will then recruit adaptor proteins and clathrin triskelions to the outside membrane of the cell ...
In molecular biology caveolins are a family of integral membrane proteins that are the principal components of caveolae ... The caveolin gene family has three members in vertebrates: CAV1, CAV2, and CAV3, coding for the proteins caveolin-1, caveolin-2 ... All three members are membrane proteins with similar structure. Caveolin forms oligomers and associates with cholesterol and ... Various classes of signaling molecules, including G-protein subunits, receptor and non-receptor tyrosine kinases, endothelial ...
... is a complex of proteins that has been shown to be important in recycling transmembrane receptors from endosomes to ... The cargo carrier is transported to the TGN by motor proteins such as dynein. Tethering of the cargo carrier to the recipient ... However, it is clear that there are other complexes and proteins that act in this retrieval process. So far it is not clear ... Retromer plays a central role in the retrieval of several different cargo proteins from the endosome to the trans-Golgi network ...
Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6". The Journal of ... protein transport. • vesicle fusion. • Golgi ribbon formation. • vesicle-mediated transport. • intracellular protein transport ... regulation of cellular protein localization. • endosome organization. • regulation of protein localization. • vesicle docking. ... This protein-related article is a stub. You can help Wikipedia by expanding it.. *v ...
This protein-related article is a stub. You can help Wikipedia by expanding it. *v ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038/ ... RefSeq (protein). NP_001153800. NP_001153801. NP_115674. NP_001153800.1. NP_001153801.1. ... Synaptotagmin-3 is a protein that in humans is encoded by the SYT3 gene.[5][6] ...
ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1 gene. The protein encoded by this ... Zhao L, Helms JB, Brunner J, Wieland FT (1999). "GTP-dependent binding of ADP-ribosylation factor to coatomer in close ... "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
"GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins". ... 2000). "RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport". Mol. Biol. ... RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins ... Regulator of G protein signaling 4 protein is 37% identical to RGS1 and 97% identical to rat Rgs4. This protein negatively ...
Transmembrane emp24 domain-containing protein 2 is a protein that in humans is encoded by the TMED2 gene. TMED2 has been shown ... Fiedler K, Veit M, Stamnes MA, Rothman JE (September 1996). "Bimodal interaction of coatomer with the p24 family of putative ... two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular ... Majoul I, Straub M, Hell SW, Duden R, Söling HD (July 2001). "KDEL-cargo regulates interactions between proteins involved in ...
... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex ... The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also ...
wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary ... knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound ...
Coatomer Protein / Cytosol / Animals / Membranes, Artificial / Metabolism Language: English Journal: Protein & Cell Year: 2016 ... Coatomer Protein / Cytosol / Animals / Membranes, Artificial / Metabolism Language: English Journal: Protein & Cell Year: 2016 ... Coatomer Protein , Chemistry , Metabolism , Cytosol , Chemistry , Metabolism , GTPase-Activating Proteins , Chemistry , ... Studies on coat protein I (COPI) have contributed to a basic understanding of how coat proteins generate vesicles to initiate ...
In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ...
Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae ... Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae. ... Both proteins contain cytoplasmic exposed C termini that have the ability to interact directly with COPI and COPII coat ... Protein trafficking is achieved by a bidirectional vesicle flow between the various compartments of the eukaryotic cell. COPII ...
The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. ...
Coatomer-dependent protein delivery to lipid droplets.. Soni KG, Mardones GA, Sougrat R, Smirnova E, Jackson CL, Bonifacino JS. ... Imaging intracellular fluorescent proteins at nanometer resolution.. Betzig E, Patterson GH, Sougrat R, Lindwasser OW, Olenych ... Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway. ...
Coatomer protein complex, subunit epsilon. COPE. 263. 1179. NM_001861. Cytochrome c oxidase subunit IV isoform 1. COX4I1. 129. ... Preferred therapeutic proteins are interferones, growth factors, anti-angiogenesis proteins, apoptosis modulating proteins, ... The proteins can be either expressed in a secreted form or in cellular compartments. The expressed proteins can further be ... When proteins are expressed transiently a foreign gene that codes for the particular protein is expressed by recipient/host ...
A general protein machinery that buds and fuses transport vesicles is harnessed to generate the complex web of intracellular ... Carrier Proteins / physiology * Coatomer Protein * Endoplasmic Reticulum / metabolism * GTP-Binding Proteins / physiology ... The protein machinery of vesicle budding and fusion Protein Sci. 1996 Feb;5(2):185-94. doi: 10.1002/pro.5560050201. ... A general protein machinery that buds and fuses transport vesicles is harnessed to generate the complex web of intracellular ...
GTP-binding protein, the ADP-ribosylation factor (ARF). Binding of ARF to Golgi membranes is necessary before coatomer/beta-COP ... exchange on ARF-1 protein, and which is inhibited by brefeldin A. We suggest that activation of ARF proteins for membrane ... In addition to the coatomer (a cytosol-derived complex of seven polypeptide chains, one of which is beta-COP), the non-clathrin ... Brefeldin A added to cells causes the rapid and reversible dissociation of a Golgi-associated peripheral membrane protein (M(r ...
The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: COPI ( ... Coatomer+Protein at the US National Library of Medicine Medical Subject Headings (MeSH) Boehm, Markus; Bonifacino, Juan S. ( ... COP II is a coatomer that coats the vesicles transporting proteins from the ER to the golgi complex. This pathway is referred ...
Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. Amino acid differences in be ... Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. ... 0/Coatomer Protein; 0/DNA Primers; 0/DNA, Protozoan; 0/Protozoan Proteins ... Coatomer Protein / genetics*. DNA Primers / genetics. DNA, Protozoan / genetics. Evolution, Molecular. Genes, Protozoan. Models ...
coatomer protein complex, subunit epsilon. MGI:1891702 1 matching records from 1 references.. Summary by Age and Assay: Numbers ...
Coatomer protein complex, subunit beta 1. 1.85. 1.52. N/A. 21070976. Diablo homolog. N/A. 1.54. 1.50. ... 10 μg total protein lysates loaded. Protein levels were normalized to actin loading control. Aconitase 2 is detected at ∼80 kDa ... Table I Significantly changed proteins post-EGF exposure; proteins identified with significant changes following EGF treatment ... subcellular distribution of all proteins significantly altered following EGF treatment (n = 294 proteins across 48 h time ...
Abbreviation for coatomer protein.. COP. 1. Capillary osmotic pressure.. 2. Colloid oncotic pressure. ...
In this review, we will summarize recent advances in regard to LD-related membrane trafficking proteins and discuss future ... In this review, we will summarize recent advances in regard to LD-related membrane trafficking proteins and discuss future ... In recent years, multiple membrane trafficking proteins have been identified through LD proteomics and genetic analyses. These ... In recent years, multiple membrane trafficking proteins have been identified through LD proteomics and genetic analyses. These ...
... coatomer protein complex, subunit gamma 2 54161 Copg1; coatomer protein complex, subunit gamma 1 59042 Cope; coatomer protein ... 14688 Gnb1; guanine nucleotide binding protein (G protein), beta 1 14702 Gng2; guanine nucleotide binding protein (G protein), ... 14707 Gng5; guanine nucleotide binding protein (G protein), gamma 5 14708 Gng7; guanine nucleotide binding protein (G protein ... major vault protein K17267 COPG; coatomer subunit gamma K17267 COPG; coatomer subunit gamma K17268 COPE; coatomer subunit ...
... coatomer protein; CT, Cholera toxin; ER, endoplasmic reticulum; GFP, green fluorescent protein; KDELR, KDEL-receptor; PE, ... 1994) Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell. 79:1199-1207 pmid: ... 1997) Coatomer (COPI)-coated vesiclesrole in intracellular transport and protein sorting. Curr. Opin. Cell Biol. 9:484-487 pmid ... 1998) gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer. J. Cell Biol. 140:751- ...
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex miRNA assays. By ...
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex Assays. By ... The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating ...
coatomer subunit zeta-1 [Source:RefSeq peptide;Acc:NP_571583]. Human Orthologue:. COPZ1. Human Description:. coatomer protein ... coatomer protein complex, subunit zeta 1 Gene [Source:MGI Symbol;Acc:MGI:1929063]. ...
coatomer protein complex, subunit beta 1 [Source:HGNC Symbol;Acc:2231]. Mouse Orthologue:. Copb1. Mouse Description:. coatomer ... coatomer subunit beta [Source:RefSeq peptide;Acc:NP_001002013]. Human Orthologue:. COPB1. Human Description:. ... protein complex, subunit beta 1 Gene [Source:MGI Symbol;Acc:MGI:1917599]. ...
coatomer protein complex subunit alpha. HEP-COP. 1q23.2. COPB2 coatomer protein complex subunit beta 2. beta-COP, betaprime- ... syntaxin binding protein 5 like. KIAA1006, LLGL4. 3q13.33. TAF5 TATA-box binding protein associated factor 5. TAF2D. TAFII100. ... POC1 centriolar protein B. WDR51B. TUWD12, FLJ14923. 12q21.33. PPP2R2A protein phosphatase 2 regulatory subunit Balpha. PR52A, ... mitogen-activated protein kinase binding protein 1. KIAA0596. 15q15.1. MED16 mediator complex subunit 16. THRAP5. DRIP92, ...
coatomer protein complex, subunit alpha. 5285498. Incomplete. BC037941. coatomer protein complex, subunit alpha. ... Protein Similarities Based on Shared Motif Content. Find gene products sharing protein motifs with: NP_004362 Protein ... BP] intracellular protein transport *[BP] pancreatic juice secretion *[BP] retrograde vesicle-mediated transport, Golgi to ER * ...
Coatomer protein complex subunit zeta 2. Predicted locationi. All transcripts of all genes have been analyzed regarding the ... PROTEIN DETECTED IN PLASMA - PROXIMITY EXTENSION ASSAYi. The protein profiling results based on proximity extension assays ( ... PROTEIN CONCENTRATION IN PLASMA - MASS SPECTROMETRYi. The protein concentration in blood is quantified by mass spectrometry- ... Protein expression levels are reported as Normalized Protein Expression (NPX).. Read more ...
coatomer protein complex, subunit beta 1. Protein Similarities Based on Shared Motif Content. ... BP] intracellular protein transport *[BP] protein transport *[BP] transport *[BP] vesicle-mediated transport *[CC] COPI vesicle ...
The cancer tissue page shows antibody staining of the protein in 20 different cancers. ... Coatomer protein complex subunit zeta 2. Predicted locationi. All transcripts of all genes have been analyzed regarding the ... Evidence at protein level. Protein expression. normal tissuei. A summary of the overall protein expression pattern across the ... Protein evidencei. Evidence score for genes based on UniProt protein existence (UniProt evidence); a Human Protein Atlas ...
Coatomer: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles.. Nature. 1991-01-17 ... 運輸囊泡(Transport vesicles)在真核生物中,通過在不同細胞器及細胞表面進行轉運發揮它的作用。目前已知的運輸囊泡有網格蛋白囊泡、外被體蛋白(英语:Coat protein)Ⅰ(coat protein、COPI(英语:COPI)囊泡)和 ... Lee, C; Goldberg, J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle
Seven coat proteins have been identified and they represent subunits of a complex known as coatomer. The subunits are ... In eukaryotic cells protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non- ... The alpha-COP encoded by COPA shares high sequence similarity with RET1P the alpha subunit of the coatomer complex in yeast. ...
... β-coatomer protein) (orange), and DIAP (red). βCOP is required for general secretion and viability and DIAP (Drosophila ... E, Protein sequence homology between Drosophila Paf-AHα and human PAFAH1B2 demonstrates a highly conserved protein. Green boxes ... 2A). The protein levels of APP and actin were unaffected. Likewise, the level of NCT and the maturation of this protein, a key ... Aβ is derived from amyloid precursor protein (APP), a type I transmembrane protein that traffics through the secretory pathway ...
  • COPII coated vesicles mediate anterograde protein transport from the endoplasmic reticulum to the Golgi apparatus, whereas retrograde Golgi-to-endoplasmic reticulum vesicles use the COPI coat. (unibas.ch)
  • Two types of coatomers are known: COPI (retrograde transport from trans-Golgi network to cis-Golgi network and endoplasmic reticulum) COPII (anterograde transport from ER to the cis-Golgi) Coatomers are functionally analogous and evolutionarily homologous to clathrin adaptor proteins, also known as adaptins, which regulate endocytosis from the plasma membrane and transport from the trans-Golgi network to lysosomes. (wikipedia.org)
  • In eukaryotic cells protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). (bio-rad.com)
  • Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. (sciencemag.org)
  • Many resident proteins of the endoplasmic reticulum (ER) are localized to that compartment by continuous retrieval from the Golgi complex. (embopress.org)
  • However, both vesicle types are devoid of endoplasmic reticulum (ER) resident proteins, and each contains targeting proteins necessary for docking at the Golgi complex. (nih.gov)
  • Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. (genecards.org)
  • Once at the Golgi membrane, the coatomer complex may assist in the movement of protein and lipid components back to the endoplasmic reticulum. (genetex.com)
  • We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. (pubmedcentralcanada.ca)
  • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. (eu.org)
  • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. (eu.org)
  • Retrieval of transmembrane proteins to the endoplasmic reticulum. (eu.org)
  • Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval. (eu.org)
  • Asparagine- or N -linked carbohydrates are added to nascent proteins as they enter the lumen of the endoplasmic reticulum (ER). (jimmunol.org)
  • The working hypothesis assumes that sorting decisions are already made at the site where the membrane proteins are born, that is the endoplasmic reticulum (ER). (meduniwien.ac.at)
  • The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs) implications for fusion and fusion regulation. (mpg.de)
  • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. (mpg.de)
  • The coatomer-interacting protein Dsl 1 p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. (mpg.de)
  • Coatomer proteins are involved in regulating transport between the endoplasmic reticulum (ER) and the Golgi complex and in intra-Golgi transport. (novusbio.com)
  • As determined by confocal microscopy, HCV proteins expressed from VT7-HCV7.9 localize largely in a globular-like distribution pattern in the cytoplasm, with some proteins co-localizing with the endoplasmic reticulum (ER) and mitochondria. (biomedcentral.com)
  • The KDEL receptor (KDELR) is a seven-transmembrane-domain protein involved in retrograde transport of protein chaperones from the Golgi complex to the endoplasmic reticulum. (hindawi.com)
  • The transport of cargoes from the endoplasmic reticulum (ER) to the Golgi complex involves temporary mislocalisation of ER-resident proteins into post-ER compartments. (hindawi.com)
  • Schweizer A, Fransen, JAM, Matter K, Kreis TE, Ginsel L, Hauri HP (1990) Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to Golgi apparatus. (springer.com)
  • BACKGROUND: Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have beenshown to be critical components of the coated vesicles that are involved in thetransportation of cargo molecules from the endoplasmic reticulum to the Golgicomplex. (embl.de)
  • Moreover, retention of APP695 proteins in the endoplasmic reticulum led to neither βA4 secretion nor to processing by β-secretase in human SH-SY5Y neuroblastoma cells. (jneurosci.org)
  • Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. (embl.de)
  • Located at the C-terminus of ER type I membrane proteins (cytoplasmic in this topology), interacts with members of the coatomer (COPI). (eu.org)
  • ER retention and retrieving signal found at the C-terminus of type I ER membrane proteins (cytoplasmic in this topology). (eu.org)
  • The di-Lysine motif is found in type I membrane proteins of the ER and interacts directly with COPI (gamma-COP), which then drives the recycling of type I membrane proteins to the ER. (eu.org)
  • PHB-domain proteins are integral membrane proteins or are strongly associated with cell membranes via posttranslational modifications (i.e., acyl moieties) or via hydrophobic regions. (hindawi.com)
  • Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. (embl.de)
  • Sorting of integral membrane proteins is mediated vesicular trafficking between a variety of organelles. (fishersci.com)
  • The AP-1 and AP-3 complexes are involved in protein sorting from the TGN and endosomes, while AP-2, µ2 (AP50) interacts with integral membrane proteins via binding to tyrosine-based signals with the canonical motif YXXφ. (fishersci.com)
  • Thus, AP50/µ2 may be involved in targeting integral membrane proteins that are sorted based on tyrosine-based signals and involved in assembly of functional ion channels associated with clathrin coated vesicles. (fishersci.com)
  • The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. (uniprot.org)
  • Studies on coat protein I ( COPI ) have contributed to a basic understanding of how coat proteins generate vesicles to initiate intracellular transport. (bvsalud.org)
  • Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. (wikipedia.org)
  • A general protein machinery that buds and fuses transport vesicles is harnessed to generate the complex web of intracellular transport pathways critical for such diverse processes as cell growth, endocytosis, hormone release, and neurotransmission. (nih.gov)
  • Brefeldin A added to cells causes the rapid and reversible dissociation of a Golgi-associated peripheral membrane protein (M(r) 110,000) which was found to be identical to one of the subunits of the coat of Golgi-derived (non-clathrin) coated vesicles, beta-COP, implying that brefeldin A prevents transport by blocking the assembly of coats and thus the budding of enclosed vesicles. (nih.gov)
  • In addition to the coatomer (a cytosol-derived complex of seven polypeptide chains, one of which is beta-COP), the non-clathrin (COP) coat of Golgi-derived vesicles contains stoichiometric amounts of a small (M(r) approximately 20,000) GTP-binding protein, the ADP-ribosylation factor (ARF). (nih.gov)
  • The coatomer is a protein complex that coats membrane-bound transport vesicles. (wikipedia.org)
  • COPI is a coatomer that coats the vesicles transporting proteins from the Golgi complex to the ER. (wikipedia.org)
  • Before the COP I protein can coat vesicles on the Golgi membrane, it must interact with a small GTPase called ARF1 (ADP ribosylation factor). (wikipedia.org)
  • COP1 coated vesicles also contain p24 proteins that assist with cargo sorting. (wikipedia.org)
  • COP II vesicles select the proper cargo by directly interacting with ER export signals that are present in transmembrane ER proteins. (wikipedia.org)
  • Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. (biomedsearch.com)
  • The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. (abcam.com)
  • Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. (embopress.org)
  • The dilysine motif is recognized by coatomer subunits ( Cosson and Letourneur, 1994 ), and dilysine‐tagged transmembrane cargo is thereby packaged into COPI(coatomer)‐coated vesicles for retrograde transport to the ER ( Letourneur et al , 1994 ). (embopress.org)
  • The cytosolic yeast proteins Sec13p-Sec31p, Sec23p-Sec24p, and the small GTP-binding protein Sar1p generate protein transport vesicles by forming the membrane coat termed COPII. (nih.gov)
  • Another set of yeast cytosolic proteins, coatomer and Arf1p (COPI), also form coated buds and vesicles from the nuclear envelope. (nih.gov)
  • The formation of coat protein complex I (COPI)-coated vesicles is regulated by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor 1 (Arf1), which in its GTP-bound form recruits coatomer to the Golgi membrane. (rupress.org)
  • Arf GTPase-activating protein (GAP) catalyzed GTP hydrolysis in Arf1 triggers uncoating and is required for uptake of cargo molecules into vesicles. (rupress.org)
  • This gene encodes a protein subunit of the coatomer complex associated with non-clathrin coated vesicles. (genetex.com)
  • The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. (mdpi.com)
  • Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. (wikipedia.org)
  • Moelleken, J. 2006-10-14 00:00:00 COPI-coated vesicles are protein and liquid carriers that mediate transport within the early secretory pathway. (deepdyve.com)
  • PRCs with reduced Sec6 function accumulate secretory vesicles and fail to transport proteins to the rhabdomere, but show normal localization of proteins to the apical stalk membrane and the basolateral membrane. (pubmedcentralcanada.ca)
  • Assembly of the coatomer (COPI) onto non-clathrin coated vesicles is regulated by ADP-ribosylation factor (ARF). (novusbio.com)
  • The transport protein particle (TRAPP) was originally identified in as a vesicle tethering factor for COPII‐coated vesicles at the Golgi (Sacher et al , 2001 ). (embopress.org)
  • Duden R, Griffiths G, Frank R, Argos P, Kreis TE (1991) ß-COP, a 110kD protein associated with nonclathrin coated vesicles and cisternae of the Golgi complex shows homology to b-adaptin. (springer.com)
  • Scheel J, Kreis TE (1991) Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro. (springer.com)
  • Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE (1991) ADP-ribosylation factor (ARF) is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. (springer.com)
  • The newly detected group ofGOLD-domain proteins, which might simultaneously bind membranes and otherproteins, point to the existence of a novel class of adaptors that could have arole in the assembly of membrane-associated complexes or in regulating assemblyof cargo into membranous vesicles. (embl.de)
  • For this to occur, resident proteins must be packaged into retrograde-directed transport vesicles, and to occur at the rate of anterograde transport, resident proteins must be present in vesicles at a higher concentration than in cisternal membranes. (rupress.org)
  • This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. (embl.de)
  • Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (uniprot.org)
  • A unifying function of Arf proteins, performed in conjunction with their regulators and effectors, is sensing, modulating and transporting the lipids that make up cellular membranes. (biologists.org)
  • In this study, we show that ArfGAP2 and ArfGAP3 do not bind directly to membranes but are recruited via interactions with coatomer. (rupress.org)
  • However, only very weak (less than twofold) stimulation by coatomer of full-length ArfGAP1 was found in an assay using full-length myristoylated Arf1 on Golgi membranes. (rupress.org)
  • In NAD+-depleted cells and in the presence of dialized cytosol, BFA detached coat proteins from Golgi membranes with normal potency but failed to alter the organelle's structure. (nih.gov)
  • Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. (genecards.org)
  • Transfer of proteins across membranes. (deepdyve.com)
  • Transfer to proteins across membranes. (deepdyve.com)
  • Here we show that cells of the planctomycete Gemmata obscuriglobus have the ability to uptake proteins present in the external milieu in an energy-dependent process analogous to eukaryotic endocytosis, and that internalized proteins are associated with vesicle membranes. (pnas.org)
  • Mannosidase 2 is a 135kD protein located on the luminal side of the Golgi membranes. (acris-antibodies.com)
  • In these proteins, the GOLD domain co-occurs with lipid-, sterol- or fatty acid-binding domains such as PH, CRAL-TRIO, FYVE oxysterol binding- and acyl CoA-binding domains, suggesting that these proteins may interact with membranes. (embl.de)
  • Béthune, J. and Wieland, F.T. (2018) Assembly of COPI and COPII Vesicular Coat Proteins on Membranes. (haw-hamburg.de)
  • These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals. (sciencemag.org)
  • Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. (mpg.de)
  • Both proteins contain cytoplasmic exposed C termini that have the ability to interact directly with COPI and COPII coat complexes. (unibas.ch)
  • The cytoplasmic coatomer protein COPI. (wikipedia.org)
  • The COP1 proteins recognize the proper cargo by interacting with sorting signals on the cytoplasmic domains of the protein. (wikipedia.org)
  • As examined by electron microscopy, HCV proteins induced formation of large electron-dense cytoplasmic structures derived from the ER and containing HCV proteins. (biomedcentral.com)
  • Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. (embl.de)
  • To analyze the involvement of the endosomal/lysosomal system in the processing of APP695 into βA4, we created APP695 chimeras by exchanging the cytoplasmic domain of APP695 with that of the human lysosomal-associated membrane protein-1 (hLAMP-1) and the human cation-dependent mannose 6-phosphate receptor (CD-MPR). (jneurosci.org)
  • The coatomer protein complex is made up of seven nonidentical protein subunits. (wikipedia.org)
  • These seven nonidentical protein subunits are part of two protein subcomplexes. (wikipedia.org)
  • Seven coat proteins have been identified and they represent subunits of a complex known as coatomer. (bio-rad.com)
  • We show that Pex30p traffics through the ER and segregates in punctae to which peroxisomes specifically append, and we ascertain its transient interaction with all subunits of the COPI coatomer complex suggesting the involvement of a vesicle-mediated transport. (mcponline.org)
  • BIG1 knockout mouse nerves specifically decrease the amounts of Arf1 in the AP1 clathrin adaptor protein subunits but not the Arf1 binding to GGA1 (Golgi-localized, gamma-adaptin ear-containing, Arf-binding protein 1) transporting proteins. (sciencemag.org)
  • The amounts of Arf1 in the COPI coatomer protein subunits were comparable in the knockout mice and controls. (sciencemag.org)
  • Adaptin subunits recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal appendage domains. (embl.de)
  • This entry represents the small sigma and mu subunits of various adaptins from different AP clathrin adaptor complexes (including AP1, AP2, AP3 and AP4), and the zeta and delta subunits of various coatomer (COP) adaptors. (embl.de)
  • Protein trafficking is achieved by a bidirectional vesicle flow between the various compartments of the eukaryotic cell. (unibas.ch)
  • The Arf small G proteins regulate protein and lipid trafficking in eukaryotic cells through a regulated cycle of GTP binding and hydrolysis. (biologists.org)
  • Members of the Arf family of small GTP-binding (G) proteins are key regulators of eukaryotic cell organization. (biologists.org)
  • ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. (mdpi.com)
  • The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. (mdpi.com)
  • In eukaryotic cells, small GTP-binding proteins comprise the largest family of signaling proteins. (mdpi.com)
  • Archain sequences are well conserved among eukaryotes and this protein may play a fundamental role in eukaryotic cell biology. (acris-antibodies.com)
  • Planctomycetes are also exceptional among Bacteria because they carry genes homologous to those coding for membrane coat (MC) proteins central to eukaryotic endocytosis ( 23 ). (pnas.org)
  • The structural motifs of L-type lectins are now known to be present in a variety of glycan-binding proteins from other eukaryotic organisms. (springer.com)
  • The GOLD (for Golgi dynamics) domain is a protein module found in several eukaryotic Golgi and lipid-traffic proteins. (embl.de)
  • Eukaryotic proteins of the p24 family. (embl.de)
  • The alpha-COP encoded by COPA shares high sequence similarity with RET1P the alpha subunit of the coatomer complex in yeast. (bio-rad.com)
  • Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. (sciencemag.org)
  • When human proteins are mapped to yeast, we find a strong positive correlation (r = 0.50, P = 3.9 × 10 -4 ) between evolutionary conservation and the number of interacting proteins, which is also found when mapped to other model organisms. (biomedcentral.com)
  • Despite the preferential conservation of complexes, and the fact that the human interactome comprises an abundance of transient interactions, we demonstrate how transferring human PPIs to yeast augments this well-studied protein interaction network, using the coatomer complex and replisome as examples. (biomedcentral.com)
  • Human proteins, like yeast proteins, show a correlation between the number of interacting partners and evolutionary conservation. (biomedcentral.com)
  • A combination of low-throughput (LTP) and HTP interaction studies have produced large networks of interacting proteins in Homo sapiens (human), Rattus norvegicus (rat), Mus musculus (mouse), Drosophila melanogaster (fly), Caenorhabditis elegans (worm), and Saccharomyces cerevisiae (yeast) (see Additional data file 1 for sources). (biomedcentral.com)
  • Abgent has over fifteen years of experience producing recombinant proteins in E. coli and mammalian cells (CHO and HEK293, etc), and we have added a powerful yeast expression platform to our menu of services. (abgent.com)
  • Use1p is a yeast SNARE protein required for retrograde traffic to the ER. (mpg.de)
  • The transport protein particle ( TRAPP ) was initially identified as a vesicle tethering factor in yeast and as a guanine nucleotide exchange factor ( GEF ) for Ypt1/Rab1. (embopress.org)
  • Proteins more distantly related to ERGIC-53 and VIP36 are present in yeast and other fungi and in protozoa. (springer.com)
  • Schekman R (1985) Protein localization and membrane traffic in yeast. (springer.com)
  • Yeast oxysterol-binding protein homologue 3 (OSH3). (embl.de)
  • Next, the ARF1 protein recruits COP1 to the golgi complex membrane by interacting with β-COP and γ-COP. (wikipedia.org)
  • ARF-GAP1 is responsible for deactivating the ARF1 protein by activating the GTPase. (wikipedia.org)
  • Arf1 is the founding member of the family, and was originally identified as a protein factor required for the ADP-ribosylation of the adenylate cyclase activator Gsα by cholera toxin ( Kahn and Gilman, 1986 ). (biologists.org)
  • Although previously speculated, our results now demonstrate a function for coatomer in ArfGAP-catalyzed GTP hydrolysis by Arf1. (rupress.org)
  • A 100-1,000-fold stimulatory effect of coatomer on GTP hydrolysis was described for the catalytical domain of ArfGAP1 when a soluble version of Arf1, NΔ17Arf1, was used ( Goldberg, 1999 ). (rupress.org)
  • GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). (genecards.org)
  • Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. (harvard.edu)
  • Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. (mdpi.com)
  • Arf1 is a small guanosine triphosphate-binding protein that plays multiple roles in intracellular trafficking and related signaling, both of which are processes involved in cell morphogenesis. (sciencemag.org)
  • We demonstrate that the Arf1 guanine nucleotide exchange factor, brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1)/Arfgef1, and the effector Arf1 regulate the initiation of myelination of axons by Schwann cells. (sciencemag.org)
  • We suggest that p53/58 function may be required for the coupled exchange of COPII for COPI coats during segregation of anterograde and retrograde transported proteins. (nih.gov)
  • Whether and how cargo proteins are recruited upstream of Sar1 and COPII is unclear. (biologists.org)
  • Accordingly, we study how the proteins mature and reach the ER exit sites to recruit the COPII (coatomer proteins II) coat. (meduniwien.ac.at)
  • 4. Sucic S, El-Kasaby A, Kudlacek O, Sarker S, Sitte HH, Marin P, Freissmuth M (2011) The Serotonin Transporter Is an Exclusive Client of the Coat Protein Complex II (COPII) Component SEC24C. (meduniwien.ac.at)
  • 85 kDa protein representing COPII from PC-12 cell extract. (novusbio.com)
  • There exist two Coatomer-Protein mechanisms (COPI and COPII) and although they have mechanistic parallels, they are molecularly distinct. (novusbio.com)
  • Retrograde transport from the Golgi to the ER retrieves ER resident proteins that have escaped with the anterograde flux ( Pelham 1991 ). (rupress.org)
  • Thus, ER retrieval defines a general signal-mediated, COPI-dependent pathway of retrograde transport from the Golgi to the ER, and not simply a mechanism for localization of ER resident proteins. (rupress.org)
  • Through association with merely ER resident proteins, in particular with proteins containing a reticulon homology domain, and with other peroxins, Pex30p designates peroxisome contact sites at ER subdomains. (mcponline.org)
  • A nterograde transport along the exocytic pathway is the flux of proteins and lipids from the ER through the Golgi apparatus to their final destination in an intracellular compartment, such as the endosomes, or to the plasma membrane. (rupress.org)
  • Retrograde transport along the exocytic pathway is the flux of proteins and lipids from later to earlier exocytic compartments, reversing the order of organelle entry with respect to the anterograde transport. (rupress.org)
  • Intracellular organelles maintain their homeostasis through the continuous exchange of proteins and lipids, which tend to intermix during membrane trafficking. (hindawi.com)
  • The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). (acris-antibodies.com)
  • Gamma subunit of coatomer, a heptameric protein complex that together with Arf1p forms the COPI coat. (yeastrc.org)
  • In addition to their fundamental roles in vesicular and non-vesicular lipid trafficking, we will highlight more specialized roles of Arf proteins, including functions in lipid droplet metabolism, the cytoskeleton, cell division and trafficking to cilia ( Box 1 ). (biologists.org)
  • Since blood meal feeding creates a unique metabolic challenge as a result of the extremely high protein and iron content of blood, it is possible that interfering with blood meal metabolism could provide a novel control strategy for mosquito born diseases. (bio5.org)
  • Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. (wikipedia.org)
  • The product of this gene is an epsilon subunit of coatomer protein complex. (wikipedia.org)
  • This gene plays an important role in regulating the transport of proteins within cells. (wikipedia.org)
  • ARFGAP2 (ADP Ribosylation Factor GTPase Activating Protein 2) is a Protein Coding gene. (genecards.org)
  • RNA sequencing revealed that protein mitogen-activated protein kinase 11 ( MAPK11 ) was a potential downstream negative regulatory gene of TRIM67 . (jcancer.org)
  • TRIM67 , a TRIM family member, is a protein-coding gene located at 1q42.2 consisting of approximately 59 kb DNA bases that encodes TRIM67 (84 kDa) [ 12 ]. (jcancer.org)
  • Examining overlapping PPI networks, Gene Ontology (GO) terms, and gene expression data, we are able to demonstrate that protein complexes are conserved preferentially, compared to transient interactions in the network. (biomedcentral.com)
  • It has similarities to heat shock proteins and clathrin-associated proteins, and may be involved in vesicle structure or trafficking.This gene maps in a region, which include the mixed lineage leukemia and Friend leukemia virus integration 1 genes, where multiple disease-associated chromosome translocations occur. (acris-antibodies.com)
  • Following treatment with forskolin, thapsigargin, or dexamethasone, the CRE binding protein (CREB) was phosphorylated at levels correlating with the level of induced gene expression. (bio5.org)
  • Protein sequence for the given gene in S288C and other strains, when available. (yeastgenome.org)
  • Antigen standard for coatomer protein complex, subunit beta 2 (beta prime) (COPB2), transcript variant 1 is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. (creativebiomart.net)
  • CAPN8 (Calpain 8) is a Protein Coding gene. (genecards.org)
  • Tumor-specific silencing of COPZ2 gene encoding coatomer protein complex subunit ζ 2 renders tumor cells dependent on its paralogous gene COPZ1. (evrogen.com)
  • The protein product of the GOLGA3 gene was designated golgin-160 based on its 160kDa molecular mass in mammalian cell extracts. (acris-antibodies.com)
  • Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. (sciencemag.org)
  • Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. (embopress.org)
  • The biochemical basis for recognition of dilysine motifs by coatomer has been controversial, but one path of research has led in recent years to a clear delineation of the dilysine motif‐binding sites. (embopress.org)
  • A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. (wikipedia.org)
  • GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. (wikipedia.org)
  • Using a dual track SILAC-based quantitative interaction proteomics approach, we established a comprehensive network of stable as well as transient interactions of the peroxin Pex30p, an integral membrane protein. (mcponline.org)
  • The preferential conservation of proteins with higher degree leads to enrichment in protein complexes when interactions are transferred between organisms using interologs. (biomedcentral.com)
  • The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (bio-rad.com)
  • Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. (genecards.org)
  • This domain is predicted to mediatediverse protein-protein interactions. (embl.de)
  • Taken together, our data indicate that Pex30p-containing protein complexes act as focal points from which peroxisomes can form and that the tubular ER architecture organized by the reticulon homology proteins Rtn1p, Rtn2p and Yop1p controls this process. (mcponline.org)
  • Transport from one compartment of this pathway to another is mediated by vesicular carriers, which are formed by the controlled assembly of coat protein complexes (COPs) on donor organelles. (mdpi.com)
  • Transcription of miRNA-encoding genes is catalyzed by RNA polymerase II, and the transcripts are spliced into mature miRNA via dicer-like enzymes and several protein complexes ( Bartel, 2004 ). (frontiersin.org)
  • The p24 proteins form hetero-oligomeric complexes and are believed tofunction as receptors for specific secretory cargo. (embl.de)
  • Schopp, I.M. and Béthune, J. (2018) Split-BioID - Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment. (haw-hamburg.de)
  • Analyzing context-specific protein complexes. (haw-hamburg.de)
  • Two sorting signals are tyrosine-based and dileucine-based signals that interact with heterotetrameric adaptor protein complexes (AP-1, AP-2, AP-3, and AP-4), which are associated with the vesicle coats. (fishersci.com)
  • These PEX genes code for proteins, called peroxins, which are involved in peroxisome assembly and maintenance ( 5 ). (mcponline.org)
  • includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain. (yeastgenome.org)
  • In summary, our findings suggest that drought stress may enhance storage protein by regulating the expression of miRNAs and their target genes. (frontiersin.org)
  • Lonza's Clonetics® HUVEC-Human Umbilical Vein Endothelial Cells were transfected with Thermo Scientific Dharmacon siGENOME® siRNA Libraries targeting protein kinases and cell cycle related genes and screened for genes important for cell viability. (alliedacademies.org)
  • The screen targeted protein kinases and genes associated with the cell cycle to identify target genes important for cell viability. (alliedacademies.org)
  • The siRNA reagents used were Dharmacon Human siGENOME® SMARTpool® siRNA Libraries for Protein Kinases (targeting 779 genes) and Cell Cycle Regulation (targeting 111 genes) (Thermo Fisher Scientific). (alliedacademies.org)
  • Here we report the discovery of an enzyme in a Golgi-enriched fraction that catalyses guanine nucleotide (GDP-GTP) exchange on ARF-1 protein, and which is inhibited by brefeldin A. We suggest that activation of ARF proteins for membrane localization by compartmentalized exchange enzymes is in general the first committed step in membrane transformation pathways. (nih.gov)
  • Dominant-negative mutations in NtRab2 proteins inhibited their Golgi localization, blocked the delivery of Golgi-resident as well as plasmalemma and secreted proteins to their normal locations, and inhibited pollen tube growth. (plantcell.org)
  • Schwann cell-specific BIG1 conditional knockout mice, which have been generated here, exhibit reduced myelin thickness and decreased localization of myelin protein zero in the myelin membrane, compared with their littermate controls. (sciencemag.org)
  • Activation of the GTPase also reverses the interaction between Sar1 and the Sec23-Sec24 protein dimer. (wikipedia.org)
  • Dopamine receptor D3 regulates endocytic sorting by a Prazosin-sensitive interaction with the coatomer COPI. (harvard.edu)
  • Protein-protein interaction (PPI) networks have been transferred between organisms using interologs, allowing model organisms to supplement the interactomes of higher eukaryotes. (biomedcentral.com)
  • GTPases are inactivated through either the intrinsic capability of the GTPase to hydrolyze GTP to GDP+Pi or an interaction with another protein group, the GTPase-activating proteins (GAPs). (mdpi.com)
  • Ribosomal protein P2 alpha, a component of the ribosomal stalk, which is involved in the interaction. (yeastrc.org)
  • The GOLD domain can also be found associated with a RUN domain, which may have a role in the interaction of various proteins with cytoskeletal filaments. (embl.de)
  • Reduced Aβ production was not attributable to altered β-amyloid precursor protein (APP) ectodomain shedding but was a result of an enhanced degradation of APP C-terminal fragments (CTFs) in the absence of PAFAH1B2 but not its close homolog PAFAH1B3. (jneurosci.org)
  • In the course of HCV protein production, there is disruption of the Golgi apparatus, loss of spatial organization of the ER, appearance of some "virus-like" structures and swelling of mitochondria. (biomedcentral.com)
  • This FocusOn presents an antibody panel to proteins specific for the Golgi apparatus. (acris-antibodies.com)
  • We suggest that ArfGAP2 and ArfGAP3 are coat protein-dependent ArfGAPs, whereas ArfGAP1 has a more general function. (rupress.org)
  • The coatomer complex, also known as the coat protein complex 1, forms in the cytoplasm and is recruited to the Golgi by activated guanosine triphosphatases. (genetex.com)
  • Coat Protein Complex I" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Coat Protein Complex I" by people in Harvard Catalyst Profiles by year, and whether "Coat Protein Complex I" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Coat Protein Complex I" by people in Profiles. (harvard.edu)
  • Guanine-nucleotide exchange factors (GEFs), GDP dissociation inhibitors (GDIs), and GTPase-activating proteins are regulators of small GTP-binding proteins ( Figure 1 ). (mdpi.com)
  • Because they can be purified and added exogenously to cells, retrograde transport of toxin proteins is initially unidirectional, in contrast to the recycling behavior of ER residents, KDEL-receptor (KDELR), or p24 proteins, thus allowing observation of retrograde transport in the absence of concurrent anterograde transport. (rupress.org)
  • Luminal ER proteins may be retrieved by means of a C‐terminal KDEL sequence that binds to the KDEL receptor to trigger retrograde transport ( Lewis and Pelham, 1992 ). (embopress.org)
  • Proteolytically cleaves the beta-subunit of coatomer complex (By similarity). (genecards.org)
  • In addition, protein transport and lipid exchange often occur between LDs and various organelles to control lipid homeostasis in response to multiple stress responses and cellular signaling. (frontiersin.org)
  • Beyond fundamental membrane trafficking roles, Arf proteins also regulate mitosis, plasma membrane signaling, cilary trafficking and lipid droplet function. (biologists.org)
  • In this Cell Science at a Glance article and the accompanying poster, we discuss the unique features of Arf small G proteins, their functions in vesicular and lipid trafficking in cells, and how these functions are modulated by their regulators, the GEFs and GAPs. (biologists.org)
  • Plasma membrane domains of polarized cells display distinct protein and lipid compositions. (pubmedcentralcanada.ca)
  • HDL is a class of heterogeneous lipoproteins containing approximately equal amounts of lipid and protein. (ahajournals.org)
  • Other than in the p24 proteins, the GOLDdomain is always found combined with lipid- or membrane-association domains such as the pleckstrin homology (PH), Sec14p and FYVE domains. (embl.de)
  • The antibody recognizes an epitope in the β-COP protein (110 kDa) and stains the periphery of the Golgi complex using immunocytochemical techniques. (genetex.com)
  • 10 μg total protein lysates loaded. (mcponline.org)
  • Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). (creativebiomart.net)
  • While low levels of CFTR mRNA could be identified in the normal human neutrophil, we were unable to detect CFTR protein in human neutrophil lysates or immunoprecipitates. (ersjournals.com)
  • Tight spatial and temporal regulation of the relatively small number of Arf proteins is achieved by their guanine nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs), which catalyze GTP binding and hydrolysis, respectively. (biologists.org)
  • Check out links to articles that cite our custom service antibodies, peptides, and proteins in major peer-reviewed journals, organized by research category. (abgent.com)
  • It is important in the later stages of protein secretion where it seems to play a key role in the sorting and targeting of secreted proteins to the correct destination. (acris-antibodies.com)
  • The GOLD domain, a novel protein module involved in Golgi function and secretion. (embl.de)
  • RESULTS: Using sensitivesequence-profile analysis methods, we identified a novel beta-strand-rich domain,the GOLD (Golgi dynamics) domain, in the p24 proteins and several other proteins with roles in Golgi dynamics and secretion. (embl.de)
  • CONCLUSIONS: Theidentification of the GOLD domain could aid in directed investigation of the roleof the p24 proteins in the secretion process. (embl.de)
  • Inactivation of COPI vesicle formation in conditional sec21 (gamma-COP) mutants rapidly blocks transport of certain proteins along the early secretory pathway. (unibas.ch)
  • We visualized a fluorescent-protein (FP) fusion to Rab6, a Golgi-associated GTPase, in conjunction with fluorescent secretory pathway markers. (rupress.org)
  • We describe a green fluorescent protein (GFP)-based assay for investigating membrane traffic on the secretory pathway in plants. (plantcell.org)
  • These G proteins induce activation of PKA and Src and regulate retrograde and anterograde Golgi trafficking. (hindawi.com)
  • This result suggests that cisternal progression takes place substantially more slowly than most protein transport and therefore is unlikely to be the predominant mechanism of anterograde movement. (rupress.org)
  • Expression of recombinant protein encoded by LOC387715 in Escherichia coli. (biomedsearch.com)
  • With this appreciation, the challenge of understanding the precise molecular mechanisms of these many facets of cell biology has been reduced to a series of problems in protein structure and chemistry. (nih.gov)
  • Inhibiting a molecular process cells use to direct proteins to their proper destinations causes more than 90 percent of affected mosquitoes to die within 48 hours of blood feeding, a UA team of biochemists found. (innovations-report.com)
  • With state-of-the art molecular biology and protein biochemistry labs, we work with our clients to rapidly evaluate in parallel to identify the optimal expression system for candidate proteins. (abgent.com)
  • The domain is present in plant, fungal, and animal proteins, but plant and animal L-type lectins have divergent sequences and different molecular properties. (springer.com)
  • These secretory and endosomal membrane systems intersect at the trans-Golgi network (TGN) and are maintained by recycling pathways ( Saraste and Goud, 2007 ), in which Arf proteins play a major role. (biologists.org)
  • APP695 proteins were constructed also, which carried sorting signals responsible for recycling between the trans -Golgi network (TGN) and the cell surface. (jneurosci.org)
  • The sigma subunit plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. (embl.de)
  • Once Sar1 interacts with the ER membrane, a membrane protein called Sec12 acts a guanine nucleotide exchange factor and substitutes GTP for GDP on Sar1. (wikipedia.org)
  • Furthermore, we show that Rab11 forms a complex with Sec5 and that Sec5 interacts with Sec6 suggesting that the exocyst is a Rab11 effector that facilitates protein transport to the apical rhabdomere in Drosophila PRCs. (pubmedcentralcanada.ca)
  • It interacts with the Golgi integral membrane protein Giantin. (embl.de)
  • Here, pursuing negative- stain electron microscopy coupled with single-particle analyses, and also performing CXMS (chemical cross-linking coupled with mass spectrometry ) for validation, we have reconstructed the structure of coatomer in its soluble form. (bvsalud.org)
  • While plant lectins are secreted-soluble proteins and found at high level in specialised tissues, animal L-type lectins are (often membrane-bound) luminal proteins that are found at low levels in many different cell types. (springer.com)
  • Microinjection of antibodies that block coatomer protein I (COPI) function inhibited trafficking of a KDEL-receptor FP-fusion, but not FP-Rab6. (rupress.org)
  • 58K protein antibodies are excellent for use as markers for the Golgi complex. (acris-antibodies.com)
  • It has similarities to heat shock proteins and clathrin-associated proteins, and may be involved in vesicle structure or trafficking. (acris-antibodies.com)
  • Contains experimentally-derived protein half-life data obtained using stable isotope labeling by amino acids (SILAC) coupled with mass spectrometry. (yeastgenome.org)
  • Recombinant Rhesus monkey COPE full length or partial length protein was expressed. (creativebiomart.net)