BooksBiological 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.Allied Health Occupations: Occupations of medical personnel who are not physicians, and are qualified by special training and, frequently, by licensure to work in supporting roles in the health care field. These occupations include, but are not limited to, medical technology, physical therapy, physician assistant, etc.Library Collection Development: Development of a library collection, including the determination and coordination of selection policy, assessment of needs of users and potential users, collection use studies, collection evaluation, identification of collection needs, selection of materials, planning for resource sharing, collection maintenance and weeding, and budgeting.Textbooks as Topic: Books used in the study of a subject that contain a systematic presentation of the principles and vocabulary of a subject.Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.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)Exocytosis: Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Vesicular Transport Proteins: A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.Transport Vesicles: Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.Organelles: Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.Neurosciences: The scientific disciplines concerned with the embryology, anatomy, physiology, biochemistry, pharmacology, etc., of the nervous system.Angiolymphoid Hyperplasia with Eosinophilia: Solitary or multiple benign cutaneous nodules comprised of immature and mature vascular structures intermingled with endothelial cells and a varied infiltrate of eosinophils, histiocytes, lymphocytes, and mast cells.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)Biomedical Research: Research that involves the application of the natural sciences, especially biology and physiology, to medicine.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Coronary Vessel Anomalies: Malformations of CORONARY VESSELS, either arteries or veins. Included are anomalous origins of coronary arteries; ARTERIOVENOUS FISTULA; CORONARY ANEURYSM; MYOCARDIAL BRIDGING; and others.ADP-Ribosylation Factors: MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47ADP-Ribosylation Factor 1: ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Adenosine Diphosphate Ribose: An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Coatomer Protein: A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.Coated Vesicles: Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.Coat Protein Complex I: A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Receptors, CCR: Chemokine receptors that are specific for CC CHEMOKINES.Chemokine CCL19: A CC-type chemokine with specificity for CCR7 RECEPTORS. It has activity towards T LYMPHOCYTES and B LYMPHOCYTES.Trypanosoma brucei brucei: A hemoflagellate subspecies of parasitic protozoa that causes nagana in domestic and game animals in Africa. It apparently does not infect humans. It is transmitted by bites of tsetse flies (Glossina).Semaphorin-3A: The prototypical and most well-studied member of the semaphorin family. Semaphorin-3A is an axon-repulsive guidance cue for migrating neurons in the developing nervous system. It has so far been found only in vertebrates, and binds to NEUROPILIN-1/plexin complex receptors on growth cones. Like other class 3 semaphorins, it is a secreted protein.Protozoan Proteins: Proteins found in any species of protozoan.PhrasesSubcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Mannose-Binding Lectins: A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE.Oligosaccharides: Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.Endoplasmic Reticulum: 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)Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Caenorhabditis elegans: A species of nematode that is widely used in biological, biochemical, and genetic studies.Genetic Pleiotropy: A phenomenon in which multiple and diverse phenotypic outcomes are influenced by a single gene (or single gene product.)Caenorhabditis elegans Proteins: Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.Estuaries: A partially enclosed body of water, and its surrounding coastal habitats, where saltwater from the ocean mixes with fresh water from rivers or streams. The resulting mixture of seawater and fresh water is called brackish water and its salinity can range from 0.5 to 35 ppt. (accessed http://oceanservice.noaa.gov/education/kits/estuaries/estuaries01_whatis.html)Eye Infections, Parasitic: Mild to severe infections of the eye and its adjacent structures (adnexa) by adult or larval protozoan or metazoan parasites.Ampicillin: Semi-synthetic derivative of penicillin that functions as an orally active broad-spectrum antibiotic.Microalgae: A non-taxonomic term for unicellular microscopic algae which are found in both freshwater and marine environments. Some authors consider DIATOMS; CYANOBACTERIA; HAPTOPHYTA; and DINOFLAGELLATES as part of microalgae, even though they are not algae.

Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. (1/342)

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)

LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. (2/342)

In Saccharomyces cerevisiae, vesicles that carry proteins from the ER to the Golgi compartment are encapsulated by COPII coat proteins. We identified mutations in ten genes, designated LST (lethal with sec-thirteen), that were lethal in combination with the COPII mutation sec13-1. LST1 showed synthetic-lethal interactions with the complete set of COPII genes, indicating that LST1 encodes a new COPII function. LST1 codes for a protein similar in sequence to the COPII subunit Sec24p. Like Sec24p, Lst1p is a peripheral ER membrane protein that binds to the COPII subunit Sec23p. Chromosomal deletion of LST1 is not lethal, but inhibits transport of the plasma membrane proton-ATPase (Pma1p) to the cell surface, causing poor growth on media of low pH. Localization by both immunofluorescence microscopy and cell fractionation shows that the export of Pma1p from the ER is impaired in lst1Delta mutants. Transport of other proteins from the ER was not affected by lst1Delta, nor was Pma1p transport found to be particularly sensitive to other COPII defects. Together, these findings suggest that a specialized form of the COPII coat subunit, with Lst1p in place of Sec24p, is used for the efficient packaging of Pma1p into vesicles derived from the ER.  (+info)

Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat. (3/342)

The regulation of intracellular vesicular trafficking is mediated by specific families of proteins that are involved in vesicular budding, translocation, and fusion with target membranes. We purified a vesicle-associated protein from hepatic microsomes using sequential column chromatography and partially sequenced it. Oliogonucleotides based on these sequences were used to clone the protein from a rat liver cDNA library. The clone encoded a novel protein with a predicted mass of 137 kDa (p137). The protein had an N terminus WD repeat motif with significant homology to Sec31p, a member of the yeast COPII coat that complexes with Sec13p. We found that p137 interacted with mammalian Sec13p using several approaches: co-elution through sequential column chromatography, co-immunoprecipitation from intact cells, and yeast two-hybrid analysis. Morphologically, the p137 protein was localized to small punctate structures in the cytoplasm of multiple cultured cell lines. When Sec13p was transfected into these cells, it demonstrated considerable overlap with p137. This overlap was maintained through several pharmacological manipulations. The p137 compartment also demonstrated partial overlap with ts045-VSVG protein when infected cells were incubated at 15 degrees C. These findings suggest that p137 is the mammalian orthologue of Sec31p.  (+info)

Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. (4/342)

The Sec23p/Sec24p complex functions as a component of the COPII coat in vesicle transport from the endoplasmic reticulum. Here we characterize Saccharomyces cerevisiae SEC24, which encodes a protein of 926 amino acids (YIL109C), and a close homologue, ISS1 (YNL049C), which is 55% identical to SEC24. SEC24 is essential for vesicular transport in vivo because depletion of Sec24p is lethal, causing exaggeration of the endoplasmic reticulum and a block in the maturation of carboxypeptidase Y. Overproduction of Sec24p suppressed the temperature sensitivity of sec23-2, and overproduction of both Sec24p and Sec23p suppressed the temperature sensitivity of sec16-2. SEC24 gene disruption could be complemented by overexpression of ISS1, indicating functional redundancy between the two homologous proteins. Deletion of ISS1 had no significant effect on growth or secretion; however, iss1Delta mutants were found to be synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1. Moreover, overexpression of ISS1 could suppress mutations in SEC22. These genetic interactions suggest that Iss1p may be specialized for the packaging or the function of COPII v-SNAREs. Iss1p tagged with His(6) at its C terminus copurified with Sec23p. Pure Sec23p/Iss1p could replace Sec23p/Sec24p in the packaging of a soluble cargo molecule (alpha-factor) and v-SNAREs (Sec22p and Bet1p) into COPII vesicles. Abundant proteins in the purified vesicles produced with Sec23p/Iss1p were indistinguishable from those in the regular COPII vesicles produced with Sec23p/Sec24p.  (+info)

Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum. (5/342)

The COPII coat is required for vesicle budding from the endoplasmic reticulum (ER), and consists of two heterodimeric subcomplexes, Sec23p/Sec24p, Sec13p/Sec31p, and a small GTPase, Sar1p. We characterized a yeast mutant, anu1 (abnormal nuclear morphology) exhibiting proliferated ER as well as abnormal nuclear morphology at the restrictive temperature. Based on the finding that ANU1 is identical to SEC24, we confirmed a temperature-sensitive protein transport from the ER to the Golgi in anu1-1/sec24-20 cells. Overexpression of SFB2, a SEC24 homologue with 56% identity, partially suppressed not only the mutant phenotype of sec24-20 cells but also rescued the SEC24-disrupted cells. Moreover, the yeast two-hybrid assay revealed that Sfb2p, similarly to Sec24p, interacted with Sec23p. In SEC24-disrupted cells rescued by overexpression of SFB2, some cargo proteins were still retained in the ER, while most of the protein transport was restored. Together, these findings strongly suggest that Sfb2p functions as the component of COPII coats in place of Sec24p, and raise the possibility that each member of the SEC24 family of proteins participates directly and/or indirectly in cargo-recognition events with its own cargo specificity at forming ER-derived vesicles.  (+info)

Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. (6/342)

We find that the peripheral ER in Saccharomyces cerevisiae forms a dynamic network of interconnecting membrane tubules throughout the cell cycle, similar to the ER in higher eukaryotes. Maintenance of this network does not require microtubule or actin filaments, but its dynamic behavior is largely dependent on the actin cytoskeleton. We isolated three conditional mutants that disrupt peripheral ER structure. One has a mutation in a component of the COPI coat complex, which is required for vesicle budding. This mutant has a partial defect in ER segregation into daughter cells and disorganized ER in mother cells. A similar phenotype was found in other mutants with defects in vesicular trafficking between ER and Golgi complex, but not in mutants blocked at later steps in the secretory pathway. The other two mutants found in the screen have defects in the signal recognition particle (SRP) receptor. This receptor, along with SRP, targets ribosome-nascent chain complexes to the ER membrane for protein translocation. A conditional mutation in SRP also disrupts ER structure, but other mutants with translocation defects do not. We also demonstrate that, both in wild-type and mutant cells, the ER and mitochondria partially coalign, and that mutations that disrupt ER structure also affect mitochondrial structure. Our data suggest that both trafficking between the ER and Golgi complex and ribosome targeting are important for maintaining ER structure, and that proper ER structure may be required to maintain mitochondrial structure.  (+info)

Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. (7/342)

The events regulating coat complex II (COPII) vesicle formation involved in the export of cargo from the endoplasmic reticulum (ER) are unknown. COPII recruitment to membranes is initiated by the activation of the small GTPase Sar1. We have utilized purified COPII components in both membrane recruitment and cargo export assays to analyze the possible role of kinase regulation in ER export. We now demonstrate that Sar1 recruitment to membranes requires ATP. We find that the serine/threonine kinase inhibitor H89 abolishes membrane recruitment of Sar1, thereby preventing COPII polymerization by interfering with the recruitment of the cytosolic Sec23/24 COPII coat complex. Inhibition of COPII recruitment prevents export of cargo from the ER. These results demonstrate that ER export and initiation of COPII vesicle formation in mammalian cells is under kinase regulation.  (+info)

The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase. (8/342)

We have studied the structural and functional properties of the pre-Golgi intermediate compartment (IC) in normal rat kidney cells using analytical cell fractionation with p58 as the principal marker. The sedimentation profile (sediterm) of p58, obtained by analytical differential centrifugation, revealed in steady-state cells the presence of two main populations of IC elements whose average sedimentation coefficients, s(H)=1150+/-58S ('heavy') and s(L)=158+/-8S ('light'), differed from the s-values obtained for elements of the rough and smooth endoplasmic reticulum. High resolution analysis of these subpopulations in equilibrium density gradients further revealed that the large difference in their s-values was mainly due to particle size. The 'light' particle population contained the bulk of COPI and COPII coats, and redistribution of p58 to these particles was observed in transport-arrested cells, showing that the two types of elements are also compositionally distinct and have functional counterparts in intact cells. Using a specific antibody against the 16 kDa proteolipid subunit of the vacuolar H(+)-ATPase, an enrichment of the V(o )domain of the ATPase was observed in the p58-positive IC elements. Interestingly, these elements could contain both COPI and COPII coats and their density distribution was markedly affected by GTP(&ggr;)S. Together with morphological observations, these results demonstrate that, in addition to clusters of small tubules and vesicles, the IC also consists of large-sized structures and corroborate the proposal that the IC elements contain an active vacuolar H(+)-ATPase.  (+info)

*COPI

"ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein ... Sönnichsen B, Watson R, Clausen H, Misteli T, Warren G (1996). "Sorting by COP I-coated vesicles under interphase and mitotic ... COPII vesicles Clathrin vesicles Glyceraldehyde 3-phosphate dehydrogenase#ER to Golgi transport Exomer Coat Protein Complex I ... A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly". Science. 349 (6244): 195-198. doi: ...

*ARF1

1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ... "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 ...

*B2-adapt-app C

McMahon HT, Mills IG (August 2004). "COP and clathrin-coated vesicle budding: different pathways, common approaches". Curr. ... AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins ( ... This is an adaptor protein which helps the formation of a clathrin coat around a vesicle. This entry represents a subdomain of ...

*Clathrin adaptor protein

"COP and clathrin-coated vesicle budding: different pathways, common approaches". Curr. Opin. Cell Biol. 16 (4): 379-91. doi: ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated ... lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly ...

*SAR1B

... which govern the intracellular trafficking of proteins in coat protein (COP)-coated vesicles. Mutations in the SAR1B gene are ... Schekman R, Orci L (March 1996). "Coat proteins and vesicle budding". Science. 271 (5255): 1526-33. doi:10.1126/science. ... "Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders". Nature Genetics. 34 (1): 29-31. ... "Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders". Nature Genetics. 34 (1): 29-31. ...

*COPB1

1991). "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta- ... "Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ...

*Brefeldin A

Activated Arf1p then recruits coat protein β-COP, a subunit of the COP-I complex, to cargo-bound receptors on the membrane. ... of SNARE proteins in the Golgi which would otherwise be bound to coat protein-coated vesicles and removed with the vesicles ... Coat protein recruitment is necessary for proper vesicle formation and transport. Brefeldin A reversibly inhibits the function ... protein transport from the endoplasmic reticulum to the Golgi apparatus indirectly by preventing association of COP-I coat to ...

*Endocytosis

Coat complexes that have been well characterized so far include coat protein-I (COP-I), COP-II, and clathrin. Clathrin coats ... vesicles that have a morphologically characteristic coat made up of the cytosolic protein clathrin. Clathrin-coated vesicles ( ... Coats function to deform the donor membrane to produce a vesicle, and they also function in the selection of the vesicle cargo ... Coated vesicles were first purified by Barbara Pearse, who discovered the clathrin coat molecule in 1976. Active transport ...

*List of MeSH codes (A11)

... clathrin-coated vesicles MeSH A11.284.430.214.190.875.190.880.180.180 - cop-coated vesicles MeSH A11.284.430.214.190.875. ... transport vesicles MeSH A11.284.430.214.190.875.190.880.180 - coated vesicles MeSH A11.284.430.214.190.875.190.880.180.160 - ... 190.880.810 - secretory vesicles MeSH A11.284.430.214.190.875.190.880.830 - synaptic vesicles MeSH A11.284.430.214.190.875. ... coated pits, cell-membrane MeSH A11.284.149.165.175.160 - caveolae MeSH A11.284.149.165.355 - glycocalyx MeSH A11.284.149.165. ...

*Vesicular transport protein

COP 1 (Cytosolic coat protein complex ) : retrograde transport ; Golgi ----> Endoplasmic reticulum COP 2 (Cytosolic coat ... As a result, vesicular transporters govern the concentration of molecules within a vesicle. Examples include: Archain ARFs ... is a membrane protein that regulates or facilitates the movement of specific molecules across a vesicle's membrane. ... each using its own coat and GTPase. ...

*SURF4

... transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat ... proteins (COPs). The specific function of this protein has not been determined but its yeast homolog is directly required for ... packaging glycosylated pro-alpha-factor into COPII vesicles. This gene uses multiple polyadenylation sites, resulting in ...

*COP1

For the membrane coated vesicle used in transport, see here. Fagol Caspase recruitment domain-containing protein 16 is an ... 2006). "Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell death". Biochim. Biophys. Acta. 1762 (8): 742-54 ... "Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing". J Biol Chem. 276 (37): ...

*COPG2

Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles". Nature. 349 (6306): 248-51. ... Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C ... Yamasaki K, Hayashida S, Miura K, Masuzaki H, Ishimaru T, Niikawa N, Kishino T (Nov 2000). "The novel gene, gamma2-COP (COPG2 ...

*COPE (gene)

Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Eugster A, Frigerio G, Dale M, Duden R (2000). "COP I domains required for coatomer integrity, and novel interactions with ARF ... is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ...

*COPG

It is one of seven proteins in the COPI coatomer complex that coats vesicles as they bud from the Golgi complex. COPG has been ... Lowe, M; Kreis T E (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. UNITED STATES. 271 ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... 2000). "Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution". FEBS Lett ...

*COPA (gene)

Chow VT, Quek HH (1997). "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP ... Lowe M, Kreis TE (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. ...

*COPB2

The Golgi coatomer complex (see MIM 601924) constitutes the coat of nonclathrin-coated vesicles and is essential for Golgi ... Lowe M, Kreis TE (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... Stenbeck G, Harter C, Brecht A, Herrmann D, Lottspeich F, Orci L, Wieland FT (1993). "beta'-COP, a novel subunit of coatomer". ...

*Alpha solenoid

Vesicle coat proteins frequently contain alpha solenoids and share common domain architecture with some NPC proteins. Three ... Field, Mark C.; Sali, Andrej; Rout, Michael P. (13 June 2011). "On a bender-BARs, ESCRTs, COPs, and finally getting your coat ... vesicle coat proteins, and nuclear pore complexes". Current Opinion in Cell Biology. 21 (1): 4-13. doi:10.1016/j.ceb.2008.12. ... "Components of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture". PLoS Biology. 2 (12): e380. ...

*Vesicular transport adaptor protein

The best characterized type of vesicle is the clathrin coated vesicle (CCV). The formation of a COPII vesicle at the ... Components of COPI (cop one) a coatomer, and TSET (T-set) a membrane trafficking complex have similar heterotetramers of the AP ... but the coat of COPI is not closely related to the coats of either CCVs or COPII vesicles. AP-5 is associated with 2 proteins, ... but the ultrastructure of that coat is not known. The coat of AP-4 is unknown. An almost universal feature of coat assembly is ...

*Golgi apparatus

Cargo then progress toward the trans face in COPI-coated vesicles. This model proposes that COPI vesicles move in two ... ARFs are small GTPases which regulate vesicular trafficking through the binding of COPs to endosomes and the Golgi. BFA ... Proteins are delivered from the ER to the cis face using COPII-coated vesicles. ... Once matured, the TGN cisternae dissolves to become secretory vesicles. While this progression occurs, COPI vesicles ...
Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum (PubMed:27138255 ...
In this study, we showed that Sec12 recruitment to ER exit sites by interactions with cTAGE5 is necessary for collagen transport from the ER. As the interaction between cTAGE5 and Sec12 did not alter the activity of Sec12 toward Sar1, cTAGE5-mediated Sec12 concentration may be important for the localized activation of Sar1 in the vicinity of the ER exit sites. In this regard, it has been reported that Sedlin is somehow involved in the inactivation of Sar1 through interaction with TANGO1 at ER exit sites and is specifically required for collagen secretion (Venditti et al., 2012). Thus, it is interesting to speculate that the exit of collagen from the ER may rely on specific activation-inactivation mechanisms-Sar1 might first be activated by the cTAGE5-Sec12 complex and then inactivated by TANGO1-Sedlin. In this case, tight regulation of the Sar1 GTPase cycle at ER exit sites would be important for collagen secretion from the ER, although we cannot totally rule out the possibility that ...
Marian Blanca Ramírez from the CSIC in Spain has been studying the effects of LRRK2, a protein associated with Parkinsons disease, on cell motility. A Travelling Fellowship from Journal of Cell Science allowed her to spend time in Prof Maddy Parsons lab at Kings College London, learning new cell migration assays and analysing fibroblasts cultured from individuals with Parkinsons. Read more on her story here. Where could your research take you? The deadline to apply for the current round of Travelling Fellowships is 23rd Feburary 2018. Apply now!. ...
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
On page 1029, Supek et al. illustrate how a peripheral membrane protein organizes a coat protein complex involved in secretory vesicle formation.. The protein in question, yeast Sec16p, is an ER resident required in vivo for COPII-dependent vesicle budding. In vitro, Sec16p is not necessary for budding from liposomes reconstituted with pure cytosolic COPII proteins. However, this in vitro reaction depends on a nonhydrolyzable form of GTP, probably because the COPII coat falls apart when Sar1p (the initiator of coat assembly) hydrolyzes GTP. Until now, the function of Sec16p in liposome budding could not be tested, because the protein was difficult to purify. Supek et al. report conditions that stabilize Sec16p and have purified enough protein for in vitro studies. Microsomal membranes stripped of endogenous Sec16p were stimulated in vesicle budding by the purified. protein, but only in the presence of hydrolyzable GTP. Thus, the in vivo function of Sec16p may be either to slow GTP hydrolysis ...
CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Abstract. COPII-coated ER-derived transport vesicles from Saccharomyces cerevisiae contain a distinct set of membrane-bound polypeptides. One of these polypeptides, termed Erv14p (ER-vesicle protein of 14 kD), corresponds to an open reading frame on yeast chromosome VII that is predicted to encode an integral membrane protein and shares sequence identity with the Drosophila cornichon gene product. Experiments with an epitope-tagged version of Erv14p indicate that this protein localizes to the ER and is selectively packaged into COPII-coated vesicles. Haploid cells that lack Erv14p are viable but display a modest defect in bud site selection because a transmembrane secretory protein, Axl2p, is not efficiently delivered to the cell surface. Axl2p is required for selection of axial growth
Pandey A, Fernandez MM, Steen H, Blagoev B, Nielsen MM, Roche S, Mann M, Lodish HF. Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways. J Biol Chem 2000;275:38633-38639 ...
Structural Component Of 3 Distinct Complexes; Subunit Of Nup84 Nuclear Pore Sub-complex (NPC), COPII Vesicle Coat, And Seh1-associated (SEA) Complex; COPII Vesicle Coat Is Required For ER To Golgi Transport; The Nup84 Subcomplex Contributes To Nucleocytoplasmic Transport, NPC Biogenesis And Processes That May Require Localization Of Chromosomes At The Nuclear Periphery, Including Transcription; Homologous To Human SEC13; Abundance Increases Under DNA Replication Stress
Member Of The P24 Family Involved In ER To Golgi Transport; Similar To Emp24p And Erv25p; Role In Misfolded Protein Quality Control; Forms A Heterotrimeric Complex With Erp1p, Emp24p, And Erv25p; Localized To COPII-coated Vesicles; ERP2 Has A Paralog, ERP4, That Arose From The Whole Genome Duplication
Synonyms for E (exit) site in Free Thesaurus. Antonyms for E (exit) site. 3 words related to ribosome: cell organ, cell organelle, organelle. What are synonyms for E (exit) site?
Precise inheritance of organelles during mitosis ensures the proper organisation and function of daughter cells. Inheritance of the Golgi complex, a single copy organelle, requires its disassembly before mitosis; Golgi disassembly is driven by mitotic inhibition of COPII-dependent export of proteins from endoplasmic reticulum exit sites (ERESs) to the Golgi. Helen Hughes and David Stephens have been investigating how ERESs are restored at the end of mitosis and, on page 4032, they report that Sec16A - the major human orthologue of Sec16, which defines the site of COPII vesicle budding in yeast - defines the site at which COPII-dependent budding reinitiates after mitosis. Using quantitative 4D imaging of HeLa cells stably expressing fluorescently labelled Sec16A, the authors show that, unlike all other COPII components, Sec16A remains associated with ERESs throughout mitosis. Moreover, Sec16A localisation is coincident with the reappearance of COPII puncta on mitotic exit. Hughes and Stephens ...
Exit sites (ES) are specialized domains of the endoplasmic reticulum (ER) at which cargo proteins of the secretory pathway are packaged into COPII-coated vesicles. Although the essential COPII proteins (Sar1p, Sec23p-Sec24p, Sec13p-Sec31p) have been characterized in detail and their sequential binding kinetics at ER membranes have been quantified, the basic processes that govern the self-assembly and spatial organization of ERES have remained elusive. Here, we have formulated a generic computational model that describes the process of formation of ERES on a mesoscopic scale. The model predicts that ERES are arranged in a quasi-crystalline pattern, while their size strongly depends on the cargo-modulated kinetics of COPII turnover - that is, a lack of cargo leads to smaller and more mobile ERES. These predictions are in favorable agreement with experimental data obtained by fluorescence microscopy. The model further suggests that cooperative binding of COPII components, for example mediated by regulatory
Peng, R.; Grabowski, R.; De Antoni, A.; Gallwitz, D.: Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proceedings of the National Academy of Sciences USA 96, pp. 3751 - 3756 (1999 ...
The nucleus is one of the defining features of eukaryotes and the question of its origin is intimately linked to the evolution of the eukaryotic cell. It is delimited by a double lipid bilayer called the nuclear envelope, which separates the nuclear interior from the cytoplasm. The inner and outer membranes of the nucleus are continuous with one another creating a single folded envelope, interrupted by nuclear pore complexes (NPCs), which enable transport of proteins and RNA between nucleoplasm and cytoplasm.. A combination of proteomic and bioinformatic analyses has shown that numerous Nups are conserved between yeast and vertebrates. As this only describes a subset of eukaryotic diversity, comparative genomic analyses were used to establish the extent to which the NPC is conserved across the eukaryotic tree. NPCs have been suggested to share a common origin with vesicle coat proteins of the endomembrane system. An additional goal of this work was therefore to establish the distribution of ...
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
The protein encoded by this gene is reported to be a component of the Golgi matrix. It may act as a golgin protein by negatively regulating transit of secretory cargo and by acting as a structural scaffold of the Golgi. Alternative splicing results in multiple transcript variants ...
Transport vesicles form at a donor compartment and fuse to an acceptor compartment mediate the movement of cargo proteins within eukaryotic cells from one subcellular compartment to another. COPII vesicles specifically provide the means of transport for proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The in vitro enrichment of COPII vesicles was undertaken with the intent of better understanding COPII dependent transport between the ER and Golgi. This approach allowed for the identification of abundant vesicle proteins, one of which is Erv14p, an ER-vesicle protein of 14 kDa. Erv14p is an integral membrane protein that localized to the ER and Golgi and was responsible for the efficient transport of at least one secretory cargo protein, Ax12p. Erv14p was not essential. However, genetic analysis of ERV14 deletion strains carrying thermosensitive alleles encoding for COPII components and other proteins known to participate in ER to Golgi vesicle trafficking revealed a variety ...
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.
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Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
We explain Golgi Body with video tutorials and quizzes, using our Many Ways(TM) approach from multiple teachers.This lesson will discuss the structure and function of the golgi body.
Golgi Dynamics. How can it happen that the resident proteins appear to remain in place while the transient proteins, destined for other sites in the cell, move through the organelle in a cis to trans direction?. Over the years a number of ideas have been put forth they fall into two general models.. 1. Vesicle Transport Model. This model assumes that the cisternae are essentially stationary and contain their resident proteins. The transient proteins are selected and concentrated in vesicles by the process of vesicle formation that is driven by coat proteins and their interaction with cargo receptor proteins as described in the last lecture. See vesicle formation animation for review of how this works.. These transport vesicles bud from the periphery of the Golgi cisterna as shown in the picture above, and then fuse with the appropriate target cisterna (trans to the point of origin) via the normal vesicle targeting process. In this manner a transient protein makes is way down the Golgi stack, cis ...
Intracellular transport between the ER and Golgi is mediated by vesicles that bud from donor membranes and then fuse with acceptor membranes. Bi-directional vesicle transport maintains distinct organelle composition through a process known as molecular sorting. Collectively, molecular sorting refers to the process of actively selecting or excluding proteins and lipids into transport vesicles. Some of the proteins involved in sorting have been identified although the mechanisms remain obscure. This dissertation examines proteins contained on ER-derived vesicles (Ervs) and how these proteins facilitate sorting. Erv function requires bi-directional ER to Golgi transport therefore it was determined how the cytoplamic tail sequences of Emp24p and Erv25p function in transport. Both Emp24p and Erv25p tail sequences are sufficient to direct anterograde transport and interact with COPII subunits, however the Erv25p tail is necessary to direct retrograde transport. A vexing question regarding p24 function ...
Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (By similarity). Involved in ER-Golgi transport (PubMed:27276012). Regulates ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (By similarity). Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12)
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 chief function of Golgi body is secretion from a cell of protein materials, such as enzymes, hormones etc., that are not easily diffusible through the cell membrane. After being synthesized in the rough endoplasmic reticulum, the secretory proteins pass into the cisternae of Golgi body through the tubules of ER and Golgi body, and are stored in the Golgi vacuoles. From the vacuoles the secretory materials are released in the cytoplasm in the form of membrane bound tiny vesicels. These vesicles then pass towards the border of the cell and fuse with the cell membrane in such a manner that the secretory materials are expelled out of the cell keeping the cell membrane unbroken. By the same mechanism the Golgi body also helps in the release of neurotransmitters and neuro-hormones from nerve cells.. ...
Résumé : ORP2 is a ubiquitously expressed OSBP-related protein previously implicated in triacylglycerol (TG) metabolism at endoplasmic reticulum (ER) - lipid droplet (LD) contacts, cholesterol transport, and adrenocortical steroidogenesis. We now characterize the functional role of ORP2 by employing ORP2-knock-out (KO) hepatoma cells generated by CRISPR-Cas9 gene editing. Loss of ORP2 did not affect the major cellular phospholipids, cholesterol, or oxysterols, nor the quantity of ER-LD contact sites. However, the knock-out resulted in reduced expression of SREBP-1 target genes and mRNAs encoding glycolytic enzymes, defective TG synthesis and storage, inhibition of LD growth upon fatty acid loading, reduction of glucose uptake, glycogen synthesis, glycolysis (ECAR) and Akt activity. ORP2 was found to form a physical complex with key controllers of Akt, Cdc37 and Hsp90. In addition to the metabolic phenotypes, the ORP2-KO cells showed defects in adhesion, lamellipodieae formation, migration and ...
The Golgi body (or Golgi complex, apparatus), and Endoplasmic reticulum (ER) are both organelles found in the majority of eukaryotic cells. They are very closely associated and show both similarities and differences in structure and function.
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In this work, we identify a C. elegans protein, TMEM-131, which has homologs in most animals, with essential roles in collagen secretion. These roles appear evolutionarily conserved for Drosophila and human TMEM131 homologs. We propose that TMEM131 proteins recruit premature collagen monomers through N-terminal PapD-L domains, whereas its C-terminal TRAPIDs bind to TRAPPC8, which promotes collagen secretion as a key component of TRAPP complex during the ER-to-Golgi transport of COPII vesicles (Fig. 7F). Although we did not recognize any apparent homologous C-propeptide protein sequence in C. elegans COL-19 or COL-101, their normal secretion still requires TMEM-131 as Drosophila, or human collagen I secretion requires TMEM131 homologs. Despite the lack of obvious sequence similarity between the C. elegans cuticle collagens and the COLFI domain of mammalian fibrillar collagens, TMEM131 family proteins appear to have evolved similar functions among different species. As COL-19::GFP secretion also ...
Sec24-like transport protein; Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII is composed of at least five proteins- the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex (By similarity) (1038 aa ...
Membrane, Proteins, Endoplasmic Reticulum, Reticulum, Secretory Pathway, Yeast, Gtpase, Coated Vesicles, Copi, Copi-coated Vesicles, and Clathrin
The world of fusion energy is a world of extremes. For instance, the center of the ultrahot plasma contained within the walls of doughnut-shaped fusion machines known as tokamaks can reach temperatures well above the 15 million degrees Celsius core of the sun. And even though the portion of the plasma closer to the tokamaks inner walls is 10 to 20 times cooler, it still has enough energy to erode the layer of liquid lithium that may be used to coat components that face the plasma in future tokamaks. ...
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The protein encoded by this gene is a member of the SEC22 family of vesicle trafficking proteins. It seems to complex with SNARE and it is thought to play a role in the ER-Golgi protein trafficking. This protein has strong similarity to Mus musculus and Cricetulus griseus proteins.[provided by RefSeq, Sep 2009 ...
Well test have begun on my neice to try and find out why she had a stroke, she had been having headaches since july, had ct at er and shots but to no avail she was sent for mri and was called she had,had a stroke,recently to pin point when doc told her it was in a area that would affect her vision she remembered 2 days before mri she couldnt see out off her left eye when she got up that morning, but returned she wss feeling weak even before stroke and had numness in few fingers and toes but
Moreover, there are some collagen molecules containing sequences of hydrophobic amino acids inserted in the plasma membrane. For example, type XIII and XVII collagens. Collagen type XVII is part of the molecular structure of hemidesmosomes. No matter the type, collagen is synthesized inside the cell as a precursor: the pro-collagen molecule. First, alpha chains are synthesized in the endoplasmic reticulum, where proline becomes hydroxyproline by hydroxylation. Proline and hydroxyproline may be up to 20 % of the alpha chain. GLycosylation (type O-glycosylation) of alpha chains also occurs in the reticulum. At this point, three alpha chains join together by hydrogen bonds to finally form the pro-collagen molecule. Disulfide bridges are also formed between the alpha chains. Pro-collagen molecules are recognized and linked by transmembrane receptors and packaged in COPII coated vesicles. Typical COPII vesicles are 60 to 90 nm in diameter, but COPII vesicles transporting pro-collagen are 500 nm in ...
4 See WIPO 2006a, Introduction Section. 5 Paris Convention for the Protection of Industrial Property (Paris, 20 March 1883), as revised at Stockholm, 14 July 1967, and amended 28 September 1979, 828 U.N.T.S. 303 (entered into force 7 July 1884) [hereinafter Paris Convention], available at: http://www.wipo.int/export/sites/www/treaties/en/ip/paris/pdf/trtdocs_wo020.pdf (accessed 3 February 2010). 6 Berne Convention for the Protection of Literary and Artistic Works (Berne, 9 September 1886), as revised at Paris, 24 July 1971, and amended 28 September 1979, 1161 U.N.T.S. 30 (The Act of Paris entered into force 15 December 1972) [hereinafter Berne Convention], available at: http://www.wipo.int/treaties/en/ip/berne/trtdocs_wo001.html (accessed 3 February 2010). 7 WIPO 2001, para. 65. The Secretariat suggests that the more important definitional and conceptual issues have to do with the substantive and procedural standards affecting the availability, acquisition, scope, maintenance and enforcement ...
Efficient and accurate protein secretion is a fundamental process that plays a pivotal role in the ability of al eukaryotic cells to function, grw and communica...
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…
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Cellular processesCellular processesSporulation and germinationspore coat assembly protein SafA (TIGR02899; HMM-score: 63.9) ...
(There is also W eakness E or вexitв site, which binds the tRNAs that have been used during translation before they are ejected from the ribosome. HERBICIDES h.
article{1864472, abstract = {Endocytosis is a crucial mechanism by which eukaryotic cells internalize extracellular and plasma membrane material, and it is required for a multitude of cellular and developmental processes in unicellular and multicellular organisms. In animals and yeast, the best characterized pathway for endocytosis depends on the function of the vesicle coat protein clathrin. Clathrin-mediated endocytosis has recently been demonstrated also in plant cells, but its physiological and developmental roles remain unclear. Here, we assessed the roles of the clathrin-mediated mechanism of endocytosis in plants by genetic means. We interfered with clathrin heavy chain (CHC) function through mutants and dominant-negative approaches in Arabidopsis thaliana and established tools to manipulate clathrin function in a cell type-specific manner. The chc2 single mutants and dominant-negative CHC1 (HUB) transgenic lines were defective in bulk endocytosis as well as in internalization of ...
Author(s): Katsura, Kaitlin A | Advisor(s): Den Besten, Pamela | Abstract: Amelogenesis Imperfecta (AI) is a clinical diagnosis that encompasses a group of genetic mutations, each affecting processes involved in tooth enamel formation and thus, result in various enamel defects. The hypomaturation enamel phenotype has been described for mutations involved in the later stage of enamel formation, including Klk4, Mmp20, C4orf26, and Wdr72. Using a candidate gene approach we discovered a novel Wdr72 human mutation, resulting in a hypomaturation AI phenotype, to be a 5-base pair deletion (c.806_810delGGCAG; p.G255VfsX294). To gain insight into the function of WDR72, we used computer modeling of the full-length human WDR72 protein structure and found that the predicted N-terminal sequence forms two beta-propeller folds with an alpha-solenoid tail at the C-terminus. This domain iteration is characteristic of vesicle coat proteins, such as beta′-COP, suggesting a role for WDR72 in the formation of membrane
A case-control study of 1103 Chilean maternal-fetal dyads and 1637 unpaired African American samples (836 maternal, 837 fetal) concluded that the fetal minor allele rs2549782(G) was associated with 1.3x increased risk (CI: 1.075-1.619) for pre-eclampsia in the African American population (p = 0.009), but not in the Chilean population. }} [PMID 20843824] Genetic diversity at endoplasmic reticulum aminopeptidases is maintained by balancing selection and is associated with natural resistance to HIV-1 infection. [PMID 20595269] Serum cytokine receptors in ankylosing spondylitis: relationship to inflammatory markers and endoplasmic reticulum aminopeptidase polymorphisms. [PMID 19578876 ...
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 ...
Read "The molecular characterization of transport vesicles, Plant Molecular Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Complete information for CTAGE5 gene (Protein Coding), CTAGE Family Member 5, ER Export Factor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
also called the Golgi apparatus or golgi complex) a flattened, layered, sac-like organelle that looks like a stack of pancakes and is located near the nucleus. It produces the membranes that surround the lysosomes. The Golgi body packages proteins a ...
KCNH2 encodes the Kv11.1 α-subunit that underlies the rapidly activating delayed-rectifier K+ current in the heart. Loss-of-function KCNH2 mutations cause long QT syndrome type 2 (LQT2), and most LQT2-linked missense mutations inhibit the trafficking of Kv11.1 channel protein to the cell surface membrane. Several trafficking-deficient LQT2 mutations (e.g., G601S) generate Kv11.1 proteins that are sequestered in a microtubule-dependent quality control (QC) compartment in the transitional endoplasmic reticulum (ER). We tested the hypothesis that the QC mechanisms that regulate LQT2-linked Kv11.1 protein trafficking are mutation-specific. Confocal imaging analyses of HEK293 cells stably expressing the trafficking-deficient LQT2 mutation F805C showed that, unlike G601S-Kv11.1 protein, F805C-Kv11.1 protein was concentrated in several transitional ER subcompartments. The microtubule depolymerizing drug nocodazole differentially affected G601S- and F805C-Kv11.1 protein immunostaining. Nocodazole caused G601S
The Golgi body, or Golgi apparatus is a collection of flattened membrane sacks called cisternae that carry out the processing,packaging, and sorting of a variety of cellular products in higher plants and animals.This important cellular organelle was named in honor of Camillo Golgi ,the Italian neuroanatomist who first described it in brain cells.
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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Searchable collection of scientific articles, peer-reviewed journals and publications from the PTR-MS Community. Sophisticated search and filters tools allow to look for articles, titles, keywords, authors or year. Acccess abstracts and follow DOI-links!
Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (Probable). ...
ARF GAP Lis a kind of important regulator of introcellular transport. Recently, a novel human gene has been found from a cDNA library of second trimester human fetal liver. The amino acid sequence encoded by the novel gene has 32% similarity to rat ARF1 GAP, was thus termed as ARFGAP3. Functional studies of the new gene were performed. The full-length cDNA of ARFGAP3 was amplified from the human total placenta RNA by RT-PCR technique, then subcloned into pGEM-T vector and sequenced. The RNA Master blot and multiple tissue Northern blot analysis were used to define the expression profile and the transcript size of ARFGAP3 in human tissues. It was shown that ARFGAP3 was strongly expressed in glands and testis and that ARFGAP3 mRNA existed as only one kind of transcript of 2.7 kb in various human tissues. Then, the expression and purification of the recombinant human ARFGAP3 (rhARFGAP3) were performed. It was demonstrated that rhARFGAP3 exhibited strong GTPase-activating protein ( GAP) activity ...
... , a) Golgi body: It is also known as lipochondria or dictyosome. It arises from ER and is formed by four structures. It lies near cell membrane. Cisternae: They are curved with dilated ends and are parallel to each other.
Actin-severing proteins ADF/cofilin are required for the sorting of secretory cargo at the trans-Golgi network (TGN) in mammalian cells. How do these cytoplasmic proteins interact with the cargoes in the lumen of the TGN ...
At ER, the doctor asked me to have an abdominal CT scan, which I declined, because it is not only expensive, but will create a lot of radiation exposure. But I did have the abdominal X-Ray and blood test, both of which came back normal. At the time I left ER, I felt a lot better. I came to work with very sleepy eyes. Maybe I should be more careful with what I eat or drink in the future, especially cold bottled Coke ...
The classical tango is a dance characterized by a 2/4 or 4/4 rhythm in which the partners dance in a coordinated way, allowing dynamic contact. There is a surprising similarity between the tango and how KCNE β-subunits
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Page contains details about 1,2-dipalmitoyl-sn-glycero-phosphatidylcholine vesicles . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
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Ok so some buddys were telling me that I might want to invest into some Cell-Tech.. So I was wondering what I should stack it with? Has anybody used
Expression of ARFGAP2 (FLJ14576, IRZ, Zfp289, ZNF289) in epididymis tissue. Antibody staining with HPA016649 and HPA018152 in immunohistochemistry.
In article ,bcshoh$kb8$1 at news.hccnet.nl,, anton at vredegoor.doge.nl (Anton Vredegoor) wrote: , Output from a test run: , , zipped : 0.985 sec. , ranged : 0.425 sec. , inplace : 0.206 sec. Interesting. When I try it, what I find is that zipped is usually but not always fastest, inplace is a little slower, and ranged is significantly slower -- data at end of message. I tried also a simple generator based one but it didnt do better than the others: def generate(L): return list(generator(L)) def generator(L): last = object() for x in L: if x != last: yield x last = x The test data: % python test.py zipped : 0.090 sec. ranged : 0.190 sec. inplace : 0.090 sec. generate: 0.120 sec. % python test.py zipped : 0.090 sec. ranged : 0.180 sec. inplace : 0.100 sec. generate: 0.110 sec. % python test.py zipped : 0.130 sec. ranged : 0.170 sec. inplace : 0.100 sec. generate: 0.110 sec. % python test.py zipped : 0.070 sec. ranged : 0.150 sec. inplace : 0.110 sec. generate: 0.110 sec. % python test.py zipped ...
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this article talks about the use and misuse of sec.-498 A of I.P.C.,it also talks about the measures and also it talks about the role of judiciary in it.

Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking | JCBDifferential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking | JCB

Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123:1365-1371. ... COPI-coated vesicles were purified via sucrose density centrifugation. 50% of the vesicle fractions (V) and 0.5% of input (I) ... Two human ARFGAPs associated with COP-I-coated vesicles. Traffic. 8:1644-1655. ... The formation of coat protein complex I (COPI)-coated vesicles is regulated by the small guanosine triphosphatase (GTPase) ...
more infohttp://jcb.rupress.org/content/183/4/725

Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. | JCBHydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. | JCB

Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.. G Tanigawa, L Orci, M Amherdt ... Coat assembly is triggered when ARF binds GTP, initiating transport vesicle budding, and coat disassembly is triggered when ARF ... Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. ... helps to provide vectoriality to vesicle transport. ...
more infohttp://jcb.rupress.org/content/123/6/1365

β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis...β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis...

β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis ... 1993) β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular ... is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67: 239-253PubMed ... Duden R, Griffiths G, Frank R, Argos P, Kreis TE (1991) ß-COP, a 110kD protein associated with nonclathrin coated vesicles and ...
more infohttps://rd.springer.com/chapter/10.1007/978-3-662-02928-2_26

Xpert search results for Cell orgXpert search results for Cell org

3.2 Formation of clathrin and COP-coated vesicles. This unit explains the function of the cytoskeleton and its role in ... 3.3 Fusion of vesicles with the target membrane. This unit explains the function of the cytoskeleton and its role in ... This unit explains the function of the cytoskeleton and its role in controlling transport of vesicles between different ... This unit explains the function of the cytoskeleton and its role in controlling transport of vesicles between different ...
more infohttps://www.nottingham.ac.uk/xpert/scoreresults.php?keywords=Cell%20org&start=3120&end=3140

Fusion of Biological Membranes and Related Problems, Subcellular Biochemistry by Herwig J. Hilderson | 9780306463136 | BooktopiaFusion of Biological Membranes and Related Problems, Subcellular Biochemistry by Herwig J. Hilderson | 9780306463136 | Booktopia

Membrane Proteins of COP-Coated Vesicles. p. 15. Membrane Proteins of Clathrin-Coated Vesicles. p. 17. ... Reconstitution of Coated Vesicles from Chemically Defined Liposomes. p. 19. Polymerization of Coatomer and COPI Bud Formation. ... Acyl-CoA and Vesicle Trafficking, Lessons from Yeast Mutants. p. 200. Allosteric Effects of Long-Chain Acyl-CoA on Vesicle ... Nuclear Vesicle Fusion Requires GTP Hydrolysis. p. 288. Early Evidence for a Putative Role of ARFs in Nuclear Vesicle Dynamics ...
more infohttps://www.booktopia.com.au/fusion-of-biological-membranes-and-related-problems-herwig-j-hilderson/book/9780306463136.html

Redistribution of Sec16 to the cytosol by the P1092L mu | Open-iRedistribution of Sec16 to the cytosol by the P1092L mu | Open-i

COP-Coated Vesicles/metabolism*. *Endoplasmic Reticulum/metabolism*. *Fungal Proteins/genetics/metabolism*. *Pichia/genetics/ ... During the budding of coat protein complex II (COPII) vesicles from transitional endoplasmic reticulum (tER) sites, Sec16 has ... During the budding of coat protein complex II (COPII) vesicles from transitional endoplasmic reticulum (tER) sites, Sec16 has ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC3814151_3406fig5&req=4

Removal of Sec16 from tER sites by anchoring on cytosol | Open-iRemoval of Sec16 from tER sites by anchoring on cytosol | Open-i

COP-Coated Vesicles/metabolism*. *Endoplasmic Reticulum/metabolism*. *Fungal Proteins/genetics/metabolism*. *Pichia/genetics/ ... During the budding of coat protein complex II (COPII) vesicles from transitional endoplasmic reticulum (tER) sites, Sec16 has ... During the budding of coat protein complex II (COPII) vesicles from transitional endoplasmic reticulum (tER) sites, Sec16 has ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC3814151_3406fig7&req=4

Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds, Plant Molecular Biology ...Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds, Plant Molecular Biology ...

COP-coated vesicles in intracellular protein transport. Harter, C.. * A strobilurin fungicide enhances the resistance of ... cDNA microarray analysis of gene expression during Fe-deficiency stress in barley suggests that polar transport of vesicles is ...
more infohttps://www.deepdyve.com/lp/springer_journal/specific-patterns-of-changes-in-wheat-gene-expression-after-treatment-CxYLae5hyr

Reconstitution of Intracellular Transport, Volume 219 - 1st EditionReconstitution of Intracellular Transport, Volume 219 - 1st Edition

T. Serafini and J.E. Rothman, Purification of Golgi Cisternae-Derived COP-Coated Vesicles. ... M. Pypaert and G. Warren, Morphological Studies of Formation of Coated Pits and Coated Vesicles in Broken Cells. ... P.G. Woodman and G. Warren, Isolation and Characterization of Functional, Clathrin Coated, Endocytic Vesicles. ... E. Sztul, Transcytotic Vesicle Fusion with the Plasma Membrane.. B.M. Mullock and J.P. Luzio, Reconstitution of Rat Liver ...
more infohttps://www.elsevier.com/books/reconstitution-of-intracellular-transport-219/rothman/978-0-12-182120-3

Endoplasmosis and exoplasmosis: the evolutionary principles underlying endocytosis, exocytosis, and vesicular transport |...Endoplasmosis and exoplasmosis: the evolutionary principles underlying endocytosis, exocytosis, and vesicular transport |...

Harter C. COP-coated vesicles in intracellular protein transport. FEBS Lett. 1995;369(1):89-92. CrossRefPubMed ... Vesicle coats: structure, function, and general principles of assembly. Trends Cell Biol. 2013;23(6):279-288. CrossRefPubMed ... The COPII cage: unifying principles of vesicle coat assembly. Nat Rev Mol Cell Biol. 2006;7(10):727-738. CrossRefPubMed ... A novel class of clathrin-coated vesicles budding from endosomes. J Cell Biol. 1996;132(1-2):21-33. CrossRefPubMed ...
more infohttps://www.springermedizin.at/endoplasmosis-and-exoplasmosis-the-evolutionary-principles-under/14928906

Gene Report for G00002204 - Genes2Cognition Neuroscience Research ProgrammeGene Report for G00002204 - Genes2Cognition Neuroscience Research Programme

Two human ARFGAPs associated with COP-I-coated vesicles.. Frigerio G, Grimsey N, Dale M, Majoul I and Duden R ... In contrast to ARFGAP1, both ARFGAP2 and ARFGAP3 are associated with COP-I-coated vesicles generated from Golgi membranes in ... The formation of coat protein complex I (COPI)-coated vesicles is regulated by the small guanosine triphosphatase (GTPase) ... by regulating the uncoating of coat protein I (COPI)-coated vesicles. Depletion of ArfGAP1 by RNA interference, however, causes ...
more infohttp://www.genes2cognition.org/db/Gene/G00002204

囊泡 - 维基百科,自由的百科全书囊泡 - 维基百科,自由的百科全书

En bloc incorporation of coatomer subunits during the assembly of COP-coated vesicles.. The Journal of cell biology. 1994-03, ... 並且介導COPⅡ囊泡的形成。根據COPⅡ囊泡裝配的貨物分子大小,Sec31 C端的氨基酸序列可以成不同幾何形狀的COPⅡ籠型,從而使COPⅡ囊泡容納前膠原、
more infohttps://zh.wikipedia.org/wiki/%E5%9B%8A%E6%B3%A1

COPI-mediated Transport, The Journal of Membrane Biology | 10.1007/s00232-006-0859-7 | DeepDyveCOPI-mediated Transport, The Journal of Membrane Biology | 10.1007/s00232-006-0859-7 | DeepDyve

ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein ... A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta- ... zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly ... Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin ...
more infohttps://www.deepdyve.com/lp/springer_journal/copi-mediated-transport-32yDHbBIvx

Frontiers | Activators and Effectors of the Small G Protein Arf1 in Regulation of Golgi Dynamics During the Cell Division Cycle...Frontiers | Activators and Effectors of the Small G Protein Arf1 in Regulation of Golgi Dynamics During the Cell Division Cycle...

Misteli, T., and Warren, G. (1994). COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell- ... Sönnichsen, B., Watson, R., Clausen, H., Misteli, T., and Warren, G. (1996). Sorting by COP I-coated vesicles under interphase ... recruit several coat complexes, including GGA1-3/clathrin, AP-1/clathrin, AP-3/clathrin, and AP-4 coats (Bonifacino and Glick, ... The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins. Science 346:1256898. doi: ...
more infohttps://www.frontiersin.org/articles/10.3389/fcell.2018.00029/full

ARFGAP2 Gene - GeneCards | ARFG2 Protein | ARFG2 AntibodyARFGAP2 Gene - GeneCards | ARFG2 Protein | ARFG2 Antibody

Two human ARFGAPs associated with COP-I-coated vesicles. (PMID: 17760859) Frigerio G … Duden R (Traffic (Copenhagen, Denmark) ... Gamma-COP appendage domain - structure and function. (PMID: 14690497) Watson PJ … Owen DJ (Traffic (Copenhagen, Denmark) 2004) ... Among its related pathways are Vesicle-mediated transport and Transport to the Golgi and subsequent modification. Gene Ontology ...
more infohttps://www.genecards.org/cgi-bin/carddisp.pl?gene=ARFGAP2

Genome-Wide Screen Reveals sec21 Mutants of Saccharomyces cerevisiae Are Methotrexate-Resistant | G3: Genes | Genomes | GeneticsGenome-Wide Screen Reveals sec21 Mutants of Saccharomyces cerevisiae Are Methotrexate-Resistant | G3: Genes | Genomes | Genetics

1993 zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly. J. Cell Biol. 123: 1727-1734. ... and assembly of COP-coated vesicles (Kuge et al. 1993; Beck et al. 2009), may be important in mediating the transport of ... 1994 Yeast beta- and beta′-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein ... Together, these findings suggest that the conserved function of COPI coatomer complex in the intercompartmental vesicle- ...
more infohttps://www.g3journal.org/content/7/4/1251

Coatomer beta subunit, C-terminal (IPR011710) | InterPro | EMBL-EBICoatomer beta subunit, C-terminal (IPR011710) | InterPro | EMBL-EBI

COP and clathrin-coated vesicle budding: different pathways, common approaches.. Curr. Opin. Cell Biol. 16 379-91 2004 ... This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat ... As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. Coatomer complexes also influence ... Coatomer protein complex I (COPI)-coated vesicles are involved in transport between the endoplasmic reticulum and the Golgi but ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR011710

Definition of Divisions Of The Peripheral Nervous System | Chegg.comDefinition of Divisions Of The Peripheral Nervous System | Chegg.com

Question 6 options: Cop II coated vesicles move cargo from the ER to the Golgi. Starting nearest the nucleus and moving toward ...
more infohttps://www.chegg.com/homework-help/definitions/divisions-of-the-peripheral-nervous-system-14

Cell and Molec Final Flashcards - Cram.comCell and Molec Final Flashcards - Cram.com

transport vesicles with distincive protein coats What is the default pathway for secretion? ... What allows secretory proteins to be packed into vesicles at high concentrations? ...
more infohttp://www.cram.com/flashcards/cell-and-molec-final-349489

p38 MAPK regulates COPII recruitment<...p38 MAPK regulates COPII recruitment<...

keywords = "COP-Coated Vesicles, Endoplasmic Reticulum, HeLa Cells, Humans, p38 Mitogen-Activated Protein Kinases", ... Here, we investigate regulation of coat protein complex II (COPII) recruitment onto ER export sites in permeabilized cells. In ... N2 - Here, we investigate regulation of coat protein complex II (COPII) recruitment onto ER export sites in permeabilized cells ... AB - Here, we investigate regulation of coat protein complex II (COPII) recruitment onto ER export sites in permeabilized cells ...
more infohttps://discovery.dundee.ac.uk/en/publications/p38-mapk-regulates-copii-recruitment

Gendoo - Relevant featuresGendoo - Relevant features

Coated Vesicles 被覆小胞 COP-Coated Vesicles COP被覆小胞 ... Clathrin-Coated Vesicles クラスリン被覆小胞 Cell Surface Extensions 細胞表面 ... Coat Protein Complex I コート蛋
more infohttp://gendoo.dbcls.jp/cgi-bin/gendoo.cgi?geneid=30011&taxonomy=human

Exosomes with Immune Modulatory Features Are Present in Human Breast Milk | The Journal of ImmunologyExosomes with Immune Modulatory Features Are Present in Human Breast Milk | The Journal of Immunology

COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr. Opin. Cell Biol. 16: 379-391. ... To analyze the morphology of the obtained vesicles, they were coated to anti-MHC class II beads and analyzed by EM. The ... In additional experiments the milk vesicle preparation was coated to anti-MHC class II Dynabeads and/or anti-CD81 latex beads, ... 2⇑C). Vesicles from mature milk were positive for HLA-ABC for all individuals, whereas vesicles of colostrum from five of eight ...
more infohttp://www.jimmunol.org/content/179/3/1969?ijkey=be94bbe3eb25492e8eeda7cbf19526884ddc705c&keytype2=tf_ipsecsha

Regulation of Early Endosome Fusion In Vitro | Springer for Research & DevelopmentRegulation of Early Endosome Fusion In Vitro | Springer for Research & Development

ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP coated vesicles: a novel role for a GTP-binding protein. ... Woodman, P., and Warren, G. (1991). Isolation of functional, coated endocytic vesicles. J. Cell Biol. 112, 1133-1141.PubMed ... Characterisation of the early endosome and putative endocytic carrier vesicles in vivo and with an ssay of vesicle fusion in ... Membrane Transport Early Endosome Late Endosome Endocytic Pathway Transport Vesicle These keywords were added by machine and ...
more infohttps://rd.springer.com/chapter/10.1007/978-3-662-02928-2_45

ARF1 Antibody (1D9) (NB300-505): Novus BiologicalsARF1 Antibody (1D9) (NB300-505): Novus Biologicals

ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. ... Arf has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co- ...
more infohttps://www.novusbio.com/products/arf1-antibody-1d9_nb300-505

Dartmouth Digital Library ProgramDartmouth Digital Library Program

coated vesicles. ; golgi apparatus. ; saccharomyces cerevisiae -- molecular aspects. ; phospholipids -- physiological effect ... biochemical assays have revealed that intracellular protein trafficking is mediated by a conserved mechanism of vesicle budding ... cop-coated vesicles (1). *iron-sulfur proteins. (1). Youve searched:. All Collections ...
more infohttp://libarchive.dartmouth.edu/cdm/search/searchterm/Saccharomyces
  • Spiral Coating of the Endothelial Caveolar Membranes as Revealed by Electron Tomography and Template Matching. (springermedizin.at)
  • ALPS motifs are unstructured in solution but form an amphipathic α helix once bound to highly curved membranes as present on a vesicle. (rupress.org)
  • The phenotypes observed in the triple ArfGAP knockdown cells are similar to those seen in beta-COP-depleted cells. (genes2cognition.org)
  • Both the triple ArfGAP- and beta-COP-depleted cells accumulate characteristic vacuolar structures that are visible under electron microscope. (genes2cognition.org)
  • In addition, an increased number of Foxp3 + CD4 + CD25 + T regulatory cells were observed in PBMC incubated with milk vesicle preparations. (jimmunol.org)
  • M.G. Waters, C.J.M. Beckers, and J.E. Rothman , Purification of Coat Protomers. (elsevier.com)
  • Functional analysis revealed that the vesicle preparation inhibited anti-CD3-induced IL-2 and IFN-γ production from allogeneic and autologous PBMC. (jimmunol.org)
  • Gamma-COP appendage domain - structure and function. (ebi.ac.uk)
  • We isolated vesicles from colostrum and mature milk by differential ultracentrifugation and sucrose gradient fractionation and characterized them both morphologically by electron microscopy (EM) and phenotypically by flow cytometry, Western blot and mass spectrometry (MS). We found that these vesicles display similar shapes, sizes, and densities as those of previously described exosomes. (jimmunol.org)