The Golgi apparatus has long been suggested to be important for directing secretion to specific sites on the plasma membrane in response to extracellular signaling events. However, the mechanisms by which signaling events are coordinated with Golgi apparatus function remain poorly understood. Here, we identify a scaffolding function for the Golgi matrix protein GM130 that sheds light on how such signaling events may be regulated. We show that the mammalian Ste20 kinases YSK1 and MST4 target to the Golgi apparatus via the Golgi matrix protein GM130. In addition, GM130 binding activates these kinases by promoting autophosphorylation of a conserved threonine within the T-loop. Interference with YSK1 function perturbs perinuclear Golgi organization, cell migration, and invasion into type I collagen. A biochemical screen identifies 14-3-3zeta as a specific substrate for YSK1 that localizes to the Golgi apparatus, and potentially links YSK1 signaling at the Golgi apparatus with protein transport events, cell
TY - JOUR. T1 - Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs. AU - Dobrosotskaya, Irina Y.. AU - Goldstein, Joseph L.. AU - Brown, Michael S.. AU - Rawson, Robert B.. PY - 2003/9/12. Y1 - 2003/9/12. N2 - In mammalian cells, membrane-bound sterol regulatory element-binding proteins (SREBPs) are transported from ER to Golgi where they are processed proteolytically to generate soluble transcription factors that activate lipid synthesis. ER-to-Golgi transport requires SCAP, a sterol-regulated escort protein. In sterol-treated cells, the SCAP/SREBP complex binds to Insig-1 or Insig-2, which retains the complex in the ER, blocking SREBP processing and decreasing lipid synthesis. In Drosophila cells, the endogenous SCAP/SREBP complex is transported to Golgi, but transport is blocked by phosphatidylethanolamine instead of sterols. Here, we show that mammalian SREBP-2 is not transported to Golgi when ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
XPLDHTNVTA PQASMMFQYF VKVVPTVYMK VDGEAPLPPQ VLRTNQFSVT RHEKVANGLL GDQGLPGVFV LYELSPMMVK LTEKHRSFTH FLTGVCAIIG GMFTVAGLID SLIYHSARAI QKKIDLGKTT ...
Rab GTPases control vesicle movement and tethering membrane events in membrane trafficking. We used the 38 human Rab GTPase activating proteins (GAPs) to identify which of the 60 Rabs encoded in the human genome function at the Golgi complex. Surprisingly, this screen identified only two GAPs, RN-tre and TBC1D20, disrupting both Golgi organization and protein transport. RN-tre is the GAP for Rab43, and controls retrograde transport into the Golgi from the endocytic pathway. TBC1D20 is the ER-localized GAP for Rab1, and is the only GAP blocking the delivery of secretory cargo from the ER to the cell surface. Strikingly, its expression causes the loss of the Golgi complex, highlighting the importance of Rab1 for Golgi biogenesis. These effects can be antagonized by reticulon, a binding partner for TBC1D20 in the ER. Together, these findings indicate that Rab1 and Rab43 are key Rabs required for the biogenesis and maintenance of a functional Golgi structure, and suggest that other Rabs acting at the Golgi
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 ...
Multiple epidemiologic observations and meta-analysis clearly indicate the link between alcohol abuse and the incidence and progression of prostate cancer; however, the mechanism remains enigmatic. Recently, it was found that ethanol (EtOH) induces disorganization of the Golgi complex caused by impaired function of the largest Golgi matrix protein, giantin (GOLGB1), which, in turn, alters the Golgi docking of resident Golgi proteins. Here, it is determined that in normal prostate cells, histone deacetylase 6 (HDAC6), the known regulator of androgen receptor (AR) signaling, localizes in the cytoplasm and nucleus, while its kinase, glycogen synthase kinase β (GSK3β), primarily resides in the Golgi. Progression of prostate cancer is accompanied by Golgi scattering, translocation of GSK3β from the Golgi to the cytoplasm, and the cytoplasmic shift in HDAC6 localization. Alcohol dehydrogenase-generated metabolites induces Golgi disorganization in androgen-responsive LNCaP and 22Rv1 cells, ...
TY - JOUR. T1 - Genetic analysis of the subunit organization and function of the conserved oligomeric Golgi (COG) complex. T2 - Studies of COG5- and COG7-deficient mammalian cells. AU - Oka, Toshihiko. AU - Vasile, Eliza. AU - Penman, Marsha. AU - Novina, Carl D.. AU - Dykxhoorn, Derek M.. AU - Ungar, Daniel. AU - Hughson, Frederick M.. AU - Krieger, Monty. PY - 2005/9/23. Y1 - 2005/9/23. N2 - The conserved oligomeric Golgi (COG) complex is an eight-subunit (Cog1-8) peripheral Golgi protein involved in Golgi-associated membrane trafficking and glycoconjugate synthesis. We have analyzed the structure and function of COG using Cog1 or Cog2 null Chinese hamster ovary cell mutants, fibroblasts from a patient with Cog7-deficient congenital disorders of glycosylation, and stable Cog5-deficient HeLa cells generated by RNA interference. Although the dilation of some Golgi cisternae in Cog5-deficient cells resembled that observed in Cog1- or Cog2-deficient cells, their global glycosylation defects (less ...
Microtubules (MT) are required for the efficient transport of membranes from the trans-Golgi and for transcytosis of vesicles from the basolateral membrane to the apical cytoplasm in polarized epithelia. MTs in these cells are primarily oriented with their plus ends basally near the Golgi and their minus-ends in the apical cytoplasm. Here we report that isolated Golgi and Golgi-enriched membranes from intestinal epithelial cells possess the actin based motor myosin-I, the MT minus-end-directed motor cytoplasmic dynein and its in vitro motility activator dynactin (p150/Glued). The Golgi can be separated into stacks, possessing features of the Golgi cisternae, and small membranes enriched in the trans-Golgi network marker TGN 38/41. Whereas myosin-I is present on all membranes in the Golgi fraction, dynein is present only on the small membrane fraction. Dynein, like myosin-I, is associated with membranes as a cytoplasmic peripheral membrane protein. Dynein and myosin-I coassociate with membranes ...
gi,17538522,ref,NP_501092.1, component of oligomeric Golgi complex 2; brefeldin A-sensitive, LDLC related peripheral Golgi protein, required for normal Golgi function; contains an N myristoylation domain (78.6 kD) (4H802) [Caenorhabditis elegans] gi,2498513,sp,Q21444,COG2_CAEEL Conserved oligomeric Golgi complex component 2 (LDLC protein homolog) gi,1078836,pir,,B53542 brefeldin A-sensitive Golgi protein LDLC - Caenorhabditis elegans gi,807871,emb,CAA84428.1, Cog2 protein [Caenorhabditis elegans] ...
The Golgi complex, also known as the Golgi apparatus or simply the Golgi, is a cytoplasmic organelle. It is found in eukaryote cells, as in animals, plants, and fungi. The complex was discovered by Camillo Golgi in 1898. Golgi, who worked at Pavia, Italy, was ignored. His discovery was said to be dirt on his lenses. Years later, electron microscope pictures showed structures just like in the original Golgi drawings. It is made of several flattened sac-like membranes which look like a stack of pancakes. The main function of the Golgi apparatus is to process and package macromolecules, such as proteins and lipids. They come to the Golgi after being built, and before they go to their destination. In general, what the Golgi does is Much of the enzymatic processing is post-translational modification of proteins. The Golgi complex inspects them for flaws and discards extra material added during their manufacture, wraps them up and then targets them for packaging. The Golgi complex is especially active ...
The stiochiometric phosphorylation of golgin-84 in mitosis together with its binding to active rab1 suggested that it may play a role in Golgi structure and/or membrane trafficking through the Golgi apparatus. To address a possible structural role for golgin-84, GFP-tagged full-length and truncated versions of the protein were expressed in HeLa cells, and effects upon Golgi structure were analyzed by immunofluorescence microscopy (Fig. 5 a). At moderate expression levels, none of the golgin-84 constructs elicited any significant change in Golgi structure (unpublished data). Furthermore, constructs that failed to target to the Golgi apparatus had no effects upon Golgi structure even at very high levels of expression (Fig. 5 a; unpublished data). In contrast, expression at high levels of both full-length and golgin-84 lacking the head region had dramatic effects upon Golgi structure, converting the ribbon into punctate structures dispersed throughout the cytoplasm (Fig. 5 b). EM analysis of the ...
Background: In hepatocytes and alcohol-metabolizing cultured cells, Golgi undergoes ethanol (EtOH)-induced disorganization. Periniclear and organized Golgi is important in liver homeostasis, but how the Golgi remains intact is unknown. Work from our laboratories showed that EtOH-altered cellular function could be reversed after alcohol removal; we wanted to determine whether this recovery would apply to Golgi. Methods: We used alcohol-metabolizing HepG2 (VA-13) cells (cultured with or without EtOH for 72 h) and rat hepatocytes (control and EtOH-fed (Lieber-DeCarli diet). For recovery, EtOH was removed and replenished with control medium (48 hours for VA-13 cells) or control diet (10 days for rats). Results: EtOH-induced Golgi disassembly was associated with de-dimerization of the largest Golgi matrix protein giantin, along with impaired transport of selected hepatic proteins. After recovery from EtOH, Golgi regained their compact structure, and alterations in giantin and protein transport were restored.
GBRs (GABAB receptors; where GABA stands for γ-aminobutyric acid) are G-protein-coupled receptors that mediate slow synaptic inhibition in the brain and spinal cord. In vitro assays have previously demonstrated that these receptors are heterodimers assembled from two homologous subunits, GBR1 and GBR2, neither of which is capable of producing functional GBR on their own. We have used co-immunoprecipitation in combination with bioluminescence and fluorescence resonance energy transfer approaches in living cells to assess directly the interaction between GBR subunits and determine their subcellular localization. The results show that, in addition to forming heterodimers, GBR1 and GBR2 can associate as stable homodimers. Confocal microscopy indicates that, while GBR1/GBR1 homodimers are retained in the endoplasmic reticulum and endoplasmic reticulum-Golgi intermediate compartment, both GBR2/GBR2 homodimers and GBR1/GBR2 heterodimers are present at the plasma membrane. Although these observations ...
Recent studies showed that the phospholipase subunits of Platelet Activating Factor Acetylhydrolase (PAFAH) Ib, α1 and α2 partially localize to the Golgi complex and regulate its structure and function. Using siRNA knockdown of individual subunits, we find that α1 and α2 perform overlapping and unique roles in regulating Golgi morphology, assembly, and secretory cargo trafficking. Knockdown of either α1 or α2 reduced secretion of soluble proteins, but neither single knockdown reduced secretion to the same degree as knockdown of both. Knockdown of α1 or α2 inhibited reassembly of an intact Golgi complex to the same extent as knockdown of both. Transport of VSV-G was slowed but at different steps in the secretory pathway: reduction of α1 slowed trans Golgi network to plasma membrane transport, whereas α2 loss reduced endoplasmic reticulum to Golgi trafficking. Similarly, knockdown of either subunit alone disrupted the Golgi complex but with markedly different morphologies. Finally, ...
STAT transcription factors signal from the plasma membrane to the nucleus in response to growth factors and cytokines, but little is known about activation of STAT1 from intracellular sites. Here we show that transient transfection of COS cells with fibroblast growth factor receptors (FGFRs) led to ligand-independent phosphorylation of the receptors, including intracellular immature forms. FGF-independent activation of STAT1 was demonstrated at the Golgi apparatus where it was colocalized with FGFRs. Both FGFR1 and FGFR2 induced strong phosphorylation of STAT1 causing redistribution of the Golgi apparatus, while FGFR3 and FGFR4 induced less phosphorylation of STAT1 and little or no redistribution of the Golgi apparatus. Upon expression of a cytosolic mutant of FGFR4 lacking the transmembrane as well as the extracellular region (CytR4), STAT1 was phosphorylated and transferred to the nucleus. The results indicate that immature forms of FGFRs form incomplete signaling complexes on Golgi membranes trapping
The protein encoded by this gene resides in the golgi, and constitutes one of the 8 subunits of the conserved oligomeric Golgi (COG) complex, which is required for normal golgi morphology and localization. Mutations in this gene are associated with the congenital disorder of glycosylation type IIe.[provided by RefSeq, May 2010 ...
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 ...
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We then studied the effect of the I44A ubiquitin variant on the Golgi system in two ways. First, we added wt or I44A ubiquitin to the mitotic cytosol that was used for the disassembly of the membranes, reisolated the membranes, and then performed the reassembly in the absence of exogenous ubiquitin with either interphase cytosol or pure p97-p47. In a second approach, we performed the disassembly under normal conditions and added the exogenous ubiquitin variants during the reassembly step, to either interphase cytosol or p97-p47. In both cases, the extent of Golgi disassembly and subsequent reassembly of cisternae was determined by stereological analysis of EM images. In these experiments, addition of exogenous VCIP135 was not required because the membranes were not salt washed. Furthermore, since the assay relied on physical removal of soluble mitotic regulators, such as cyclin B, that need to be degraded in vivo, this allowed us to look exclusively at the processes occurring on the ...
Coloured scanning electron micrograph (TEM) of Golgi apparatus, stacks of cisternae and vesicles (Euglena sp.). The Golgi apparatus is a cell organelle in all plant and animal cells. The apparatus consists of flattened membrane bound sacs located close to the endoplasmic reticulum. The Golgi apparatus receives proteins and lipids (fats) from the rough endoplasmic reticulum. It modifies some of them and sorts, concentrates and packs them into sealed droplets called vesicles. Depending on the contents these are despatched to one of three destinations: within the cell to lysosomes; to the cell plasma membrane; outside the cell. . Magnification: x11,010 when shortest axis printed at 25 millimetres. - Stock Image C032/1221
The distribution of beta 1,2 N-acetylglucosaminyltransferase I (NAGT I), alpha 1,3-1,6 mannosidase II (Mann II), beta 1,4 galactosyltransferase (GalT), alpha 2,6 sialyltransferase (SialylT) was determined by immuno-labelling of cryo-sections from HeLa cell lines. Antibody labelling in the HeLa cell line was made possible by stable expression of epitope-tagged forms of these proteins or forms from species to which specific antibodies were available. NAGT I and Mann II had the same distribution occupying the medial and trans cisternae of the stack. GalT and SialylT also had the same distribution but they occupied the trans cisterna and the trans-Golgi network (TGN). These results generalise our earlier observations on the overlapping distribution of Golgi enzymes and show that each of the trans compartments of the Golgi apparatus in HeLa cells contains unique mixtures of those Golgi enzymes involved in the construction of complex, N-linked oligosaccharides. ...
TY - JOUR. T1 - Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. AU - Yoshimori, Tamotsu. AU - Keller, Patrick. AU - Roth, Michael G.. AU - Simons, Kai. PY - 1996/4. Y1 - 1996/4. N2 - The question of how membrane proteins are delivered from the TGN to the cell surface in fibroblasts has received little attention. In this paper we have studied how their post-Golgi delivery routes compare with those in epithelial cells. We have analyzed the transport of the vesicular stomatitis virus G protein, the Semliki Forest virus spike-glycoprotein, both basolateral in MDCK cells, and the influenza virus hemagglutinin, apical in MDCK cells. In addition, we also have studied the transport of a hemagglutinin mutant (Cys543Tyr) which is basolateral in MDCK cells. Aluminum fluoride, a general activator of heterotrimeric G proteins, inhibited the transport of the basolateral cognate proteins, as well as of the hemagglutinin mutant, from the TGN to the cell surface in BHK and ...
We have examined intracellular transport and metabolism of the fluorescent analogue of phosphatidylserine, 1-palmitoyl-2-(N-[12[(7-nitrobenz-2-oxa-1,3-diazole-4-yl)amino] dodecanoyl])-phosphatidylserine ([palmitoyl-C12-NBD]-PS) in cultured fibroblasts. When monolayer cultures were incubated with liposomes containing (palmitoyl-C12-NBD)-PS at 37 degrees C, fluorescent PS was transported to the Golgi apparatus. NBD-containing analogues of phosphatidylcholine, phosphatidylethanolamine (PE), or phosphatidic acid did not accumulate in the Golgi apparatus under the same experimental conditions. We suggest that the transport is not due to endocytosis, but is the result of incorporation and trans-bilayer movement of the (palmitoyl-C12-NBD)-PS at the plasma membrane followed by translocation of the lipid from plasma membrane to the Golgi apparatus via nonvesicular mechanisms. Uptake of fluorescent PS was inhibited by depletion of cellular ATP and was blocked by structural analogues of the lipid or by ...
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 ...
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.. ...
The Conserved Oligomeric Golgi complex can be an evolutionarily conserved multisubunit tethering complex (MTC) thats crucial for intracellular membrane trafficking and Golgi homeostasis. inhabitants. Preliminary analysis uncovered that 8 times after transfection with specific COG-subunit-specific CRISPR constructs a subpopulation of cells (around 5% of the full total population) appeared which have high GNL binding in comparison to control cells (data not really shown). Through the 5% GNL positive inhabitants observed by movement cytometry, presumed COG KO cells had been one cell sorted right into a 96 well dish. Each plate yielded ~10C15 individual colonies. Around the secondary GNL binding test several colonies exhibited diminished GNL staining (~3 for each plate) and these clones were always still positive for the targeted subunit and served as an internal control. We preserved at least 2C5 Cog unfavorable clones for each subunit KO as assessed by high GNL binding (assessed by IF, Physique ...
TY - JOUR. T1 - Motoring around the Golgi. AU - Allan, Victoria J.. AU - Thompson, Heather M.. AU - McNiven, Mark A.. PY - 2002/10. Y1 - 2002/10. N2 - The Golgi apparatus is a dynamic organelle through which nascent secretory and transmembrane proteins are transported, post-translationally modified and finally packaged into carrier vesicles for transport along the cytoskeleton to a variety of destinations. In the past decade, studies have shown that a number of molecular motors are involved in maintaining the proper structure and function of the Golgi apparatus. Here, we review just some of the many functions performed by these mechanochemical enzymes - dyneins, kinesins, myosins and dynamin - in relation to the Golgi apparatus.. AB - The Golgi apparatus is a dynamic organelle through which nascent secretory and transmembrane proteins are transported, post-translationally modified and finally packaged into carrier vesicles for transport along the cytoskeleton to a variety of destinations. In ...
After viral infection and the stimulation of some pattern-recognition receptors, TANK-binding kinase I (TBK1) is activated by K63-linked polyubiquitination followed by trans-autophosphorylation. While the activated TBK1 induces type I interferon production by phosphorylating the transcription factor IRF3, the precise molecular mechanisms underlying TBK1 activation remain unclear. We report here the localization of the ubiquitinated and phosphorylated active form of TBK1 to the Golgi apparatus after the stimulation of RIG-I-like receptors (RLRs) or Toll-like receptor-3 (TLR3), due to TBK1 K63-linked ubiquitination on lysine residues 30 and 401. The ubiquitin-binding protein optineurin (OPTN) recruits ubiquitinated TBK1 to the Golgi apparatus, leading to the formation of complexes in which TBK1 is activated by trans-autophosphorylation. Indeed, OPTN deficiency in various cell lines and primary cells impairs TBK1 targeting to the Golgi apparatus and its activation following RLR or TLR3 stimulation.
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…
Anti-Golgi complex antibodies (AGAs) are primarily associated with systemic lupus erythematosus and Sjögrens syndrome. Here we report on the immunoreactivity of AGAs against five Golgi autoantigens (giantin, golgin-245, golgin-160, golgin-95/GM130, and golgin-97) and provide data from epitope mapping on the most common Golgi autoantigen, namely giantin. A total of 80 human sera containing AGAs, as defined by indirect immunofluorescence on HEp-2 cells, were analyzed by ELISA using recombinant autoantigens and immunoprecipitation. The proportion of AGA sera that reacted with the five Golgi autoantigens was correlated with the molecular mass of the Golgi antigens. Autoantibodies to giantin, the largest Golgi autoantigen, were the predominant AGAs, being found in 50% of the AGA sera. Epitope mapping of giantin was performed using six recombinant fragments spanning the entire protein. Antigiantin-positive sera with low titer autoantibodies recognized epitopes in the carboxyl-terminal fragments that are
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 ...
The Golgi apparatus in mammalian interphase cells is composed of flattened, membrane-bound structures approximately 1µm long, named Golgi cisternae. Between two and five cisternae align in a parallel fashion forming a Golgi stack[34]. At the onset of mitosis, the Golgi stacks take a polarized position around the cell nucleus and centrosome in a cis-trans fashion. The cisternae of same polarity belonging to two adjacent stacks are connected by thin tububules, forming the Golgi Ribbons [35] Towards the end on interphase at G2/M of the cell cycle the Golgi ribbons begin to disassemble and assume a peri-nuclear arrangement around the nucleus. Micro-tubules are known to assist in this structural organization[36]. Unlinking the Golgi ribbon This process emerge from Interphase to early G2 (prophase). It unlinks the golgi ribbon by detaching the cells tubular connections between the cells stacks [36]. In this process the ribbon may be converted into stacks depending on the protein enzymes such as ...
The Golgi apparatus in mammalian interphase cells is composed of flattened, membrane-bound structures approximately 1µm long, named Golgi cisternae. Between two and five cisternae align in a parallel fashion forming a Golgi stack[32]. At the onset of mitosis, the Golgi stacks take a polarized position around the cell nucleus and centrosome in a cis-trans fashion. The cisternae of same polarity belonging to two adjacent stacks are connected by thin tububules, forming the Golgi Ribbons [33] Towards the end on interphase at G2/M of the cell cycle the Golgi ribbons begin to disassemble and assume a peri-nuclear arrangement around the nucleus. Micro-tubules are known to assist in this structural organization[34]. Unlinking the Golgi ribbon This process emerge from Interphase to early G2 (prophase). It unlinks the golgi ribbon by detaching the cells tubular connections between the cells stacks [35]. In this process the ribbon may be converted into stacks depending on the protein enzymes such as ...
Golgi apparatus also called the secretary organelle of the cell because it packages material synthesized in the ER and dispatches it to intracellular like plasma membrane and lysosomes and extracellular like cell-surface target ...
An Endoscopic and Transcranial Perspective of Basal Cisternal Membranes. E, Endoscopic view directed through the opticocarotid triangle. The...
Rough ER is named for its rough appearance, which is due to the ribosomes attached to its outer (cytoplasmic) surface. Rough ER lies immediately adjacent to the cell nucleus, and its membrane is continuous with the outer membrane of the nuclear envelope. The ribosomes on rough ER specialize in the synthesis of proteins that possess a signal sequence that directs them specifically to the ER for processing. (A number of other proteins in a cell, including those destined for the nucleus and mitochondria, are targeted for synthesis on free ribosomes, or those not attached to the ER membrane; see the article ribosome.) Proteins synthesized by the rough ER have specific final destinations. Some proteins, for example, remain within the ER, whereas others are sent to the Golgi apparatus, which lies next to the ER. Proteins secreted from the Golgi apparatus are directed to lysosomes or to the cell membrane; still others are destined for secretion to the cell exterior. Proteins targeted for transport to ...
Predicted to be involved in several processes, including Golgi organization; Golgi vesicle transport; and protein stabilization. Predicted to localize to the Golgi transport complex; cytosol; and plasma membrane. Is expressed in several structures, including brain; pancreas; and reproductive system. Orthologous to human COG3 (component of oligomeric golgi complex 3 ...
Two pathways for the transport of integral membrane proteins appear to exist in protoplasts of suspension-cultured tobacco cells, as Jiang and Rogers (1998) have recently demonstrated by using chimeric integral membrane reporter proteins. Whereas γ-TIP and BP-80 seemed to share the same vesicular pathway to the prevacuolar compartment of these cells, α-TIP did not colocalize in the same transport compartments. Instead, after leaving the ER, α-TIP apparently reached an undefined compartment, bypassing the Golgi apparatus. In contrast to these results, α-TIP does indeed pass through the Golgi apparatus of developing pea cotyledons. Furthermore, because ,90% of the dense vesicles were significantly labeled with α-TIP antibodies in situ and because nearly all of the dense vesicles were also labeled with antibodies raised against the two storage proteins vicilin and legumin (Hohl et al., 1996), α-TIP seems to be cotransported with the storage protein precursor polypeptides along the same ...
The Golgi apparatus, or Golgi complex, functions as a factory in which proteins received from the ER are further processed and sorted for transport to their eventual destinations: lysosomes, the plasma membrane, or secretion. In addition, as noted earlier, glycolipids and sphingomyelin are synthesized within the Golgi. In plant cells, the Golgi apparatus further serves as the site at which the complex polysaccharides of the cell wall are synthesized. The Golgi apparatus is thus involved in processing the broad range of cellular constituents that travel along the secretory pathway. ...
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 ...
Biology Assignment Help, Egg - synergids, Egg - Synergids The three cells of the egg apparatus are arranged in triangular fashion with the egg sharing a common wall with the two synergids and the central cell. In the egg the wall is thicker at the micropylar end and is absent at the cha
Anti-Golgi complex antibodies (AGAs) are primarily associated with systemic lupus erythematosus and Sjögrens syndrome. Here we report on the immunoreactivity of AGAs against five Golgi autoantigens (giantin, golgin-245, golgin-160, golgin-95/GM130, and golgin-97) and provide data from epitope mapping on the most common Golgi autoantigen, namely giantin. A total of 80 human sera containing AGAs, as defined by indirect immunofluorescence on HEp-2 cells, were analyzed by ELISA using recombinant autoantigens and immunoprecipitation. The proportion of AGA sera that reacted with the five Golgi autoantigens was correlated with the molecular mass of the Golgi antigens. Autoantibodies to giantin, the largest Golgi autoantigen, were the predominant AGAs, being found in 50% of the AGA sera. Epitope mapping of giantin was performed using six recombinant fragments spanning the entire protein. Antigiantin-positive sera with low titer autoantibodies recognized epitopes in the carboxyl-terminal fragments that are
1Department of Biochemistry and Molecular Biology, College of Medicine, and 2Department of Internal Medicine, University of Nebraska Medical Center, Omaha, NE, USA, 3Omaha Western Iowa Health Care System, VA Service, Department of Research Service, Omaha, NE, USA. The abnormalities in the Golgi apparatus function are important for the development of alcoholic liver injury, but mechanism and consequences have not been defined. Previously, we found that formation of compact Golgi requires dimerization of the largest Golgi matrix protein, giantin, which is catalyzed by protein disulfide isomerase A3 (PDIA3). Here, in both HepG2 cells expressing alcohol dehydrogenase and hepatocytes isolated from alcohol-fed rats, we show that ethanol administration induces crucial Golgi disorganization, as reflected by conversion of its main body to the several mini-Golgi structures, exhibiting swollen and distended cisternae. This Golgi fragmentation was accompanied by reduced level of giantin and its dimer form, ...
ADP-ribosylation factor-like protein 4A (ARL4A) is a developmentally regulated member of the ARF/ARL GTPase family. The primary structure of ARL4A is very similar to that of other ARF/ARL molecules, but its function remains unclear. The trans-Golgi network golgin GCC185 is required for maintenance of Golgi structure and distinct endosome-to-Golgi transport. We show here that GCC185 acts as a new effector for ARL4 to modulate Golgi organization. ARL4A directly interacts with GCC185 in a GTP-dependent manner. Sub-coiled-coil regions of the CC2 domain of GCC185 are required for the interaction between GCC185 and ARL4A. Depletion of ARL4A reproduces the GCC185-depleted phenotype, causing fragmentation of the Golgi compartment and defects in endosome-to-Golgi transport. GCC185 and ARL4A localize to the Golgi independently of each other. Deletion of the ARL4A-interacting region of GCC185 results in inability to maintain Golgi structure. Depletion of ARL4A impairs the interaction between GCC185 and ...
Arl1 (ARF like protein1) is a poorly understood member of ARF family small GTPases. This thesis presents an original characterization of Arl1 and its effectors. Arl1 was localized to the tans Golgi under EM. Over expression of guanine nucleotide mutants of Arl1 dramatically affects the structure and function of Golgi apparatus. Arl1-GTP was found to interact with GRIP domain of Golgins (Golgin-97, Golgin-245, GCC1 and KIAA0336). The interaction was dependent on the conserved amino acids on both switch II region of Arl1 and the GRIP domain. Collectively, the research presented in this thesis reveals Arl1 is a new regulator of Golgi structure and function and one mechanism of Arl1a??s function is that it recruits and regulates its effectors a?? GRIP domain Golgins to Golgi ...
104. Summary Rosettes of six particles have been visualized by freeze-fracture in the protoplasmic fracture (PF) faces of: a) the plasma membrane, b) Golgi cisternae, and c) Golgi-derived vesicles in mesophyll cells of Zinnia elegans that had been induced to differentiate synchronously into tracheary elements in suspension culture. These rosettes have been observed previously in the PF face of the plasma membranes of a variety of cellulose-synthesizing cells and are thought to be important in cellulose synthesis. In Zinnia tracheary elements, the rosettes are localized in the membrane over regions of secondary wall thickening and are absent between thickenings. The observation of rosettes in the Golgi cisternae and vesicles suggests that the Golgi apparatus is responsible for the selective transport and exocytosis of rosettes in higher plants, as has been previously indicated in the alga Micrasterias (GIDDINGS et al. 1980). The data presented indicate that the Golgi apparatus has a critical role ...
Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis (By similarity).
Plant Golgi stacks are mobile organelles that can travel along actin filaments. How COPII (coat complex II) vesicles are transferred from endoplasmic reticulum (ER) export sites to the moving Golgi stacks is not understood. We have examined COPII vesicle transfer in high-pressure frozen/freeze-subst …
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.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
The glycoside digitonin was used to selectively permeabilize the plasma membrane exposing functionally and morphologically intact ER and Golgi compartments. Permeabilized cells efficiently transported vesicular stomatitis virus glycoprotein (VSV-G) through sealed, membrane-bound compartments in an ATP and cytosol dependent fashion. Transport was vectorial. VSV-G protein was first transported to punctate structures which colocalized with p58 (a putative marker for peripheral punctate pre-Golgi intermediates and the cis-Golgi network) before delivery to the medial Golgi compartments containing alpha-1,2-mannosidase II and processing of VSV-G to endoglycosidase H resistant forms. Exit from the ER was inhibited by an antibody recognizing the carboxyl-terminus of VSV-G. In contrast, VSV-G protein colocalized with p58 in the absence of Ca2+ or the presence of an antibody which inhibits the transport component NSF (SEC18). These studies demonstrate that digitonin permeabilized cells can be used to ...
The spe-10 gene encodes a novel, predicted four-pass integral membrane protein that contains a highly conserved DHHC-CRD motif (Bohm et al. 1997; Putilina et al. 1999). If a potential glycosylation site following TM4 is utilized, then the N-terminal region, the DHHC-CRD zinc-finger, and the C-terminal region should all face the lumen of the MO (Figure 6A). This orientation would allow the N-linked glycans to face the exterior of the cell surface when the MOs fuse to the plasma membrane. Northern hybridizations comparing oogenesis-specific and spermatogenesis-specific transcripts indicate that the spe-10 mRNA is found only in worms that are actively engaged in spermatogenesis (Figure 4B). SPE-10 localizes within the lysosome-like FB-MOs and segregates to spermatids as they bud from the residual body during C. elegans spermatogenesis (Figure 8). These results suggest that a lack of wild-type SPE-10 in the FB-MOs of spe-10 mutants probably causes the previously described sperm ultrastructural ...
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 ...
Transport and Golgi organization protein 1 homolog; 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 s ...
In this study, we demonstrated first that QUA2 is required for normal synthesis of HG in Arabidopsis, and second that QUA2 is a predicted type II membrane protein with a lumenal putative MT domain, which, consistent with a role in the synthesis of HG, accumulates in the Golgi apparatus.. qua1 and qua2 mutants have similar phenotypes: both mutants are dwarfed, with reduced cell adhesion, and show a reduced GalA content and very similar FT-IR profiles. QUA1 - also referred to as GAUT8 (Sterling et al., 2006) - is a member of GT family 8. So far, attempts to demonstrate the enzyme activity for QUA1 expressed in a heterologous system have failed. Recently, however, GalAT activity has been observed for a protein of the same family, GAUT1, expressed in human embryonic kidney cells (Sterling et al., 2006). Given the mutant phenotype and the similarity to GAUT1, it is likely that QUA1 also encodes a GalAT. Concerning QUA2, despite several attempts, we have not been able to produce a soluble version of ...
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Approximately 80% of secreted and membrane proteins (40% of all proteins) of eukaryotes become covalently linked to sugars in the lumen of the Golgi apparatus, a cellular organelle that is part of the secretory system of all eukaryotes. The sugar donors are mostly nucleoside diphosphate sugars (nucl …
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
TY - JOUR. T1 - RNA processing bodies, peroxisomes, golgi bodies, mitochondria, and endoplasmic reticulum tubule junctions frequently pause at cortical microtubules. AU - Hamada, Takahiro. AU - Tominaga, Motoki. AU - Fukaya, Takashi. AU - Nakamura, Masayoshi. AU - Nakano, Akihiko. AU - Watanabe, Yuichiro. AU - Hashimoto, Takashi. AU - Baskin, Tobias I.. PY - 2012/4. Y1 - 2012/4. N2 - Organelle motility, essential for cellular function, is driven by the cytoskeleton. In plants, actin filaments sustain the long-distance transport of many types of organelles, and microtubules typically fine-tune the motile behavior. In shoot epidermal cells of Arabidopsis thaliana seedlings, we show here that a type of RNA granule, the RNA processing body (P-body), is transported by actin filaments and pauses at cortical microtubules. Interestingly, removal of microtubules does not change the frequency of P-body pausing. Similarly, we show that Golgi bodies, peroxisomes, and mitochondria all pause at microtubules, ...
Supplementary MaterialsFigure S1: Comparison of classical and semi-automated methods for measuring Golgi apparatus polarization. and EGF (2 ng/ml) for all those conditions tested: 10 min stimulation (ACB), 30 min stimulation (CCD), pretreatment and concurrent stimulation with U0126 (ECF), BFA (GCH), and wortmannin (ICJ). Y in m and the absolute value of the Golgi angle are plotted as cumulative distributions and examined by Kolmogorov-Smirnov statistical exams. Drug-treated conditions had been weighed against the baseline control non-e and with the activated, drug-free control (denoted by mounting brackets where appropriate). *** represents p0.001, ** represents p0.01, and * represents p0.05.(TIF) pone.0080446.s002.tif (1.7M) GUID:?73CA6A49-6462-4641-85EF-35AF912FC074 Document S1: Dining tables S1, S2, and S3 include two-way ANOVA Boneferroni post-test outcomes for the proper period factors 0 h, 24 h, and 48 h from the wound recovery assay. Dining tables S4 and S3 represent the one-way ANOVA ...
Disclosed herein is an image display system including a display apparatus, an imaging apparatus placed on a movable body; and a server apparatus. The display apparatus and the imaging apparatus are capable of communicating with the server apparatus. The imaging apparatus includes: an imaging section; a speed detection section; and a control section that controls transmission of image data and speed information to the server apparatus. The server apparatus includes: a movable body speed management section that manages the moving speed of the movable body using the speed information; and a control section that identifies an imaging apparatus that matches speed specification information, and causes image data to be transferred from the identified imaging apparatus to the display apparatus. The display apparatus includes: a display section; and a control section that performs a speed specification process, an image request transmission process, and a display process.
The subcellular localization studies of the URGT family indicated that they are located in the Golgi apparatus, which underlines their function as Golgi resident NSTs. All six URGTs are expressed ubiquitously throughout plant development, with URGT1 showing the highest expression levels and URGT2 preferentially expressed during seed development. To characterize the function of URGT1 and URGT2 in planta, we identified loss-of-function mutants and generated plants overexpressing URGT1 and URGT2.. The urgt1 mutants and plants overexpressing URGT1 confirmed its role as a UDP-Gal transporter in vivo because both mutants showed a reduction in cell wall Gal and the overexpressors accumulated Gal in the leaf cell wall. Recently, it was demonstrated that the Gal content of the cell wall could be easily manipulated (35); this is probably due to the extension of galactan side chains on the RG-I backbone. In contrast, no changes in the levels of Rha were observed in either the urgt1 mutants or ...
A sensor apparatus for monitoring voltage and/or current in an electric circuit and a system for monitoring voltages and currents in a system wherein electricity is distributed in a plurality of circuits. A sensor apparatus is associated with each phase conductor in each of the circuits. The sensor apparatus senses the electricity in the phase conductor and provides a digital output that is representative of the sensed electricity in the phase conductor. The digital output preferably includes phasor data for the sensed phase conductor. The monitoring system includes a plurality of such sensor apparatuses. The plurality of sensor apparatuses are coupled to a digital data network that provides for the exchange of sensed data among nodes on the digital data network. On a node of the network, phasor data from some of the plurality of sensor apparatuses are summed or otherwise processed to obtain phasor data representative of a plurality of the circuits.
We have identified AtPAKRP2 cDNA encoding a novel N-terminal motor KRP in Arabidopsis and determined the intracellular localization of this AtPAKRP2 protein. AtPAKRP2 and its homologs in tobacco and B. oleracea localize specifically to the phragmoplast during cell division. In addition to AtPAKRP1 (Lee and Liu, 2000), AtPAKRP2 is the second plant KRP that associates only with the phragmoplast MT array. Unlike AtPAKRP1, which is localized exclusively at or near the plus end of phragmoplast MT bundles, however, AtPAKRP2 appears in a punctate pattern with more pronounced distribution toward the division site. On the basis of biochemical and pharmacological data, AtPAKRP2 likely associates with possibly Golgi-derived vesicles in the phragmoplast. Thus, this protein is a potential motor for vesicle transport during cell plate formation.. Although AtPAKRP2 has a tripartite structure with a coiled-coil domain flanked by the motor and tail domains, it does not fall into any of the established ...
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 ...
Similar to Golgi resident protein GCP60; Acyl-CoA-binding domain-containing protein 3; Golgi complex-associated protein 1; GOCAP1; Golgi phosphoprotein 1; GOLPH1; PBR- and PKA-associated protein 7; Peripheral benzodiazepine receptor-associated protein PAP7 ...
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.
Root hairs, tubular structures that emerge from plant root epidermal cells, grow through localized exocytosis of cell-wall matrix, a process involving actin-dependent delivery of Golgi-derived vesicles containing matrix material to the growing tip. Researchers have long recognized that the cell nucleus maintains a fixed distance from the apex of the growing root hair. The mechanisms by which the nucleus maintains this position, however, and how it pertains to tip growth, remain unclear. Ketelaar et al. used time-lapse photography of Arabidopsis root hair tips to investigate nuclear behavior during root hair growth and did pharmacological analysis to implicate the actin cytoskeleton in nuclear localization. During active growth, the nucleus maintained a fixed distance from the tip, moving backwards when growth ceased to a random position in the root hair. In mutants with branched hairs, branches emerged from the site at which the nucleus was located; thereafter, nuclei moved between growing ...
Constitutive Secretion: Advanced Look --, 2.) Exocytosis After leaving the Golgi apparatus, proteins following the constitutive secretion pathway merge with the cell membrane and release their cargo by a process called exocytosis. Clicking on each of the thumbnail images will bring up a larger, labeled version of the described scene.. To see the Flash movie for the following sequence of images, click here.. ...
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Original Message----- , From: Hemant Agrawal ,[email protected], , Sent: Saturday, April 24, 2021 3:37 AM , , From: Nipun Gupta ,[email protected], , , This patch adds two test vectors for transport block in network byte , order: , - LDPC encode for Transport Block , - LDPC decode for Transport block , , Signed-off-by: Nipun Gupta ,[email protected], , --- See related comment on patch 1. Assuming this is a different PMD assumption (not an incremental one) then this should not require new vectors with the op_flag RTE_BBDEV_LDPC_ENC_NETWORK_ORDER. These would artificially create non-compatible vectors for no reason. But all existing vectors should be able to run on any PMD, the test framework will just change order endianness based on what is supported by the device so that all unit test can be run successfully on any PMD. See how it is done for LLR numerical assumptions which can differ between PMDs. Let me know if unclear , app/test-bbdev/test_vectors/ldpc_dec_tb.data , 122 , ...
Dyggve-Melchior-Clausen syndrome (DMC), a severe autosomal recessive skeletal disorder with mental retardation, is caused by mutation of the gene encoding Dymeclin (DYM). Employing patient fibroblasts with mutations characterized at the genomic and, for the first time, transcript level, we identified profound disruption of Golgi organization as a pathogenic feature, resolved by transfection of heterologous wild-type Dymeclin. Collagen targeting appeared defective in DMC cells leading to near complete absence of cell surface collagen fibers. DMC cells have an elevated apoptotic index (P< 0.01) likely due to a stress response contingent upon Golgi-related trafficking defects. We performed spatiotemporal mapping of Dymeclin expression in zebrafish embryos and identified high levels of transcript in brain and cartilage during early development. Finally, in a chondrocyte cDNA library, we identified two novel secretion pathway proteins as Dymeclin interacting partners: GOLM1 and PPIB. Together these ...
We have assessed the ability of the plant secretory pathway to handle the expression of complex heterologous proteins by investigating the fate of a hybrid immunoglobulin A/G in tobacco cells. Although plant cells can express large amounts of the antibody, a relevant proportion is normally lost to vacuolar sorting and degradation. Here we show that the synthesis of high amounts of IgA/G does not impose stress on the plant secretory pathway. Plant cells can assemble antibody chains with high efficiency and vacuolar transport occurs only after the assembled immunoglobulins have traveled through the Golgi complex. We prove that vacuolar delivery of IgA/G depends on the presence of a cryptic sorting signal in the tailpiece of the IgA/G heavy chain. We also show that unassembled light chains are efficiently secreted as monomers by the plant secretory pathway.. ...
Polyclonal antibody for CAVEOLIN 1/CAV1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. CAVEOLIN 1/CAV1 information: Molecular Weight: 20472 MW; Subcellular Localization: Golgi apparatus membrane; Peripheral
FUNCTION: This gene encodes a protein from the glycosyltransferase 32 family. The encoded enzyme catalyzes the transfer of N-acetylglucosamine to alpha-1,4-linked beta-galactose residues. This enzyme is required for type III mucin synthesis and it is largely associated with the Golgi apparatus membrane. The encoded protein appears to be expressed in adenocarcinoma cells of pancreatic, biliary tract and gastric cancers.[provided by RefSeq, Jan 2010 ...
1. General Function. Rab1 is a small GTP binding protein that is expressed in virtually all mammalian cells, fish, worms and flies and is homologous to the yeast protein Ypt1 (3). It is essential for ER to Golgi transport and has also been implicated in intra Golgi transport (22, 30). There are two isoforms Rab1a (205 aa) and Rab1b (201aa) which are 92% identical at the amino acid level with most differences in the carboxyl terminus (28). These two isoforms are generally localized in the same cellular regions and have similar biochemical properties and functions. Rab1a may also play a role in transcytosis (14). In addition to localization by immunoflourescence in tissue culture cells, Rab1a has been localized by immunogold labeling to vesicles between the ER and Golgi region and over Golgi stacks in NRK cells (23).. The vesicular transport activity of Rab1 is dependent on its GTPase activity as a GDP bound mutant form, Rab1aS25N and the nucleotide free mutant (N124I) block transport from ER to ...
Methods and apparatus are provided for remotely controlling the bending of an elongated member (22) by implementing energy responsible control over a member that is configured from two plastic materials of differing coefficients of thermal expansion. The disclosed methods and apparatus are particularly applicable for use in applications such as surgical catheterization where control of the member from a position relatively remote from the member is desired.