303,331 research outputs found
Drosophila REEP1 modulates ER morphology and ER stress
No full textDefects in endoplasmic reticulum (ER) membrane shaping and in lipid metabolism seem to be crucial mechanisms underlying Hereditary Spastic Paraplegia (HSP), a complex genetic disorder characterized by the axonal degeneration of corticospinal tracts. Here we report the analysis of a Drosophila melanogaster model of SPG31, an autosomal dominant form of HSP caused by mutations in the Receptor Expression Enhancing Protein1 gene (REEP1). REEP1 coordinates ER shaping within the tubular ER and confers resistance to ER stress in neurons, but the mechanism of this effect remains to be elucidated. In this work, we analyzed the effects of loss of D-REEP1 (REEPA) on the ER morphology, the Unfolded Protein Response (UPR), the locomotor activity and longevity. The absence of REEPA negatively affected longevity reducing lifespan as well as the locomotor activity. Moreover, REEPA mutant presented a larger proportion of apparent ER sheets, the up-regulation of ER-stress sensor Bip, the activation of Ire1 and ATF6 pathways, and a drastic reduction of the transcription level of two major enzymes involved in LDs biogenesis. The administration to REEPA mutant of naringenin, a flavanone known for its neuroprotective effects, rescued lifespan defect and ER homeostasis by decreasing UPR activation and enhancing LDs biogenesis, thus representing a promising strategy for the management of HSP symptoms
The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi
No full textA procedure has been established in Vero cells for the isolation of an intermediate compartment involved in protein transport from the ER to the Golgi apparatus. The two-step subcellular fractionation procedure consists of Percoll followed by Metrizamide gradient centrifugation. Using the previously characterized p53 as a marker protein, the average enrichment factor of the intermediate compartment was 41. The purified fraction displayed a unique polypeptide pattern. It was largely separated from the rough ER proteins ribophorin I, ribophorin II, BIP, and protein disulfide isomerase, as well as from the putative cis-Golgi marker N-acetylglucosamine-1-phosphodiester-alpha-N-acetylglucosaminidase, the second of the two enzymes generating the lysosomal targeting signal mannose-6-phosphate. The first enzyme, N-acetylglucosaminylphosphotransferase, for which previous biochemical evidence had suggested both a pre- and a cis-Golgi localization in other cell types, cofractionated with the cis-Golgi rather than the intermediate compartment in Vero cells. The results suggest that the intermediate compartment defined by p53 has unique properties and does not exhibit typical features of rough ER and cis-Golgi
Bulla apostolica contra errores Martini Lvtheri & Sequaciu[m].
No full textColofon: Impressum prius Romæ p[er] Iacobu[m] Mazochiu[m] de Mandato [...] Et deinde Antuerpiae [...]Machiels, J. Catalogus van de boeken gedrukt vóór 1600 ; L 174Nijhoff en Kronenberg. Nederlandsche bibliographie van 1500 tot 1540; 1342Europeana-GoogleBook
Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway
No full textERGIC-53 is a lectin-type membrane protein that continuously recycles between the ER, ER-Golgi intermediate compartment (ERGIC) and the cis-Golgi. To identify the targeting signals that mediate this recycling, N-glycosylated and myc-tagged variants of ERGIC-53 were constructed. By monitoring endoglycosidase H resistance, we measured the loss from the ER-ERGIC-cis-Golgi cycle of ERGIC-53. A domain exchange approach with the plasma membrane reporter protein CD4 showed that the transmembrane and the lumenal domains are not sufficient, while the cytoplasmic domain of ERGIC-53 is required and sufficient for pre-medial-Golgi localization. However, the ERGIC-53 cytoplasmic domain on CD4 lead to increased ER-staining by immunofluorescence microscopy indicating that this domain alone cannot provide for unbiased recycling through the ER-ERGIC-cis-Golgi compartments. Complete progress through the ER-ERGIC-cis-Golgi recycling pathway requires the cytoplasmic domain acting together with the lumenal domain of ERGIC-53. Dissection of the cytoplasmic domain revealed a COOH-terminal di-lysine ER-retrieval signal, KKFF, and an RSQQE targeting determinant adjacent to the transmembrane domain. Surprisingly, the two COOH-terminal phenylalanines influence the targeting. They reduce the ER-retrieval capacity of the di-lysine signal and modulate the RSQQE determinant
The ISBD(ER) and New Developments in Cataloging Electronic Resources [Version presented at the International Conference]
No full textThe topic is the ISBD(ER)--the International Standard Bibliographic Description for Electronic Resources--and a discussion of new developments affecting the cataloging of these resources that have taken place since the ISBD(ER) was published in 1997. The ISBD(ER) is a revision of the ISBD(CF)--the International Standard Bibliographic Description for Computer Files, which was produced and published in 1989. That first edition, in turn, was developed from the ISBD(NBM)--the International Standard Bibliographic Description for Non-Book Materials--which was first published in 1977 and contained the earliest provisions for covering materials that were then called machine-readable data files. The ISBD(ER) is one of seven ISBDs. While all have been affected over time by developments that have resulted in their revision, the ISBD(ER) has been particularly vulnerable to revision due to rapid advances in the technology and the emergence of new materials and formats that are--and continue to be--volatile.
Contents: 0.5 Sources of information; General material designation (GMD); Edition Area; Type and Extent of Resource Area; Physical Description Area; Notes Area; Standard Number (or Alternative Area); What lies ahead?; Where are the ISBD(ER) and AACR2 headed
Carbohydrate- and conformation-dependent cargo capture for ER-exit
No full textSome secretory proteins leave the endoplasmic reticulum (ER) by a receptor-mediated cargo capture mechanism, but the signals required for the cargo-receptor interaction are largely unknown. Here, we describe a novel targeting motif that is composed of a high-mannose type oligosaccharide intimately associated with a surface-exposed peptide beta-hairpin loop. The motif accounts for lectin ERGIC-53-assisted ER-export of the lyososomal enzyme procathepsin Z. The second oligosaccharide chain of procathepsin Z exhibits no binding activity for ERGIC-53, illustrating the selective lectin properties of ERGIC-53. Our data suggest that the conformation-based motif is only present in fully folded procathepsin Z and that its recognition by ERGIC-53 reflects a quality control mechanism that acts complementary to the primary folding machinery in the ER. A similar oligosaccharide/beta-hairpin loop structure is present in cathepsin C, another cargo of ERGIC-53, suggesting the general nature of this ER-exit signal. To our knowledge this is the first documentation of an ER-exit signal in soluble cargo in conjunction with its decoding by a transport receptor
Multiple phase-shift all-fibre DFB lasers
No full textA double (2 x π/2) phase-shifted Er/Yb fibre DFB laser shows a 50% reduction of the shift in lasing wavelength and a 10% reduction of the linewidth, compared to standard single phase-shifted fibre DFB designs
Evangelische Schatz-Kam[m]er
No full textEVANGELISCHE SCHATZ-KAM[M]ER
Evangelische Schatz-Kam[m]er (-)
Evangelische Schatz-Kam[m]er ([Theil 1]) ([1])
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Zuschrifft. ([2])
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A wash-free ER marker to monitor micropolarity during ER stress and visualize ER- Golgi transport
No full textCellular stress plays a key role to regulate and maintain organismal as well as microenvironmental homeostasis. The stress-induced response is also reflected in the micropolarity of any specific cellular compartment, which is essential to be quantified for early disease diagnosis. Alongside, coming up with a biocompatible small-molecule fluorophore NBD-Oct for exclusive endoplasmic reticulum (ER) localization simply driven by its hydrophobicity, in this contribution, we present a quantitative study of micropolarity alteration inside the ER during G1/S and G2/M phases. The cell cycle arrests caused by the induced ER stress led to the enhancement of the ER micropolarity in cells. NBD-Oct is selected among a series of analogous probes based on its fastest diffusion properties demonstrated by fluorescence recovery after the photobleaching experiment. The probe is a versatile staining agent as it could efficiently stain the ER in live/fixed mammalian cells, isolated ER, Caenorhabditis elegans, and mice tissues. Finally, a well-known biological event, ER to Golgi transport is also visualized by live-cell fluorescence microscopy using this probe. We believe this exhaustive investigation of micropolarity using NBD-based dye provides a new avenue to study ER stress that may unravel a deeper understanding of proteostasis in model systems and potentially even fixed patient samples
Anglo-normand engle(i)m(m)er
No full textHenry Albert. Anglo-normand engle(i)m(m)er. In: Romania, tome 111 n°443-444, 1990. pp. 542-543
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