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At least 577 records · Page 32Linked to original sources
PubMed1983

Scanning electron microscopy of Dalkon Shield tails.

Scanning electron micrographs of Dalkon Shield tails removed from asymptomatic patients show a variety of microbes and debris throughout their entire length. Apparently, even in undamaged tails, bacterial flora thrive in the protein-rich environment within the multifilament tail. The presence of microbes in the portion of the tail beyond the double knot indicates that an alternative mechanism of microbial transport can occur. Since transient endometritis often occurs immediately after insertion of intrauterine devices, microbes may come in contact with both exposed ends of the multifilament tail and be drawn into the tail by capillary action from the uterine environment down the tail toward the double knot as well as upward from the vagina. Such microorganisms could serve as an inoculum for infection.

Disease Reservoirs↗
PubMed1999

Immune responses in Indonesian thin tail and Merino sheep during a primary infection with Fasciola gigantica: lack of a specific IgG2 antibody response is associated with increased resistance to infection in Indonesian sheep.

After a primary infection with Fasciola gigantica, the immune responses in a resistant (Indonesian thin tail) and a susceptible (Merino) breed of sheep were analysed. The number of adult flukes recovered from the livers of the Indonesian thin tail sheep were significantly lower than those found in the Merino animals. On days 8, 14 and 25 p.i., Indonesian thin tail sheep exhibited a significantly higher eosinophilia than Merino sheep, whereas neutrophilia was significantly elevated in the Indonesian thin tail sheep on days 36 and 48 p.i. Serum from both sheep breeds demonstrated IgM, IgG1 and IgE responses to F. gigantica. In contrast, the Indonesian thin tail sheep produced significantly lower levels of IgG2 antibodies relative to the high level detected in Merino sheep. The IgE response was biphasic in both sheep breeds with the first response detected by day 14 and the second response developing from days 30 to 60 p.i. Western blotting showed that a similar profile of adult fluke antigens was recognised by IgG1 and IgE antibodies in both the Indonesian thin tail and Merino sheep. The IgE response was directed to a major antigen at about 92 kDa. We postulate that IgG2 could act as a blocking antibody for protective effector responses against F. gigantica in sheep and that the Indonesian thin tail sheep, by downregulating IgG2 responses, have an enhanced capacity for killing F. gigantica in vivo.

Animals↗
PubMed2002

Distribution of inorganic arsenic species in mine tailings of abandoned mines from Korea.

The main objective of the present study is to determine arsenic species in mine tailings by applying an ion exchange method. Three abandoned mines, Jingok, Cheonbo and Sino mines in Korea, which had produced mainly gold, were selected for the collection and analysis of the tailings. It was found that the arsenic speciation using an ion exchange method was effective to separate As(III) and As(V) in leachate of mine tailings. The concentration of As(V) was found to be 63-99% in the leachate, indicating that As(V) would be the major arsenic species in the mine tailings and the tailings were under oxic conditions. The total concentrations of arsenic and metal elements in the mine tailings were up to 62,350 mg/kg As, 40 wt.% Fe, 21,400 mg/kg Mn, and 7,850 mg/kg Al. Sulfate was the dominant anion throughout the leachate, reaching a maximum dissolved concentration of 734 mg/l. The results of XRD and SEM in the mine tailings showed that main arsenic-containing minerals were pyrite (FeS2) and arsenopyrite (FeAsS) which would be the source of arsenic contamination in the study area.

Adsorption↗
PubMed2002

Sequential extraction of sulfide-rich tailings remediated by the application of till cover, Kristineberg mine, northern Sweden.

A sequential extraction has been carried out on sulfide-rich mine tailings. The purpose was to investigate how elements released by oxidation are secondarily retained in the tailings and the possible consequences of the remediation. After investigating the solid tailings, seven samples were chosen for sequential extractions. Two samples were oxidised, situated just above the oxidation front; two samples from just below the former oxidation front with increased concentrations of several elements; two unoxidised samples were from an intermediate depth, and the deepest sample was from the tailings-peat boundary at the bottom of the impoundment. Five phases were extracted: adsorbed/exchangeable/carbonate; labile organics; amorphous Fe-oxyhydroxides/Mn-oxides; crystalline Fe-oxides; and organics/sulfides. The addition from dried porewater to the extracted fractions has been calculated and considered as minor. In the oxidised tailings, the sulfide fraction still dominates for elements such as Fe, S, Cd, Co, Cu, Hg and Zn, although the concentrations are low compared to the unoxidised tailings. Generally, the second most important fraction is the adsorbed/exchangeable/carbonate fraction. Below the oxidation front, the sulfide content of the tailings sharply increases. In the secondary enrichment zone, the total element concentrations increase compared with the deeper unoxidised samples, mainly due to secondary retention. For some elements, secondary retention is greater than the total amount extracted for the deeper unoxidised samples. In the secondary enrichment zone the adsorbed/exchangeable/carbonate fraction represents approximately 20 wt.% or more for Cd, Co, Mn, Ni and Zn. The amorphous iron oxyhydroxide or the crystalline iron oxide fractions are less important at this level, although for As, Ba and Cu the amorphous iron oxyhydroxide fraction represents up to 20 wt.%. At the lower border of the enrichment zone, the total concentration for most metals is lower, but the importance of the adsorbed/exchangeable/carbonate fraction is further enhanced for Cd, Cu, Ni and Zn. These elements have 35-60 wt.% of the total amount from this fraction. For As, Cd, Cu, Ni and Pb, the secondary fractions extracted (extractions A-D) represent between 60 and 80 wt.% of the total content. At greater depth in the impoundment the relative importance of the adsorbed/exchangeable/carbonate fraction decreases, whilst the importance of amorphous iron oxyhydroxide and crystalline iron oxide fractions increases. The adsorbed/exchangeable/carbonate fraction is the most easily remobilised fraction. A raised groundwater table previously situated below the enrichment zone may result in the release of secondarily retained metals.

Adsorption↗
PubMed2001

Colonization of mine tailings by marine invertebrates.

An experiment was conducted to determine if a tailings substrate would inhibit recolonization of benthic macrofauna upon closure of a submarine tailings disposal (STD) operation. Trays of defaunated marine sediment, serving as a reference, and trays of tailings from a proposed gold mine were placed at 21 m depth on the ocean floor to allow colonization via settlement from the water column. Trays of reference sediment and tailings, and cores of ambient sediment were collected 9, 17, and 22 months after tray placement. Probable tray effects, which were desirable given the objectives of this study, precluded direct comparison of ecological succession in the tray sediments to the ambient assemblage. The ambient macrofauna assemblage was distinguishable from the reference sediment and tailings assemblages throughout the experiment and displayed more pronounced seasonality. Differences between the reference sediment and tailings assemblages were generally insignificant, including total abundance, total biomass, number of taxa, average size of individuals, numerically dominant taxa, abundance by ecological guilds, and overall community composition. Upon cessation of STD, recolonization of a benthic macrofauna community should not be inhibited by the presence of these tailings as a benthic substrate.

Animals↗
PubMed1999

Synthesis of a single-tailed cationic lipid and investigation of its transfection.

Single-tailed cationic lipids were originally reported to have low transfection efficiency and high toxicity in plasmid delivery. We hypothesized that particular single-tailed cationic lipids may also function in plasmid transfection. To test this hypothesis, we synthesized a new cationic lipid-oleoyl ornithinate (OLON). To decrease cytotoxicity, we then introduced a potential biodegradable ester bond in the tail of lipid yielding 6-lauroxyhexyl ornithinate (LHON). The data demonstrated that the cytotoxicity of LHON was lower than that of 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP) or OLON. To investigate the transfection activity of the new lipids and determine the cellular uptake of DNA/liposome complexes, we compared the transfection of liposomes produced from double-tailed 1',2'-dioleyl-sn-glycero-3'-succinyl-1, 6-hexanediol ornithine conjugate (DOGSHDO) with an ornithine headgroup, single-tailed OLON with an ornithine head group, double-tailed DOTAP with quaternary amine group, and single-tailed cetyltrimethylammonium bromide (CTAB) with a quaternary amine group. At the optimal ratios as defined in transfection experiments, OLON/DOPE had more than 10 times the transgene expression than other liposomes even though the DNA uptake was not necessarily greater. In the experiments comparing the release of DNA from DNA/liposome complexes by anionic substances, a greater fraction of DNA was released from DNA/OLON/DOPE complexes than that from DNA/DOTAP/DOPE complexes.

Animals↗
PubMed2003

Rapid oxidation of sulfide mine tailings by reaction with potassium ferrate.

The chemistry of sulfide mine tailings treated with potassium ferrate (K2FeO4) in aqueous slurry has been investigated. The reaction system is believed to parallel a geochemical oxidation in which ferrate ion replaces oxygen. This chemical system utilized in a pipeline (as a plug flow reactor) may have application eliminating the potential for tailings to leach acid while recovering the metal from the tailings. Elemental analyses were performed using an ICP spectrometer for the aqueous phase extract of the treated tailings; and an SEM-EDX for the tailing solids. Solids were analyzed before and after treatments were applied. ICP shows that as the mass ratio of ferrate ion to tailings increases, the concentration of metals in the extract solution increases; while EDX indicates a corresponding decrease in sulfur content of the tailing solids. The extraction of metal and reduction in sulfide content is significant. The kinetic timeframe is on the order of minutes.

Chemical Precipitation↗
PubMed2001

The proximal and distal C-terminal tail domains of the CB1 cannabinoid receptor mediate G protein coupling.

The human CB1 cannabinoid receptor couples to G(i/o) proteins and inhibits neuronal voltage-gated Ca2+ channels. The role of the C-terminal tail of the CB1 cannabinoid receptor in G(i/o) protein coupling was examined using the superior cervical ganglion neuronal expression system. Deletion of the distal intracellular C-terminal tail (amino acids 418-472) slowed the kinetics and reduced the magnitude of Ca2+ channel inhibition. Deletion of the entire intracellular C-terminal tail (amino acids 401-472) abolished Ca2+ channel inhibition demonstrating the critical role of the proximal amino acids 401-417 of the C-terminal tail in G protein signaling. Expression of the C-terminal truncated receptors on the cell surface was examined using an N-terminal CB1 antibody. Both the C-terminal truncated receptors were expressed on the cell surface and were no different from wild type CB1 cannabinoid receptors. This study establishes that the proximal CB1 cannabinoid receptor intracellular C-terminal tail domain (amino acids 401-417) is critical for G(i/o) protein coupling and that the distal C-terminal tail domain (amino acids 418-472) profoundly modulates both the magnitude and kinetics of signal transduction. Thus, the C-terminal tail of the CB1 cannabinoid receptor has a wider role in G protein coupling than was previously thought.

Amino Acid Sequence↗
PubMed1997

Evaluation of the IITC tail cuff blood pressure recorder in the rat against intraarterial pressure according to criteria for human devices.

National standards govern the manufacture and marketing of medical devices in the United States, including those for indirect blood pressure measurement in man. There are no comparable standards for devices for recording in laboratory animals. Noninvasive tail cuff blood pressure (BP) recording in the rat is widely accepted, but beset by methodologic difficulties. Intraarterial recording is regarded as the "gold standard" but is invasive and also susceptible to methodologic error. We compared the IITC Mark 12 photoelectric/oscillometric tail cuff system (IITC Life Sciences, Woodland Hills, CA) versus simultaneous femoral intraarterial recordings in spontaneously hypertensive rats, during anesthesia and 1 to 2 days after recover (150 recordings under each condition), according to the guidelines for human data collection and analysis suggested the American National Standard for automated sphygmomanometers. Within- and between-observer disagreements in estimates made by two observers from 40 anesthetized recordings were less for intraarterial measurements than for the tail cuff method. Within-observer differences (mean +/- SD of differences [SDD]) for systolic, diastolic, and mean pressure were 0 +/- 1, 0 +/- 1, and 0 +/- 1 mm Hg for intraarterial versus -1 +/- 3, 0 +/- 8, and 0 +/- 5 mm Hg for tail cuff. Between-observer differences were 0 +/- 2, 0 +/- 1, and 6 +/- 2 mm Hg versus 5 +/- 4, 13 +/- 7, and 0 +/- 5 mm Hg, respectively. Differences between tail cuff and intraarterial methods were 16 +/- 13, -5 +/- 11, and 2 +/- 8 mm Hg in anesthetized animals and 8 +/- 14, -5 +/- 9, and 0 +/- 9 mm Hg in conscious animals (39% to 82% of differences exceeded 5 mm Hg). The upper limits of clinically acceptable disagreement in the American National Standard are: mean of 5 mm Hg, SDD of 8 mm Hg. The disagreement between tail cuff and intraarterial recordings cannot be ascribed to either method with certainty. These findings do not support the manufacturer's guarantee of tail-cuff readings within "5 mm Hg of intraarterial." Inaccuracy and unreliability of devices intended for laboratory animal use have considerable scientific, fiscal, and ethical implications. Marketing of these devices should also be governed by rigorous standards.

Anesthesia↗
PubMed2001

Dendritic organization of actin comet tails.

Polymerization of actin filaments is necessary for both protrusion of the leading edge of crawling cells and propulsion of certain intracellular pathogens, and it is sufficient for generating force for bacterial motility in vitro. Motile intracellular pathogens are associated with actin-rich comet tails containing many of the same molecular components present in lamellipodia, and this suggests that these two systems use a similar mechanism for motility. However, available structural evidence suggests that the organization of comet tails differs from that of lamellipodia. Actin filaments in lamellipodia form branched arrays, which are thought to arise by dendritic nucleation mediated by the Arp2/3 complex. In contrast, comet tails have been variously described as consisting of short, randomly oriented filaments, with a higher degree of alignment at the periphery, or as containing long, straight axial filaments with a small number of oblique filaments. Because the assembly of pathogen-associated comet tails has been used as a model system for lamellipodial protrusion, it is important to resolve this apparent discrepancy. Here, using a platinum replica approach, we show that actin filament arrays in comet tails in fact have a dendritic organization with the Arp2/3 complex localizing to Y-junctions as in lamellipodia. Thus, comet tails and lamellipodia appear to share a common dendritic nucleation mechanism for protrusive motility. However, comet tails differ from lamellipodia in that their actin filaments are usually twisted and appear to be under significant torsional stress.

Actins↗
PubMed1998

Poly(A)-tail-promoted translation in yeast: implications for translational control.

The cap structure and the poly(A) tail synergistically activate mRNA translation in vivo. Recent work using Saccharomyces cerevisiae spheroplasts and a yeast cell-free translation system revealed that the poly(A) tail can function as an independent promotor for ribosome recruitment, to internal initiation sites within an mRNA. This raises the question of how regulatory upstream open reading frames and translational repressor proteins binding to the 5'UTR can function, as well as how regulated polyadenylation can support faithful activation of protein synthesis. We investigated the function of the regulatory upstream open reading frame 4 from the yeast GCN 4 gene and the effect of IRP-1 binding to an iron-responsive element introduced into the 5' UTR of reporter mRNAs. Both manipulations effectively block cap-dependent translation, whereas ribosome recruitment promoted by the poly(A) tail under non-competitive conditions can efficiently bypass both blocks. We show that the synergistic use of both, the cap structure and the poly-A tail enforced by mRNA competition reinstates the full extent of translational control by both types of 5' UTR regulatory elements. With a view towards regulated polyadenylation, we studied the function of poly(A) tails of defined length on the translation of capped mRNAs. We find that poly(A) tail elongation increases translational efficiency, particularly under competitive conditions. Our results integrate recent findings on the function of the poly(A) tail into an understanding of translational control.

5' Untranslated Regions↗
PubMed1984

Differential dissociation of histone tails from core chromatin.

The dissociation of the trypsin-sensitive basic tails of the core histones in core chromatin has been followed as a function of [NaCl] using proton NMR spectroscopy. The tails dissociate in a highly cooperative all or none manner over the salt concentration range 0.2-0.6 M, that is, below the salt concentration required to dissociate the complete molecule. Assuming that each basic tail dissociates independently, the total number of salt linkages involved in binding the tails to DNA is 103. This equals the number of basic side chains in the tails of an octamer. The standard free energy of dissociation, delta G degree, in 1 M NaCl at 297 K is 3.6 kcal/mol. Temperature had no effect on the extent of dissociation up to 45 degrees C. However, between 45 and 65 degrees C, where the premelting transition in the core chromatin occurs, the tails dissociated completely. Dissociation of the tails was associated with a conformational transition in the DNA consistent with loss of supercoiling. From this, and the results of a previous study, it can be shown that the structured, trypsin-resistant domain of each core histone octamer makes 100 salt linkages to DNA. Thus, in 10 mM salt, each core octamer makes a total of 203 salt linkages to DNA.

Animals↗
PubMed2002

Stress-induced aggregation profiles of GST-alpha-synuclein fusion proteins: role of the C-terminal acidic tail of alpha-synuclein in protein thermosolubility and stability.

Alpha-synuclein is a well-known heat-resistant protein that does not aggregate upon heat treatment, whereas glutathione S-transferase (GST) is a heat-labile protein that easily precipitates as a result of thermal stress. This paper reports the role of the C-terminal acidic tail of alpha-synuclein in protein thermosolubility and stability. The region of alpha-synuclein that is responsible for the heat resistance was initially investigated using a series of deletion mutants, and the C-terminal acidic tail (residues 96-140) was found to be crucial for the thermosolubility of alpha-synuclein. The thermal behavior of the GST-alpha-synuclein fusion protein was next investigated, and the fusion protein was seen to be extremely heat-resistant. Using a series of GST-synuclein deletion mutants, the C-terminal acidic tail of alpha-synuclein was shown to play a critical role in conferring the heat resistance of the fusion proteins. Furthermore, the acidic tail appeared to protect the fusion protein from pH- and metal-induced protein aggregation, suggesting that the acidic tail can increase the virtual stability of the protein by protecting it from the aggregation induced by environmental stresses. Interestingly, the acidic tail also appeared to protect the GST enzyme from the thermal inactivation to a considerable extent. However, CD analysis of the heat-induced secondary structural changes of the GST-alpha-synuclein fusion protein revealed that the fusion protein is irreversibly denatured by heat treatment with a slightly lowered melting temperature (Tm). Thus, the results demonstrate that introducing an acidic tail into GST promotes the thermosolubility and virtual stability of the fusion protein, although it might be unfavorable for its intrinsic stability.

Base Sequence↗
PubMed2006

Calcium-triggered membrane interaction of the alpha-synuclein acidic tail.

Alpha-synuclein (alpha-syn) is a 140-residue protein that aggregates in intraneuronal inclusions called Lewy bodies in Parkinson's disease (PD). It is composed of an N-terminal domain with a propensity to bind lipids and a C-terminal domain rich in acidic residues (the acidic tail). The objective of this study was to examine the effect of Ca(2+) on the acidic tail conformation in lipid-bound alpha-syn. We exploit the extreme sensitivity of the band III fluorescence emission peak of the pyrene fluorophore to the polarity of its microenvironment to monitor subtle conformational response of the alpha-syn acidic tail to Ca(2+). Using recombinant human alpha-syn bearing a pyrene to probe either the N-terminal domain or the acidic tail, we noted that lipid binding resulted in an increase in band III emission intensity in the pyrene probe tagging the N-terminal domain but not that in the acidic tail. This suggests that the protein is anchored to the lipid surface via the N-terminal domain. However, addition of Ca(2+) caused an increase in band III emission intensity in the pyrene tagging the acidic tail, with a corresponding increased susceptibility to quenching by quenchers located in the lipid milieu, indicative of lipid interaction of this domain. Taken together with the increased beta-sheet content of membrane-associated alpha-syn in the presence of Ca(2+), we propose a model wherein initial lipid interaction occurs via the N-terminal domain, followed by a Ca(2+)-triggered membrane association of the acidic tail as a potential mechanism leading to alpha-syn aggregation. These observations have direct implications in the role of age-related oxidative stress and the attendant cellular Ca(2+) dysregulation as critical factors in alpha-syn aggregation in PD.

Adenosine↗
PubMed1998

Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase.

The hydrophobic isoprene tail of ubiquinone-2 (Q2) exihibits binding specificity in redox reactions with bovine heart mitochondrial complex I (Ohshima, M., Miyoshi, H., Sakamoto, K., Takegami, K., Iwata, J., Kuwabara, K., Iwamura, H., and Yagi, T. (1998) Biochemistry 37, 6436-6445) and the Escherichia coli bo-type ubiquinol oxidase (Sakamoto, K., Miyoshi, H., Takegami, K., Mogi, T., Anraku, Y., and Iwamura, H. (1996) J. Biol. Chem. 271, 29897-29902). To identify the structural factor(s) of the diprenyl tail of Q2 governing the specific interaction with these enzymes, we synthesized a series of novel Q2 analogues in which only one of the structural factors of the diprenyl tail was systematically modified. In bovine complex I, the presence of the methyl branch and the pi-electron system in the first isoprene unit are responsible for high-affinity binding of Q2 to the ubiquinone reduction site, which results in a low Km and kcat values of Q2 reduction. The position of the methyl group in the tail is strictly recognized by the enzyme. In contrast to complex I, in bo-type ubiquinol oxidase, either of the two pi-electron systems in the tail is required for high-affinity binding of Q2H2 to the enzyme, while the presence of the methyl branch and the location of the pi-electron systems are not strictly recognized by the enzyme. We concluded that the role of the ubiquinone tail is not simply the enhancement of the hydrophobicity of the molecule and that molecular recognition of the tail by the quinone redox site differs among the respiratory enzymes.

Animals↗
PubMed2003

The effect of natrojarosite addition to mine tailings.

An increasingly common practice for metallurgical plants is to discard their wastes by combining them with mine tailings prior to disposing the blended material to a containment facility. This practice has occurred since 1985 at the Kidd Creek tailings impoundment where natrojarosite, a waste produced from the adjacent Zn refinery, is combined with mine tailings and is deposited in a single impoundment. To assess the environmental impact of the co-disposal, a laboratory column experiment was conducted. The column material was flotation tailings from the Kidd Creek site containing 3 wt % natrojarosite residue. Dilute sulfuric acid was passed through the column to simulate the acid generated in the unsaturated zone of the tailings impoundment. The results of this experiment were compared to the results of a previous experiment conducted on unamended flotation tailings. The results showed that the effluent from the column containing the natrojarosite-bearing mixture had a faster decrease in pH, earlier increases in the concentrations of dissolved metals such as Pb and Cd, and a greater persistence in effluent metal concentrations such as Pb, Zn and Ni. To prevent the observed enhanced release of dissolved metals from mine waste disposal areas, natrojarosite should not be co-disposed with tailings.

Chemical Precipitation↗
PubMed2006

Element flows associated with marine shore mine tailings deposits.

From 1938 until 1975, flotation tailings from the Potrerillos--El Salvador mining district (porphyry copper deposits) were discharged into the El Salado valley and transported in suspension to the sea at Chaliaral Bay, Atacama Desert, northern Chile. Over 220 Mt of tailings, averaging 0.8 +/- 0.25 wt % of pyrite, were deposited into the bay, resulting in over a 1 kilometer seaward displacement of the shoreline and an estimated 10-15 m thick tailings accumulation covering a approximately 4 km2 surface area. The Chaniaral case was classified by the United Nations Environmental Programme (UNEP) in 1983 as one of the most serious cases of marine contamination in the Pacific area. Since 1975, the tailings have been exposed to oxidation, resulting in a 70-188 cm thick low-pH (2.6-4) oxidation zone at the top with liberation of divalent metal cations, such as Cu2+, Ni2+, and Zn2+ (up to 2265 mg/L, 18.1 mg/L, and 20.3 mg/ L, respectively). Evaporation-induced transport capillarity led to metal enrichment atthe tailings surface (e.g. up to 2.4% Cu) in the form of secondary chlorides and/or sulfates (dominated by eriochalcite [CuCl.H2O] and halite). These, mainly water-soluble, secondary minerals were exposed to eolian transport in the direction of the Village of Chañaral by the predominant W-SW winds. Two element-flow directions (toward the tailings surface, via capillarity, and toward the sea) and two element groups with different geochemical behaviors (cations such as Cu, Zn, Ni, and oxyanions such as As and Mo) could be distinguished. It can be postulated, that the sea is mainly affected by the following: As, Mo, Cu, and Zn contamination, which were liberated from the oxidation zone from the tailings and mobilized through the tidal cycle, and by Cu and Zn from the subsurface waters flowing in the El Salado valley (up to 19 mg/L and 12 mg/L Zn, respectively), transported as chloro complexes at neutral pH.

El Salvador↗
PubMed2001

Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes.

A class of integral membrane proteins, referred to as 'tail-anchored proteins', are inserted into phospholipid bilayers via a single segment of hydrophobic amino acids at the C-terminus, thereby displaying a large functional domain in the cytosol. This membrane attachment strategy allows eukaryotic cells to position a wide range of cytoplasmic activities close to the surface of an intracellular membrane. Tail-anchored proteins often, but not always, demonstrate a selective distribution to specific intracellular organelles. This membrane-specific distribution is required for the large number of targeting proteins that are tail-anchored, but may or may not be critical for the numerous tail-anchored pro-apoptotic and anti-apoptotic proteins of the Bcl-2 family. Recent work has begun to address the mechanism for targeting tail-anchored proteins to their resident membranes, but questions remain. What targeting signals determine each protein's intracellular location? Are there receptors for these signals and, if so, how do they function? What steps are required to integrate tail-anchored proteins into the phospholipid bilayers? In this Traffic interchange, we summarise what is known about tail-anchored proteins, and outline the areas that are currently under study.

Endoplasmic Reticulum↗