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Chatterjee and P. Sharma and other members of the laboratory for their invaluable contributions to this review. Research in H. You can also search for this author in PubMed Google Scholar. Paroxysmal nocturnal haemoglobinuria. Compounds that are derived from isoprene 2-methylbuta-1,3-diene linked together in head-to-tail or tail-to-tail conformations and that comprise farnesyl and geranylgeranyl molecules that are used in the covalent modification of proteins on cysteine residues.
Nine interacting serum proteins C1—C9 — which are mostly enzymes — that are activated in a coordinated way and participate in bacterial lysis and macrophage chemotaxis. Molecules that form a proteinaceous coating around vesicles that are used in membrane trafficking. They are believed to be important for vesicle formation and recruitment of cargo into the forming vesicles. FRET will only occur between fluorophores in which the emission spectrum of the donor has a significant overlap with the excitation of the acceptor.
N -ethylmaleimide-sensitive fusion protein. NSF was originally isolated because of its requirement for vesicle fusion in vitro. A protein complex that is conserved from yeast to mammalian cells and is found on the Golgi compartment. Its precise function is not yet known, but it seems to be important for various steps of membrane trafficking to, and through, the Golgi.
SNARE proteins have been implicated as determinants of the specific fusion of vesicles with target membranes. Carbohydrate molecules that are linked to asparagine moieties in proteins. They have several possible structures and are built on a common core structure that is composed of N -acetylglucosamine and mannoses. The first vesicle coat protein to be identified. It is involved in membrane traffic to, and through, the endocytic pathway.
A high-molecular-weight GTPase that is thought to be involved in the 'pinching off' of vesicles from membranes. Small plasma-membrane invaginations that occur in many cell types, in particular in endothelial cells.
Caveolae are usually coated with a protein of the caveolin family. A bacterial surface glycolipid that is often a primary antigen and effector during bacterial infections. Blood cells, particularly of insects and crustacea.
They are similar in many respects to leukocytes, as they are phagocytic and are not involved in oxygen transport. Small Ras-like GTPase molecules that are implicated in regulating membrane-trafficking dynamics by recruiting effector molecules. GPI-anchored-protein-enriched early endosomal compartments. It accounts for a main fraction of the fluid phase of the endocytic content, and is formed independently of dynamin function. Reprints and Permissions.
Sorting GPI-anchored proteins. Nat Rev Mol Cell Biol 5, — Download citation. Issue Date : 01 February Anyone you share the following link with will be able to read this content:. Sorry, a shareable link is not currently available for this article. Provided by the Springer Nature SharedIt content-sharing initiative. Microbial Cell Factories Nature Communications Scientific Reports Abrash, E.
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We have prepd. The ability to form PrPSc in transgenic mice is retained by a residue "mini-prion" PrP , with the deletions and A single reversed-phase purifn. With respect to its conformational and aggregational properties and its response to proteinase digestion, sPrP was indistinguishable from its recombinant analog rPrP Certain sequences that proved to be more difficult to synthesize using the Fmoc approach, such as bovine Bo PrP , were successfully prepd.
To mimic the glycosylphosphatidyl inositol GPI anchor and target sPrP to cholesterol-rich domains on the cell surface, where the conversion of PrPC is believed to occur, a lipophilic group or biotin, was added to an orthogonally side-chain-protected Lys residue at the C-terminus of sPrP sequences.
The chem. Conversion of cellular prion protein PrPC into the pathol. However, due to inherent difficulties of expressing and purifying posttranslationally modified rPrP variants, only a limited amt.
PrP and its behavior in vitro and in vivo. Here, we present an alternative route to access lipidated mouse rPrP rPrPPalm via two semisynthetic strategies. These rPrP variants studied by a variety of in vitro methods exhibited a high affinity for liposomes and a lower tendency for aggregation than rPrP.
In vivo studies demonstrated that double-lipidated rPrP is efficiently taken up into the membranes of mouse neuronal and human epithelial kidney cells. These latter results enable expts. Paulick, Margot G. National Academy of Sciences. The glycosylphosphatidylinositol GPI anchor is a C-terminal posttranslational modification found on many eukaryotic proteins that reside in the outer leaflet of the cell membrane.
The complex and diverse structures of GPI anchors suggest a rich spectrum of biol. The authors previously synthesized a series of GPI anchor analogs with systematic deletions within the glycan core and coupled them to the GFP by a combination of expressed protein ligation and native chem. Here the authors investigate the behavior of these GPI-protein analogs in living cells.
These modified proteins integrated into the plasma membranes of a variety of mammalian cells and were internalized and directed to recycling endosomes similarly to GFP bearing a native GPI anchor. The GPI-protein analogs also diffused freely in cellular membranes. However, changes in the glycan structure significantly affected membrane mobility, with the loss of monosaccharide units correlating to decreased diffusion.
Thus, this cellular system provides a platform for dissecting the contributions of various GPI anchor components to their biol. Protein Pept. Bentham Science Publishers Ltd. In living cells, membrane proteins are essential to signal transduction, nutrient use, and energy exchange between the cell and environment.
Due to challenges in protein expression, purifn. This review describes recent advances in soln. NMR allowing the study of a select set of peripheral and integral membrane proteins.
These structural studies are possible due to solubilization of the proteins in membrane-mimetic constructs such as detergent micelles and bicelles. These examples illustrate the unique role soln. NMR spectroscopy plays in structural biol. Cited By. This article is cited by publications.
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Comparative transcriptome analysis of short-term responses to salt and glycerol hyperosmotic stress in the green alga Dunaliella salina. Algal Research , 53 , Metabolites , 11 2 , Proceedings of the National Academy of Sciences , 2 , e What do they do? Can we gain any insights into my protein of interest — PrP — by learning more about this class of proteins it is a member of? These mostly covered the structure and biogenesis of the GPI anchor itself, about which an amazing about is known.
The core sugar backbone is conserved, but the side chains branching off of it can vary, and the phosholipid head group and fatty acids can both vary as well. Every chemical structure I have found of GPI anchors has at least some parts abbreviated or summarized, and the protein is usually just shown as a picture. I wanted to get a sense of what these anchors actually look like chemically, in the context of their attached proteins, so I set out to actually draw one complete structure in ChemDraw.
The molecular weight came to 1, Da, so for context I drew in the final 16 residues of HuPrP, which weigh in comparably, at 1, Da.
In many cases, a gene has multiple isoforms, with one splicing product giving rise to a GPI-anchored protein while others give rise to secreted or transmembrane forms. The most fascinating story here is that of the mouse gene Ly6a which, thanks to a genetic polymorphism, is GPI-anchored in some mouse strains and not others.
Most of the biosynthesis takes place with the anchor inserted in the membrane in the ER but not attached to any protein. In fact, the first few steps take place on the cytosolic leaflet of the membrane, and only later does the anchor flip to the lumenal side inside the ER.
There is then further maturation of the GPI anchor as the protein migrates out of the ER toward the cell surface.
I looked and looked for a sequence logo of what amino acid sequence motif GPI transamidase recognizes, but found none. Apparently the sequence motif is quite loose [ Eisenhaber ], and apparently the GPI signals are not even homologous [ Englund ], meaning they did not evolve from a common ancestral sequence, but rather evolved convergently, to the extent that there is even any convergence.
PrP loosely follows this motif. According to published structures [e. Sonia found an excellent paper from a few years ago where they did a mutagenesis screen in haploid human cells to identify genes required for biogenesis of two GPI-anchored proteins: PrP and CD59 [ Davis ].
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