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Topic: Lipid anchored protein

Related Topics

GPI anchor

Isoprenylation

Membrane protein

Peripheral membrane protein

Integral membrane protein

Biological membrane

G protein

Lipid

Signal transduction

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	Igal Szleifer Research Group - Biophysics of Lipids
		Spontaneous liposome formation and stability in mitures of lipids with pegolated lipids: The goal in this project is to understand the conditions necessary for the formation and stability of spherical liposomes formed by mixtures of lipids with lipids conjugated with PEG (poly ethylene glycol).
		We have found that the addition of hydrophobic-hydrophilic block copolymers to a dilute lipid monolayer results in the clustering of the lipid that tend to be organized in well-ordered domains.
		We predict liquid-liquid coexistence due to differences in lipid and cholesterol packing that may be related to the presence of rafts in biological membranes.
	www.chem.purdue.edu /igal/biophysics_lipids.html (417 words)

	* Lipid - (Biology): Definition
		Lipids are a class of hydrocarbon-containing organic compounds essential for the structure and function of living cells.
		Proteins may be modified in a wide variety of ways, including phosphorylation (addition or a phosphate group), adenylation (addition of an adenine group), glycosylation (addition of a sugar group), acylation (addition of a lipid group),...
		Anchor Sequence: A hydrophobic amino acid sequence which fixes a segment of a newly synthesized, translocating protein within the lipid bilayer membrane of the endoplasmic reticulum.
	en.mimi.hu /biology/lipid.html (769 words)

	February 23, 1995
		lipid bilayer with polar "head" groups at surface and hydrophobic "tails" internal
		polar solutes; lining is either an integral protein or an ionophore; may or may not be gated (ligand or voltage) (terminology "pore" used principally in reference to
		solute binds to a protein; a conformational change occurs; and the solute is subsequently released on the other side of the membrane
	www.uky.edu /Classes/BCH/401/Watt/Chapter12/chapter12.htm (380 words)

	Trotter Group
		Multiple Sclerosis), the migration of neural tumours and the missorting of glial proteins and lipids in the pathology of human disease.
		In maturing oligodendrocytes, the glycosylphosphatidylinositol-anchored proteins F3 and NCAM 120 associate with the intracellular tyrosine kinase Fyn and the myelin lipids cholesterol and glycosphingolipids in detergent-resistant "rafts".
		The generation of the myelin sheath involves the seIective targeting to and exclusion of distinct proteins and lipids to the specialised subdomains of myelin: e.g.
	www.izn.uni-heidelberg.de /e/profiles/trotter.html (805 words)

	Membrane Proteins; Posttranslational Processing
		When a protein is synthesized and exposes a glycosylation sequence in the lumen of the ER (which is asn-X-ser or asn-X-thr), then an enzyme, oligosaccharyl transferase, moves the whole 14-sugar oligosaccharide unit from the glycolipid to the glycoprotein.
		In these cases the protein, anchored in the membrane by its signal sequence, is cleaved by an enzyme that breaks the peptide chain, then reforms an amide bond with the lipid.
		The protein remains anchored to the membrane by the lipid, rather than by its own signal sequence, but it is readily released by an enzyme, called phospholipase C, that cuts between the diglycerol phosphate (phosphatide) and the inositol bond.
	www.lclark.edu /~reiness/cellbio/lectures/lect16.htm (2014 words)

	Lipid anchored protein - Biocrawler (Site not responding. Last check: )
		In lipid anchored proteins, a covalently attached fatty acid such as palmitate or myristate serves to anchor them to the cytoplasmic face of the cell membrane.
		It is believed that the fatty acid chain inserts and assumes a place in the bilayer structure of the membrane alongside the similar fatty-acid tails of the surrounding lipid molecules.
		Prenylation is the attachment of lipid chains to proteins to facilitate their interaction with the cell membrane.
	www.biocrawler.com /encyclopedia/Lipid_anchored_protein (136 words)

	NationMaster - Encyclopedia: Prenylation
		Prenylation or isoprenylation is the addition of hydrophobic molecules to a protein to facilitate its attachment to the cell membrane.
		Prenylation or isoprenylation or lipidation is the addition of hydrophobic molecules to a protein.
		After Glomset, Gelb, and colleagues had demonstrated the structure of these prenyl groups, researchers elsewhere found that a certain type of protein responsible for cellular switching and growth functions, called the "ras" protein, has a farnesyl group attached to it which is critical to the function of the protein.
	www.nationmaster.com /encyclopedia/Prenylation (278 words)

	lateral pressure profile: description of mechanism of protein modulation
		The activity of the protein, i.e., the distribution of its conformational states (both in the absence and the presence of the stimulus) is often strongly affected by the molecular composition of the bilayer in which it is anchored.
		The underlying interactions between bilayer components (lipids or other membrane-soluble molecules) and proteins can be distinguished on the basis of "specificity": the former can influence the latter either through direct binding to localized protein sites, or indirectly, by altering the structural, thermodynamic or dynamic properties of the bilayer, which in turn modulates protein behavior.
		Whereas small variations in lipid composition can influence protein activity significantly, the accompanying changes in membrane structural properties such as thickness are typically small, although it has been argued that relatively small changes in thickness can have a significant effect on protein equilibria.
	www.dartmouth.edu /~rcantor/lpp.html (1861 words)

	Membrane protein-lipid interactions
		Integral membrane proteins have a membrane spanning region that is characterized by the presence of predominantly hydrophobic residues.
		While the basic structure of biomembranes involves a lipid bilayer, it has been shown to be essential for proper membrane function for the lipids to remain motionally dynamic and have a certain tendency to favor a non-bilayer conformation.
		The PE lipids have a headgroup that is relatively small compared to the volume/area that the hydrophobic acyl chains occupy, giving them a propensity to form inverted hexagonal phases, said to have a negative curvature.
	web.mit.edu /pcavdwel/www/membrane.html (939 words)

	Phosphatidylinositol and related lipids: structure, composition, biochemistry, and analysis
		Phosphatidylinositol is an important lipid, both as a key membrane constituent and as a participant in essential metabolic processes in all plants and animals (and in some bacteria (actinomycetes)), both directly and via a number of metabolites.
		The proteins all contain a characteristic carboxyl-terminal signal peptide with a hydrophobic tail, which is split off before the protein with a new carboxyl-terminal is combined with the amino group of the ethanolamine residue of the GPI moiety.
		Key lipids are phosphatidylinositol mannosides, with the first mannose residue attached to the 2-hydroxyl group and the second to the 6-hydroxyl of myo-inositol, which are found in the cell walls of Mycobacteria and related bacterial species.
	www.lipidlibrary.co.uk /Lipids/pi (2915 words)

	Post-Translational Modifications
		Proteins that are membrane bound or are destined for excretion are synthesized by ribosomes associated with the membranes of the endoplasmic reticulum (ER).
		Membrane associated carbohydrate is exclusively in the form of oliogsaccharides covalently attached to proteins forming glycoproteins, and to a lesser extent covalently attached to lipid forming the glycolipids.
		The protein component of all glycoproteins is synthesized from polyribosomes that are bound to the endoplasmic reticulum (ER).
	www.indstate.edu /thcme/mwking/protein-modifications.html (3869 words)

	The membrane and lipids as integral participants in signal transduction: lipid signal transduction for the non-lipid ...
		and lipids are the substrates of lipid kinases and lipid phosphatases.
		Integral membrane proteins are embedded in the lipid bilayer
		the composition of the lipid rafts and the fluidity of the membranes
	advan.physiology.org /cgi/content/full/31/1/5 (6511 words)

	Cellular Component Ontology Guidelines
		GO distinguishes single and double membranes surrounding organelles: an organelle envelope is defined as two lipid bilayers plus the space, or lumen, between them, whereas an organelle membrane is defined as a single bilayer.
		The region between the inner and outer lipid bilayers of the
		The cellular component ontology does not include terms for type I, II, etc., membrane proteins, because these classifications are not locations, but instead describe a different feature of the proteins, namely topological orientation with respect to the membrane and other cellular components.
	www.geneontology.org /GO.component.guidelines.shtml (927 words)

	Science/AAAS \| Science's STKE: Community: Forums: Lipid Rafts: Real or Artifact?
		This controversy is driven, at least in part, by the fact that most characterization of lipid rafts involves the disruption of membranes and by uncertainties about the effects of probes, such as antibodies or toxins, on the organization of raft components in intact membranes.
		A consideration of the size and stability of pure lipid domains,mainly defined in liposomes, suggests that lipid rafts in native membranes are likely to be small (consisting of a few hundred to a few thousand lipid molecules) and transient, unless stabilized by proteins (1).
		One approach is to observe the random or directed motion of membrane lipids and lipid-anchored proteins in the plane of the bilayer.
	stke.sciencemag.org /cgi/forum-display/short/stke_el;50?rss=1 (1332 words)

	Protein Spotlight Issue 69: Nerve regrowth: nipped by a no-go
		Nogo-66 receptor is a lipid-anchored protein found in the membrane of the axon, which transduces the no-go signal to the axon and stymies its efforts to sprout.
		Protein Spotlight (ISSN 1424-4721) is a monthly review written by the Swiss-Prot team of the Swiss Institute of Bioinformatics.
		Protein Spotlight (ISSN 1424-4721) is published by the Swiss-Prot group at the Swiss Institute of Bioinformatics (SIB).
	www.expasy.org /spotlight/back_issues/sptlt069.shtml (1409 words)

	The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical axons - Nature Neuroscience
		Netrin-G1 is a lipid-anchored protein that is structurally related to the netrin family of axon guidance molecules.
		The resultant fusion proteins were expressed and used in assays to test for binding to about 400 putative cell-surface human proteins that were transiently expressed in COS7 cells.
		Protein complexes were pulled down with protein A−conjugated beads (Pierce) by standard procedures (see Supplementary Methods online for details).
	www.nature.com /uidfinder/10.1038/nn1148 (5315 words)

	A Unified Model for Signal Transduction Reactions in Cellular Membranes -- Haugh 82 (2): 591 -- Biophysical Journal
		lipid modifications, and its nucleotide-binding state is regulated
		I PI 3-kinases are enzymes that modify a common lipid substrate,
		a fraction of the transfer protein is engaged by activated receptors,
	www.biophysj.org /cgi/content/full/82/2/591 (4699 words)

	Biology4Kids.com: Cell Structure: Membrane Proteins
		Peripheral proteins are not bonded as strongly to the membrane.
		This structure of the membrane with embedded proteins and a lipid bilayer was discovered in the early 1970's.
		They identified the proteins that sat on the surface, were sunk into the membrane, and the others that crossed the membrane.
	www.biology4kids.com /files/cell_membprot.html (332 words)

	Deborah A. Brown
		Lipids such as sphingolipids, which have long, saturated acyl chains, partition preferentially into these ordered domains and are enriched in rafts.
		A number of proteins that are modified with saturated acyl chains (including glycosyl phosphatidylinositol (GPI)-anchored proteins, myristoylated, and palmitoylated proteins) are enriched in rafts.
		Association of these proteins with rafts is likely to be important in function, as has already been shown for the Src-family kinase Lck in T cells.
	www.sunysb.edu /biochem/BIOCHEM/facultypages/brown (1176 words)

	Artificially Lipid-anchored Proteins Can Elicit Clustering-induced Intracellular Signaling Events in Jurkat ...
		4, and the relative level of cell-bound streptavidin (normalized to sample protein content) was measured for a replicate aliquot by anti-streptavidin immunoblotting and densitometry.
		conjugates with a saturated dipalmitoyl anchor or a tetraunsaturated
		conjugates with saturated or polyunsaturated lipid anchors induce
	www.jbc.org /cgi/content/full/280/24/22839 (5200 words)

	Prion Replication Alters the Distribution of Synaptophysin and Caveolin 1 in Neuronal Lipid Rafts -- ...
		Total protein content in different fractions of the sucrose gradient was measured by silver staining of the gels from samples obtained from retinas (A) and optic nerves (B) of controls and scrapie-infected animals at advanced stages of the disease.
		of proteins or with a drastic perturbation in the biochemical
		as caveolin 1 and synaptophysin from this subset of lipid rafts,
	ajp.amjpathol.org /cgi/content/full/165/5/1839 (6009 words)

	BB 350 Oregon State University
		Highlights Lipids II Cellular membranes are sensitive to temperature.
		We categorize membrane proteins as integral (firmly embedded in both portions of a lipid bilayer), peripheral (embedded in only one portion of the lipid bilayer), or associated (not embedded in the lipid bilayer at all, but found close to it.
		Carbohydrates (sugar compounds) have links to components in a lipid bilayer in an orientation-specific direction - all carbohydrates are located on the portion of the lipid bilayer that is on the outside of the cell.
	oregonstate.edu /instruction/bb350/highlightslipids2.html (809 words)

	Post-Translational Modifications
		Proteins that are membrane bound or are destined for excretion are synthesized by ribosomes associated with the membranes of the endoplasmic reticulum (ER).
		Membrane associated carbohydrate is exclusively in the form of oliogsaccharides covalently attached to proteins forming glycoproteins, and to a lesser extent covalently attached to lipid forming the glycolipids.
		The protein component of all glycoproteins is synthesized from polyribosomes that are bound to the endoplasmic reticulum (ER).
	web.indstate.edu /thcme/mwking/protein-modifications.html (3869 words)

	Synthesis and structural characterization of a mimetic membrane-anchored prion protein -- Hicks et al. 273 (6): 1285 -- ... (Site not responding. Last check: )
		Lipid was visible in fractions 1–3 for POPC (A, B) and in fraction 3 for raft lipids (C, D).
		from unmodified protein on a water/acetonitrile gradient in
		Sanghera N and Pinheiro TJ (2002) Binding of prion protein to lipid membranes and implications for prion conversion.
	content.febsjournal.org /cgi/content/full/273/6/1285 (6428 words)

	UniGE - Department of biochemistry - Reika Watanabe
		Proteins of different characteristics and structures must exit from the ER to reach their final destination.
		GPI-anchored proteins are known to be transported from ER to the Golgi in the separate vesicles from other secretory proteins in yeast.
		GPI-anchored proteins have been shown to have specific interactions with sphingolipid and sterol within membranes and this interaction might be crucial for their intracellular transport.
	www.unige.ch /sciences/biochimie/Research/Watanabe.html (1034 words)

	GPI Proteins
		All GPI-anchored proteins are initially synthesized with a transmembrane anchor, but after translocation across the membrane of the endoplasmic reticulum, the ecto-domain of the protein is cleaved and covalently linked to a preformed GPI anchor by a specific transamidase enzyme.
		The GPI anchor is composed of a core structure of phosphatidylinositol attached to a glycan chain which, in turn, is attached to the C-terminus of the protein.
		Addition of a glycolipid anchor to a nascent protein requires a C-terminal hydrophobic signal sequence on the protein which is rapidly exchanged for a pre-assembled anchor.
	www.cyber-dyne.com /~tom/gpi.html (3435 words)

	Lipids & Membranes
		The data are from a crystal structure of the lipid bound to a protein, PDB 1T27, solved by M. Yoder, L. Thomas, J. Tremblay, R. Oliver, L. Yarbrough and G. Helmkamp in 2001.
		is a protein associated with the cytosolic leaflet of the plasma membrane in caveolae.
		Degradation of a protein segment would indicate exposure to the aqueous phase on the side of the membrane to which the protease was added.
	www.rpi.edu /dept/bcbp/molbiochem/MBWeb/mb1/part2/lipid.htm (1942 words)

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