Synonyms for latrophilin or Related words with latrophilin

receptorfamily              coupledreceptor              transmebrane              superfamilymember              familymember              zincfinger              subfamilyb              plexin              cxcmotif              chimaerin              tetraspan              receptorprotein              haemopoietin              attractin              highaffinity              ankyrinrepeat              glypican              foxa              receptoralpha              baccessioncytokines              allatostatin              areceptor              domaincontaining              neurofascin              transmenbrane              interactingprotein              subfamilya              dickkopf              neuropilins              paqr              monocytechemotactic              receptorassociated              domainreceptor              decysin              stabilin              emilin              protocadherin              withthrombospondin              myoferlin              meprin              tintegral              repeatproteins              repeatdomain              mshhomeo              betareceptor              semaphorin              proteinwith              meltrin              spondin              calciumchannel             



Examples of "latrophilin"
Latrophilin 2 is a protein that in humans is encoded by the "ADGRL2" gene.
Latrophilin 3 is a protein that in humans is encoded by the "ADGRL3" gene.
EGF, latrophilin and seven transmembrane domain-containing protein 1 is a latrophilin-like orphan receptor of the adhesion G protein-coupled receptor family. In humans this protein is encoded by the "ELTD1" gene. ELTD1 appears to have a role in angiogenesis, both physiological and pathological, as well as glioblastoma.
The toxin stimulates a receptor, most likely latrophilin, which is a G-protein coupled receptor linked to Gαq/11. The downstream effector of Gαq/11 is phospholipase C (PLC).When activated PLC increases the cytosolic concentration of IP3, which in turn induces release of Ca from intracellular stores. This rise in cytosolic Ca may increase the probability of release and the rate of spontaneous exocytosis. Latrophilin with α-LTX can induce the activation of Protein Kinase C (PKC). PKC is responsible for the phosphorylation of SNARE proteins. Thus latrophilin with α-LTX induces the effect of exocytosis of transport vesicles. The exact mechanism has to be discovered.
As well as the major effects of α-latrotoxin pore formation, other effects of α-latrotoxin are mediated by interaction with latrophilin and intracellular signalling (see signal transduction).
The precise functions of latrophilins remain unknown. Genetic defects in latrophilin genes have been associated with diseases such as attention-deficit hyperactivity disorder and cancer.
The base of the tetramer (below the wings) is 45 Å deep and is hydrophobic, which mediates insertion into the cell membrane. Also insertion of the tetramer is only possible in presence of certain receptors (mainly neurexin Iα and latrophilin and PTPσ in a minor extent) on the membrane. Neurexin Iα only mediates insertion under presence of Ca, whereas latrophilin and PTPσ can mediate insertion without presence of Ca. So because of the channel and the insertion in the cell membrane the protein makes the cell more permeable to substances that can pass through the channel. These substances are mono- and bivalent cations, neurotransmitters, fluorescent dyes and ATP.
This gene encodes a member of the latrophilin subfamily of G protein-coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. Latrophilin-1 has been shown to recruit the neurotoxin from black widow spider venom, alpha-latrotoxin, to the synapse plasma membrane.
Which out of Latrophilin receptors and BK-potassium channels is emodepside’s primary site of action remains to be completely deduced. Both LAT-1/LAT-2 and slo-1 mutants (reduction/loss of function) show significant resistance to emodepside with it being conceivable that the presence of both is required for emodepside to induce its full effect.
Latrophilin 1 is a protein that in humans is encoded by the "ADGRL1" gene. It is a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
Mutational studies involving LAT-1 knockout and LAT-2 gene deletion mutants have revealed that the role of latrophilin receptors in the different tissues that they are expressed differs between subtypes, with LAT-1 being expressed in the pharynx of C.elegans (thereby modulating pharyngeal pumping) and LAT-2 having a role in locomotion.
The latrophilin homolog LPHN1 was shown in "C. elegans" to require a GPS for signaling, but cleavage at the GPS site was not necessary. Furthermore, having a shortened 7 transmembrane domain, but with an intact GPS domain, resulted in a loss of signaling. This suggests that having both the GPS and 7 transmembrane domain intact is involved in signaling and that the GPS site could act as or be a necessary part of an endogenous ligand.
The mechanism by which activation of UNC-13 results in neurotransmitter release (the ultimate result of latrophilin activation) is through interaction with the synaptosomal membrane protein syntaxin, with UNC-13 binding to the N-terminus of syntaxin and promoting the switch from the closed form of syntaxin (which is incompatible with SNARE complex synaptobrevin, SNAP-25 and syntaxin formation) to its open formation so that SNARE complex formation can be achieved, thereby allowing vesicle fusion and release to take place.
This gene encodes a member of the latrophilin subfamily of G protein-coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane.
This gene encodes a member of the latrophilin subfamily of G-protein coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. While several transcript variants have been described, the biological validity of only one has been determined.
The protein product of GPR113 gene is a G-protein coupled receptor. The protein has three transcript variants in humans. Of these three, GPR113 Variant 1 has the longest amino acid sequence, and has the highest identity to orthologs. This leads to the conclusion that GPR113 Variant 1 is the homo sapiens descendent of the ancestral GPR113 gene. GPR113 Var 1 contains 1079 Amino Acids, and is integral to the plasma membrane. The 7-pass receptor contains 4 domains highlighted in the figure at right: Signal Peptide (Red), Hormone Receptor Domain (Blue), Latrophilin/CL-1-like GPS domain (Orange), and the 7-transmembrane receptor (Purple). Between the Hormone Receptor Domain and the GPS is a Domain of unknown function that is not highlighted.
Once the tetramer is inserted into the cell membrane, two mechanism of actions can occur. First, insertion may lead to pore formation and possibly other effects, and second, the receptor may be activated, which leads to intracellular signaling. The four heads of the tetramer form a bowl surrounding the pore, which is restricted at one point to 10 Å. Millimolar concentrations of Ca and Mg strongly catalyses tetramer formation, suggesting that the tetrametric state is divalent cation-dependent, while EDTA favours formation of the dimer. Research also shows that concentrations of La higher than 100 µM also block tetramerisation. Pore formation can occur in pure lipid membranes, but reconstituted receptors greatly increase pore formation. Biological membranes block pore formation when no α-LTX receptors are present (neurexin, latrophilin, PTPσ). It is also known that the three highly conserved cysteine residues are involved with α-LTX receptor binding, because mutants containing serine instead of cysteine residues did not induce toxicity. The N-terminal domain needs to fold properly, in which the disulfide bonds need to be functional. The α-LTX toxin is bound by a small protein, LMWP or latrodectin. It has been observed that pore formation in lipid bilayers is impossible when latrodectin is unavailable. Lactrodectin has no effect on α-LTX toxicity.
In addition to exerting an effect on the nematode via binding to Latrophilin receptors, there is also recent evidence that indicates that emodepside also interacts with the BK potassium channel coded by the gene Slo-1. This protein (see figure for structure) is a member of the 6 transmembrane helix structural class of potassium ion channels with each subunit consisting of 6 transmembrane helices and 1 P domain (this P domain is conserved in all potassium ion channels and forms the selectivity filter that enables the channel to transport potassium ions across the membrane in great preference to other ions). These subunits group together to form high conductance BK-type channels that are gated by both membrane potential and intracellular calcium levels (this calcium ion sensing ability is accommodated by an intracellular tail region on Slo-like subunits that form a calcium ion binding motif consisting of a run of conserved aspartate residues, termed a “calcium bowl”), with their physiological role being to regulate the excitability of neurons and muscle fibres, through the way in which they participate in action potential repolariziation (with potassium ion efflux being used to repolarize the cell following depolarization).