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PubMed2004

Different functional roles of T1R subunits in the heteromeric taste receptors.

The T1R receptors, a family of taste-specific class C G protein-coupled receptors, mediate mammalian sweet and umami tastes. The structure-function relationships of T1R receptors remain largely unknown. In this study, we demonstrate the different functional roles of T1R extracellular and transmembrane domains in ligand recognition and G protein coupling. Similar to other family C G protein-coupled receptors, the N-terminal Venus flytrap domain of T1R2 is required for recognizing sweeteners, such as aspartame and neotame. The G protein coupling requires the transmembrane domain of T1R2. Surprisingly, the C-terminal transmembrane domain of T1R3 is required for recognizing sweetener cyclamate and sweet taste inhibitor lactisole. Because T1R3 is the common subunit in the sweet taste receptor and the umami taste receptor, we tested the interaction of lactisole and cyclamate with the umami taste receptor. Lactisole inhibits the activity of the human T1R1/T1R3 receptor, and, as predicted, blocked the umami taste of l-glutamate in human taste tests. Cyclamate does not activate the T1R1/T1R3 receptor by itself, but potentiates the receptor's response to l-glutamate. Taken together, these findings demonstrate the different functional roles of T1R3 and T1R2 and the presence of multiple ligand binding sites on the sweet taste receptor.

Amino Acid Sequence↗
PubMed2006

Ancestral reconstruction of the ligand-binding pocket of Family C G protein-coupled receptors.

The metabotropic glutamate receptors (mGluRs) within the Family C subclass of G protein-coupled receptors are crucial modulators of synaptic transmission. However, their closest relatives include a diverse group of sensory receptors whose biological functions are not associated with neurotransmission, raising the question of the evolutionary origin of amino acid-binding Family C receptors. A common feature of most, if not all, functional Family C receptors is the presence of an amino acid-binding site localized within the large extracellular Venus flytrap domain. Here, we used maximum likelihood methods to infer the ancestral state of key residues in the amino acid-binding pocket of a primordial Family C receptor. These residues were reconstructed in the background of the fish 5.24 chemosensory receptor, a broad-spectrum amino acid-activated receptor. Unlike the WT 5.24 receptor, which was not activated by mGluR agonists and displayed low sensitivity toward l-glutamate, the reconstructed ancestral receptor possessed a pharmacological profile characterized by high affinity for both l-glutamate and selective Group I mGluR agonists. This pharmacological phenotype could be largely recapitulated by mutating only two residues in the 5.24 receptor-binding pocket. Our results suggest that this primordial Family C receptor may have arisen early in metazoan evolution and that it already was preadapted as a glutamate receptor for its later use at excitatory synapses in glutamate-mediated neurotransmission.

Animals↗
PubMed1993

A pump-pore model for transmembrane transport of hydrophilic solutes.

Transmembrane transport of a hydrophilic solute is presumed to begin when hydrated ligand adheres in Velcro-like fashion to hydrated membrane surface. Asymmetric physical forces cause rolling movements of ligand over membrane surface until contact occurs with appropriate transport machinery, consisting of a pump (Pu) to which is tethered a ligand (Li)-specific perm-selective pore (Po). The Po is in the open form when the Li is attached to an external high-affinity allosteric site on it. The active form of the Pu is stabilized by attachment of the Li to high-affinity internal or low-affinity external allosteric sites. The active form of the Pu induces closure of the Po, even when ligand is bound to it; the inactive conformation of the Pu permits Po opening. Attachment of Li to either one of two binding sites on the active Pu and irreversible envelopment by it in Venus fly-trap fashion trigger transmembrane transport of Li. Multistep attachment of Li is rate-limiting in the transport process. Application of a simple equation derived from relevant kinetic considerations relating velocity of transport (V) to concentration of Li (L), V = k1(L)1/2, gives V-L curves approximating transport data obtained in a variety of biological systems. This model is congruent with the ability of cells to concentrate substances from extremely dilute solutions and with the adaptive informational value to cells of rates of transport.

Animals↗
PubMed1999

Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor.

We analyzed the effect of substituting serine for each of the 19 cysteine residues within the amino-terminal extracellular domain of the human Ca(2+) receptor on cell surface expression and receptor dimerization. C129S, C131S, C437S, C449S, and C482S were similar to wild type receptor; the other 14 cysteine to serine mutants were retained intracellularly. Four of these, C60S, C101S, C358S and C395S, were unable to dimerize. A C129S/C131S double mutant failed to dimerize but was unique in that the monomeric form expressed at the cell surface. Substitution of a cysteine for serine 132 within the C129S/C131S mutant restored receptor dimerization. Mutation of residues Cys-129, Cys-131, and Ser-132, singly and in various combinations caused a left shift in Ca(2+) response compared with wild type receptor. These results identify cysteines 129 and 131 as critical in formation of intermolecular disulfide bond(s) responsible for receptor dimerization. In a "venus flytrap" model of the receptor extracellular domain, Cys-129 and Cys-131 are located within a region protruding from one lobe of the flytrap. We suggest that this region represents a dimer interface for the receptor and that mutation of residues within the interface causes important changes in Ca(2+) response of the receptor.

Amino Acid Sequence↗
PubMed2000

Human Ca2+ receptor cysteine-rich domain. Analysis of function of mutant and chimeric receptors.

The 612-residue extracellular domain of the human Ca(2+) receptor (hCaR) has been speculated to consist of a Venus's-flytrap domain (VFT) and a cysteine-rich domain. We studied the function of the hCaR Cys-rich domain by using mutagenesis and chimera approaches. A chimeric hCaR with the sequence from residues 540-601 replaced by the corresponding sequence from the Fugu CaR remained fully functional. Another chimeric hCaR with the same region of sequence replaced by the corresponding sequence from metabotropic glutamate receptor subtype 1 (mGluR1) still was activated by extracellular Ca(2+) ([Ca(2+)](o)), but its function was severely compromised. Chimeric receptors with the hCaR VFT and mGluR1 seven-transmembrane domain plus C-tail domain retained good response to [Ca(2+)](o) whether the Cys-rich domain was from hCaR or from mGluR1. Mutant hCaR with the Cys-rich domain deleted failed to respond to [Ca(2+)](o), although it was expressed at the cell surface and capable of dimerization. Our results indicate that the hCaR Cys-rich domain plays a critical role in signal transmission from VFT to seven-transmembrane domain. This domain tolerates a significant degree of amino acid substitution and may not be directly involved in the binding of [Ca(2+)](o).

Amino Acid Sequence↗
PubMed2001

Human Ca(2+) receptor extracellular domain. Analysis of function of lobe I loop deletion mutants.

The G protein-coupled Ca(2+) receptor (CaR) possesses an approximately 600-residue extracellular domain involved in ligand binding and receptor activation. Based on an alignment of the amino acid sequence of the CaR with that of bacterial periplasmic-binding proteins, the first approximately 530 residues of the extracellular domain are believed to form a domain resembling a bilobed Venus's flytrap (VFT). Four insertions in the CaR sequence that do not align with those of bacterial periplasmic-binding proteins correspond to four loops within lobe I of the VFT. We constructed a series of deletion mutants of these four loops and tested their ability to form fully processed CaR as well as their ability to be activated by Ca(2+). As many as 21 residues (365) of loop III could be deleted without impairing receptor expression or activation. Deletion of portions of either loops I (50) or IV (438) did not impair receptor expression but significantly reduced Ca(2+) activation. Deletion of the entire loop II (117) abolished receptor expression and function, but the replacement of even a single residue within this deletion mutant led to expression of a monomeric form of the receptor showing increased Ca(2+) sensitivity but reduced maximal activation. Our results reveal that certain residues within loops I and IV are dispensable in formation of the VFT domain but are critical for Ca(2+) activation of the receptor. In contrast, the residues in loop II are critical for maintaining the inactive state of the CaR. We discuss these results in light of the recently defined crystal structure of the homologous domain of the type 1 metabotropic glutamate receptor.

Amino Acid Sequence↗
PubMed2004

Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit.

The gamma-aminobutyric acid type B (GABAB) receptor is an allosteric complex made of two subunits, GABAB1 (GB1) and GABAB2 (GB2). Both subunits are composed of an extracellular Venus flytrap domain (VFT) and a heptahelical domain (HD). GB1 binds GABA, and GB2 plays a major role in G-protein activation as well as in the high agonist affinity state of GB1. How agonist affinity in GB1 is regulated in the receptor remains unknown. Here, we demonstrate that GB2 VFT is a major molecular determinant involved in this control. We show that isolated versions of GB1 and GB2 VFTs in the absence of the HD and C-terminal tail can form hetero-oligomers as shown by time-resolved fluorescence resonance energy transfer (based on HTRF technology). GB2 VFT and its association with GB1 VFT controlled agonist affinity in GB1 in two ways. First, GB2 VFT exerted a direct action on GB1 VFT, as it slightly increased agonist affinity in isolated GB1 VFT. Second and most importantly, GB2 VFT prevented inhibitory interaction between the two main domains (VFT and HD) of GB1. According to this model, we propose that GB1 HD prevents the possible natural closure of GB1 VFT. In contrast, GB2 VFT facilitates this closure. Finally, such inhibitory contacts between HD and VFT in GB1 could be similar to those important to maintain the inactive state of the receptor.

Allosteric Regulation↗
PubMed2006

Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors.

Many membrane receptors are made of a ligand binding domain and an effector domain mediating intracellular signaling. This is the case for the metabotropic glutamate-like G-protein-coupled receptors. How ligand binding leads to the active conformation of the effector domain in such receptors is largely unknown. Here, we used an evolutionary trace analysis and mutagenesis to identify critical residues involved in the allosteric coupling between the Venus flytrap ligand binding domain (VFT) and the heptahelical G-protein activating domain of the metabotropic glutamate-like receptors. We have shown that a conserved interdomain disulfide bridge is required for this allosteric interaction. Taking into account that these receptors are homodimers, this finding provides important new information explaining how the different conformations of the dimer of VFT lead to different signaling of such dimeric receptors.

Animals↗
PubMed1977

Purification and characterization of a cardioexcitatory neuropeptide from the central ganglia of a bivalve mollusc.

We have purified a cardioexcitatory substance, previously designated peak C, from ganglia of the Sunray Venus clam, Macrocallista nimbosa. Low concentrations (10(-9)-10(-8) M) of this substance not only excite the isolated clam heart, but also produce tonic contractions of the isolated radula protractor muscle of the whelk, Busycon contrarium. These two muscle preparations have therefore been used as a parallel bioassay for peak C. Peak C is inactivated by proteolytic enzymes, has an isoelectric point greater than pH 10 and has an ultraviolet absorption spectrum similar to that of phenylalanine. On thin layer chromatograms, peak C separates into two components; one of these is probably a partially oxidized form produced during purification. Both components react with ninhydrin and with the Sakaguchi reagent for guanidino groups. The amino acid composition of peak C is Phe2.00Met0.81Arg1.12. N-terminal analysis, one round of Edman-dansyl degradation, and tryptic digesting are consistent with the identification of Macrocallista peak C as a tetrapeptide amide: Phe-Met-Arg-Phe-NH2 (FMRFamide).

Amino Acid Sequence↗
PubMedDate not supplied

Identification of hallucinatory themes in the Late Neolithic art of Hungary.

A number of factors that coalesced in the Venus figurines of the Late Neolithic culture from Hungary have been identified with dominant hallucinatory themes, suggesting the crucial role of ecstatic religion in this culture. This article provides a review of the nature and role of hallucinogens in the ecstatic religion of contemporary and historical cultures in order to establish a background for analysis. Analysis of these Late Neolithic artifacts indicates the presence of a number of themes associated with hallucinogen use: the presence of iconographic elements similar to eidetic forms; the use of red color; anthropo- and theriopomorphic figurines in seated postures; and specific patterns of breakage with disposal. The discussion illuminates the crucial features as well as the role and significance of these factors in ecstatic cults.

Art↗
PubMed2003

(19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a closed conformation exists in solution.

The leucine-isoleucine-valine binding protein (LIV) found in the periplasmic space of E. coli has been used as a structural model for a number of neuronal receptors. This "venus fly trap" type protein has been characterized by crystallography in only the open form. Herein we have labeled LIV with 5-fluorotryptophan (5F-Trp) and difluoromethionine (DFM) in order to explore the structural dynamics of this protein and the application of DFM as a potential (19)F NMR structural probe for this family of proteins. Based on mass spectrometric analysis of the protein overproduced in the presence of DFM, approximately 30% of the five LIV methionine residues were randomly substituted with the fluorinated analog. Urea denaturation experiments imply a slight decrease in protein stability when DFM is incorporated into LIV. However, the fluorinated methionine did not alter leucine-binding activity upon its incorporation into the protein. Binding of L-leucine stabilizes both the unlabeled and DFM-labeled LIV, and induces the protein to adopt a three-state unfolding model in place of the two-state process observed for the free protein. The (19)F NMR spectrum of DFM-labeled LIV gave distinct resonances for the five Met residues found in LIV. 5F-Trp labeled LIV gave a well resolved spectrum for the three Trp residues. Trp to Phe mutants defined the resonances in the spectrum. The distinct narrowing in line width of the resonances when ligand was added identified the closed form of the protein.

Bacterial Proteins↗
PubMed1956

The structure of paramyosin fibrils according to x-ray diffraction.

From analysis of x-ray diffraction patterns obtained with improved small-angle techniques has been derived the following description for the structure of the fibrils of the fibrous protein, paramyosin, obtained in this case from "white" portions of the adductor muscle of the clam, Venus mercenaria: 1. About 25 significantly different diffraction maxima have been resolved and found accounted for as (hk) reflections of a net whose cell elements are, for the dry material: a = 250 A, b = 720 A (fibril axis identity period), and gamma = 90.5 degrees (angle included between a and b axes). For rehydrated material a is larger (ca. 325 A), b is essentially unchanged, and gamma is slightly larger. There remains an unresolved discrepancy between the electron-optically derived, cell's a dimension (193 A) and that here reported for dry samples. 2. The h = +/-1 row lines are crossed on the diagrams (because gamma is not 90 degrees ) and thus can be distinguished in spite of natural "rotation" of fibrils (within the massive fibrous specimens) about their commonly oriented axes. The observed reflections are then found to obey a selection rule which indicates that the net cell is non-primitive and contains 5 equivalent locations (nodes) arranged as shown in Fig. 5. The nodal distribution is the same as has been previously photographed electron-optically. 3. Analysis of reflection lengths indicates that the native fibrils are not noticeably ribbon-like, having dimensions normal to the ordered net layers approximating their width across the fibril in the plane of the net layers. Corresponding transverse, interlayer spacings (possibly ca. 100 A) have not been observed, however, and may be hidden in troublesome central scatter. 4. Since paramyosin's wide-angle diffraction is very probably of alpha-type, supercoiled alpha-helices must be involved according to current interpretations of alpha-diagrams. Physicochemical evidence suggests that cables of this type, ca. 1400 A in length, may extend over two cells. Of two possible nodal connections, a favored one is shown in Fig. 5 to join 5 nodes in this way. Considerations of space filling, of transverse distribution of small-angle x-ray scattering, and of nodal significance, suggest that the cable units may be further aggregated into supercables, essentially forming rather solid rods of ca. 100 A diameter. 5. An alternative interpretation of the paramyosin small-angle diffraction, in particular of the observed selection rule, would conclude that large particles are arranged in a helical way, with minimum helix diameter about 150 A (dry). The simplest (genetic) particle connection would have 5 particles in 2 coil turns along 720 A of fibril or helix axis. This view is distinctly different from the arrangement of "rods" in net-like layers as given above, even though the rods are said to be made of supercoils or cables. Reasons are given for preferring the net-of-rods explanation over the particulate-helix model. The helix- vs. true-net ambiguity arises whenever the two types of structure are conceivable, and decision between them is difficult on the basis of the diffraction data alone.

Muscle Proteins↗
PubMed1956

The structure of actin-rich filaments of muscles according to x-ray diffraction.

From analysis of moderate- to small-angle x-ray diffraction patterns, in the light of similar experience with paramyosin, has been derived the following description for the structure of actin-rich filaments in "tinted" portions of the adductor muscle of the clam, Venus mercenaria: 1. Some 11 diffraction maxima, widely streaked along layer lines and occurring at moderate diffraction angles (spacings 7 to 60 A) appear to be accounted for as (hk) reflections of a net whose cell elements are, for dry material: a =... 82 A, b = 406 A (filament axis identity period), and gamma =... 82 degrees (angle between a and b axes). These reflections follow a selection rule which indicates that the net cell is non-primitive and contains 15 equivalent locations (nodes) arranged as shown in Fig. 5. An alternative net has b' = 351 A and 13 nodes per cell. 2. Another interpretation rolls the net into a large-scale helix and places the 15 (or 13) nodes along 7 (or 6) turns of a helical locus projecting 406 (or 351) A along the filament axis. Whether considered to be built of planar-net or helix-net cells, the individual filament contains a single cell width transverse to its axis. Transverse filament dimensions are, therefore, in either case similar (50 to 100 A). 3. Consideration of existing electron-optical, physicochemical, and x-ray diffraction data regarding isolated actin suggests that the net cell is built of rods, each containing in cross-section from one to four actin molecules which run parallel to or twisted about rod axes that extend at 12 degrees to the filament axis along the (21) diagonals of the cell. Depending on monomer shape, 2 to 15 monomers furnish length to reach across two cells, and the actin molecules are built into each rod in such a way as to repeat (or nearly repeat) structure 15 (or 13) times along the double cell length. Further details of intra-rod structure cannot be suggested because of lack of wide-angle diffraction information. 4. The actin system is sensitive to treatment of the muscle with ethanol. Concentrations of 5 per cent or greater abolish the net reflections. Other solvents-water, benzene, ether, pyridine, acetone-do not alter the pattern materially. 5. Two other reflections, occurring at the first and second layer lines of an axial periodicity of about 400 A, do not clearly belong to the actin-net system. They represent either a superstructure built upon the filaments by parts of the actin molecules themselves or by incorporated other molecular species, or they arise from an additional macromolecular component (possibly myosin, or its homologues or fractions) of similar axial periodicity.

Actin Cytoskeleton↗
PubMed2003

Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects.

Indicator molecules for caspase-3 activation have been reported that use fluorescence resonance energy transfer (FRET) between an enhanced cyan fluorescent protein (the donor) and enhanced yellow fluorescent protein (EYFP; the acceptor). Because EYFP is highly sensitive to proton (H+) and chloride ion (Cl-) levels, which can change during apoptosis, this indicator's ability to trace the precise dynamics of caspase activation is limited, especially in vivo. Here, we generated an H+- and Cl--insensitive indicator for caspase activation, SCAT, in which EYFP was replaced with Venus, and monitored the spatio-temporal activation of caspases in living cells. Caspase-3 activation was initiated first in the cytosol and then in the nucleus, and rapidly reached maximum activation in 10 min or less. Furthermore, the nuclear activation of caspase-3 preceded the nuclear apoptotic morphological changes. In contrast, the completion of caspase-9 activation took much longer and its activation was attenuated in the nucleus. However, the time between the initiation of caspase-9 activation and the morphological changes was quite similar to that seen for caspase-3, indicating the activation of both caspases occurred essentially simultaneously during the initiation of apoptosis.

Apoptosis↗
PubMed2004

Cadherin activity is required for activity-induced spine remodeling.

Neural activity induces the remodeling of pre- and postsynaptic membranes, which maintain their apposition through cell adhesion molecules. Among them, N-cadherin is redistributed, undergoes activity-dependent conformational changes, and is required for synaptic plasticity. Here, we show that depolarization induces the enlargement of the width of spine head, and that cadherin activity is essential for this synaptic rearrangement. Dendritic spines visualized with green fluorescent protein in hippocampal neurons showed an expansion by the activation of AMPA receptor, so that the synaptic apposition zone may be expanded. N-cadherin-venus fusion protein laterally dispersed along the expanding spine head. Overexpression of dominant-negative forms of N-cadherin resulted in the abrogation of the spine expansion. Inhibition of actin polymerization with cytochalasin D abolished the spine expansion. Together, our data suggest that cadherin-based adhesion machinery coupled with the actin-cytoskeleton is critical for the remodeling of synaptic apposition zone.

Actins↗
PubMed1957

Some chemical and structural properties of paramyosin.

Paramyosin fibrils from the adductor muscles of Venus mercenaria are soluble above neutrality at relatively high ionic strength. From this viscous solution it is possible, by reduction in ionic strength, to reprecipitate acicular crystals of paramyosin. In the electron microscope these fibrils manifest a symmetrical band pattern similar to that previously described by Hodge but differing in some details. The axial periods observed under the conditions of the experiment varied between 1700 and 2000 A and a simple band pattern of one-fifth the main period was frequently observed. ATPase activity of the myosin type but of much lower intensity was demonstrated. Tryptic fission of the protein occurs but the characteristics differ from those of myosin.

Animals↗
PubMed1999

Viscous Forces in Velocity Boundary Layers around Planetary Ionospheres.

A discussion is presented to examine the role of viscous forces in the transport of solar wind momentum to the ionospheric plasma of weakly magnetized planets (Venus and Mars). Observational data are used to make a comparison of the Reynolds and Maxwell stresses that are operative in the interaction of the solar wind with local plasma (planetary ionospheres). Measurements show the presence of a velocity boundary layer formed around the flanks of the ionosphere where the shocked solar wind has reached super-Alfvénic speeds. It is found that the Reynolds stresses in the solar wind at that region can be larger than the Maxwell stresses and thus are necessary in the local acceleration of the ionospheric plasma. From an order-of-magnitude calculation of the Reynolds stresses, it is possible to derive values of the kinematic viscosity and the Reynolds number that are suitable to the gyrotropic motion of the solar wind particles across the boundary layer. The value of the kinematic viscosity is comparable to those inferred from studies of the transport of solar wind momentum to the earth's magnetosphere and thus suggest a common property of the solar wind around planetary obstacles. Similar conditions could also be applicable to velocity boundary layers formed in other plasma interaction problems in astrophysics.

Journal Article↗
PubMed2004

"A bare outpost of learned European culture on the edge of the jungles of Java": Johan Maurits Mohr (1716-1775) and the emergence of instrumental and institutional science in Dutch colonial Indonesia.

The transits of Venus in 1761 and 1769 appear to mark the starting point of instrumental science in the Dutch East Indies (now Indonesia). This essay examines the conditions that triggered and constituted instrumental and institutional science on Indonesian soil in the late eighteenth century. In 1765 the Reverend J. M. Mohr, whose wife had received a large inheritance, undertook to build a fully equipped private observatory in Batavia (now Jakarta). There he made several major astronomical and meteorological observations. Mohr's initiative inspired other Europeans living on Java around 1770 to start a scientific movement. Because of the lack of governmental and other support, it was not until 1778 that this offspring of the Dutch-Indonesian Enlightenment became a reality. The Bataviaasch Genootschap van Kunsten en Wetenschappen tried from the beginning to put into effect the program Mohr had outlined. The members even bought his instruments from his widow, intending to continue his measurements. For a number of reasons, however, this instrumental program was more than the society could support. Around 1790 instrumental science in the former Dutch East Indies came to a standstill, not to be resumed for several decades.

Astronomy↗