Search results for: Demet Arac

Items from 1 to 20 out of 23 results

article

The expanding functional roles and signaling mechanisms of adhesion G protein–coupled receptors

Rory K. Morgan, Garret R. Anderson, Demet Araç, Gabriela Aust, more

Annals of the New York Academy of Sciences > 1456 > 1 > 5 - 25

The adhesion class of G protein–coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N‐terminal region that is linked to a C‐terminal seven transmembrane (7TM) domain via a GPCR‐autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS...

article

A Comprehensive Mutagenesis Screen of the Adhesion GPCR Latrophilin-1/ADGRL1

Olha Nazarko, Amanuel Kibrom, Jana Winkler, Katherine Leon, more

iScience > 2018 > 3 > C > 264-278

Adhesion G-protein-coupled receptors (aGPCRs) play critical roles in diverse cellular processes in neurobiology, development, immunity, and numerous diseases. The lack of molecular understanding of their activation mechanisms, especially with regard to the transmembrane domains, hampers further studies to facilitate aGPCR-targeted drug development. Latrophilin-1/ADGRL1 is a model aGPCR that regulates...

article

Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse

Jingxian Li, Moran Shalev-Benami, Richard Sando, Xian Jiang, more

Cell > 2018 > 173 > 3 > 735-748.e15

Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large β barrel that partially encapsulates a C-terminal domain, which emerges to the solvent through an opening...

article

Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains

Gabriel S. Salzman, Sarah D. Ackerman, Chen Ding, Akiko Koide, more

Neuron > 2016 > 91 > 6 > 1292-1304

Adhesion G protein-coupled receptors (aGPCRs) play critical roles in diverse neurobiological processes including brain development, synaptogenesis, and myelination. aGPCRs have large alternatively spliced extracellular regions (ECRs) that likely mediate intercellular signaling; however, the precise roles of ECRs remain unclear. The aGPCR GPR56/ADGRG1 regulates both oligodendrocyte and cortical development...

article

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion

Yue C. Lu, Olha V. Nazarko, Richard Sando, Gabriel S. Salzman, more

Structure > 2016 > 24 > 2 > 348

article

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion

Yue C. Lu, Olha V. Nazarko, Richard Sando, Gabriel S. Salzman, more

Structure > 2015 > 23 > 9 > 1678-1691

Fibronectin leucine-rich repeat transmembrane proteins (FLRTs) are cell-adhesion molecules with emerging functions in cortical development and synapse formation. Their extracellular regions interact with latrophilins (LPHNs) to mediate synapse development, and with Uncoordinated-5 (UNC5)/netrin receptors to control the migration of neurons in the developing cortex. Here, we present the crystal structures...

article

New functions and signaling mechanisms for the class of adhesion G protein–coupled receptors

Ines Liebscher, Brian Ackley, Demet Araç, Donna M. Ariestanti, more

Annals of the New York Academy of Sciences > 1333 > 1 > 43 - 64

The class of adhesion G protein–coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven‐transmembrane α‐helix—a structural feature of all GPCRs—the class of aGPCRs is characterized by the presence of a large N‐terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis–inducing (GAIN) domain that mediates...

article

Matching structure with function: the GAIN domain of Adhesion-GPCR and PKD1-like proteins

Simone Prömel, Tobias Langenhan, Demet Araç

Trends in Pharmacological Sciences > 2013 > 34 > 8 > 470-478

Elucidation of structural information can greatly facilitate the understanding of molecular function. A recent example is the description of the G-protein-coupled receptor (GPCR) autoproteolysis-inducing (GAIN) domain, an evolutionarily ancient fold present in Adhesion-GPCRs (aGPCRs) and polycystic kidney disease 1 (PKD1)-like proteins. In the past, the peculiar autoproteolytic capacity of both membrane...

article

Dissecting signaling and functions of adhesion G protein–coupled receptors

Demet Araç, Gabriela Aust, Davide Calebiro, Felix B. Engel, more

Annals of the New York Academy of Sciences > 1276 > 1 > 1 - 25

G protein–coupled receptors (GPCRs) comprise an expanded superfamily of receptors in the human genome. Adhesion class G protein–coupled receptors (adhesion‐GPCRs) form the second largest class of GPCRs. Despite the abundance, size, molecular structure, and functions in facilitating cell and matrix contacts in a variety of organ systems, adhesion‐GPCRs are by far the most poorly understood GPCR class...

article

Neurexins Physically and Functionally Interact with GABAA Receptors

Chen Zhang, Deniz Atasoy, Demet Araç, Xiaofei Yang, more

Neuron > 2010 > 66 > 3 > 403-416

Neurexins are presynaptic cell-adhesion molecules that form trans-synaptic complexes with postsynaptic neuroligins. When overexpressed in nonneuronal cells, neurexins induce formation of postsynaptic specializations in cocultured neurons, suggesting that neurexins are synaptogenic. However, we find that when overexpressed in neurons, neurexins do not increase synapse density, but instead selectively...

article

A Potent Peptidomimetic Inhibitor of Botulinum Neurotoxin Serotype A Has a Very Different Conformation than SNAP-25 Substrate

Jorge E. Zuniga, James J. Schmidt, Timothy Fenn, James C. Burnett, more

Structure > 2008 > 16 > 10 > 1588-1597

Botulinum neurotoxin serotype A is the most lethal of all known toxins. Here, we report the crystal structure, along with SAR data, of the zinc metalloprotease domain of BoNT/A bound to a potent peptidomimetic inhibitor (K _i = 41 nM) that resembles the local sequence of the SNAP-25 substrate. Surprisingly, the inhibitor adopts a helical conformation around the cleavage site, in contrast to...

article

Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1β Complex Reveal Specific Protein-Protein and Protein-Ca2+ Interactions

Demet Araç, Antony A. Boucard, Engin Özkan, Pavel Strop, more

Neuron > 2007 > 56 > 6 > 992-1003

Neurexins and neuroligins provide trans-synaptic connectivity by the Ca ²⁺ -dependent interaction of their alternatively spliced extracellular domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal structures of neuroligin-1 in isolation and in complex with neurexin-1β. Neuroligin-1 forms a constitutive dimer,...

article

A Quaternary SNARE–Synaptotagmin–Ca2+–Phospholipid Complex in Neurotransmitter Release

Han Dai, Nan Shen, Demet Araç, Josep Rizo

Journal of Molecular Biology > 2007 > 367 > 3 > 848-863

The function of synaptotagmin as a Ca ²⁺ sensor in neurotransmitter release involves Ca ²⁺ -dependent phospholipid binding to its two C ₂ domains, but this activity alone does not explain why Ca ²⁺ binding to the C ₂ B domain is more critical for release than Ca ²⁺ binding to the C ₂ A domain. Synaptotagmin also binds to SNARE complexes, which...

article

Selected proteins involved in neurotransmitter release

Josep Rizo, Xiaocheng Chen, Demet Araç

Trends in Cell Biology > 2006 > 16 > 7 > 339-350

SNARE proteins and synaptotagmin are key components of the complex machinery that controls Ca ²⁺ -triggered neurotransmitter release but their mechanisms of action are under debate. Recent research has shed light on which biochemical and/or biophysical properties underlie SNARE and synaptotagmin function. SNARE proteins most likely have a role in membrane fusion owing to their ability to bring...

article

SNARE-Mediated Lipid Mixing Depends on the Physical State of the Vesicles

Xiaocheng Chen, Demet Araç, Tzu-Ming Wang, Christopher J. Gilpin, more

Biophysical Journal > 2006 > 90 > 6 > 2062-2074

Reconstitution experiments have suggested that N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) proteins constitute a minimal membrane fusion machinery but have yielded contradictory results, and it is unclear whether the mechanism of membrane merger is related to the stalk mechanism that underlies physiological membrane fusion. Here we show that reconstitution of solubilized...

article

Three-dimensional Structure of the rSly1 N-terminal Domain Reveals a Conformational Change Induced by Binding to Syntaxin 5

Demet Araç, Irina Dulubova, Jimin Pei, Iryna Huryeva, more

Journal of Molecular Biology > 2005 > 346 > 2 > 589-601

Sec1/Mun18-like (SM) proteins and soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) play central roles in intracellular membrane fusion. Diverse modes of interaction between SM proteins and SNAREs from the syntaxin family have been described. However, the observation that the N-terminal domains of Sly1 and Vps45, the SM proteins involved in traffic at the endoplasmic...

article

Facile Detection of Protein−Protein Interactions by One-Dimensional NMR Spectroscopy ^†

Demet Araç, Tara Murphy, Josep Rizo

Biochemistry > 2003 > 42 > 10 > 2774 - 2780

article

On the Role of αThr183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase

Victor Kulik, Michael Weyand, Ralf Seidel, Dimitri Niks, more

Journal of Molecular Biology > 2002 > 324 > 4 > 677-690

The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase α ₂ β ₂ complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved αThr183 residue is part of loop αL6 and is located next to the α-active...

article

Three-Dimensional Structure of the Complexin/SNARE Complex

Xiaocheng Chen, Diana R. Tomchick, Evguenii Kovrigin, Demet Araç, more

Neuron > 2002 > 33 > 3 > 397-409

During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca²⁺-evoked neurotransmitter release. A combined X-ray and TROSY-based NMR study...

article

An integrated genetic, radiation hybrid, physical and transcription map of a region of distal mouse chromosome 12, including an imprinted locus and the ‘Legs at odd angles’ (Loa) mutation

Abi S Witherden, Majid Hafezparast, Sharon J Nicholson, Azlina Ahmad-Annuar, more

Gene > 2002 > 283 > 1-2 > 71-82

A variety of loci with interesting patterns of regulation such as imprinted expression, and critical functions such as involvement in tumour necrosis factor pathways, map to a distal portion of mouse chromosome 12. This region also contains disease related loci including the ‘Legs at odd angles’ mutation (Loa) that we are pursuing in a positional cloning project. To further define the region and prepare...

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Search results for: Demet Arac

The expanding functional roles and signaling mechanisms of adhesion G protein–coupled receptors

A Comprehensive Mutagenesis Screen of the Adhesion GPCR Latrophilin-1/ADGRL1

Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse

Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion

New functions and signaling mechanisms for the class of adhesion G protein–coupled receptors

Matching structure with function: the GAIN domain of Adhesion-GPCR and PKD1-like proteins

Dissecting signaling and functions of adhesion G protein–coupled receptors

Neurexins Physically and Functionally Interact with GABAA Receptors

A Potent Peptidomimetic Inhibitor of Botulinum Neurotoxin Serotype A Has a Very Different Conformation than SNAP-25 Substrate

Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1β Complex Reveal Specific Protein-Protein and Protein-Ca2+ Interactions

A Quaternary SNARE–Synaptotagmin–Ca2+–Phospholipid Complex in Neurotransmitter Release

Selected proteins involved in neurotransmitter release

SNARE-Mediated Lipid Mixing Depends on the Physical State of the Vesicles

Three-dimensional Structure of the rSly1 N-terminal Domain Reveals a Conformational Change Induced by Binding to Syntaxin 5

Facile Detection of Protein−Protein Interactions by One-Dimensional NMR Spectroscopy ^†

On the Role of αThr183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase

Three-Dimensional Structure of the Complexin/SNARE Complex

An integrated genetic, radiation hybrid, physical and transcription map of a region of distal mouse chromosome 12, including an imprinted locus and the ‘Legs at odd angles’ (Loa) mutation

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