abn161-i

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Showing 1-10 of 10 results for "abn161-i" within Papers

The 22q11.2 region regulates presynaptic gene-products linked to schizophrenia.

Ralda Nehme et al.

Nature communications, 13(1), 3690-3690 (2022-06-28)

It is unclear how the 22q11.2 deletion predisposes to psychiatric disease. To study this, we generated induced pluripotent stem cells from deletion carriers and controls and utilized CRISPR/Cas9 to introduce the heterozygous deletion into a control cell line. Here, we

Epigenetic loss of heterogeneity from low to high grade localized prostate tumours.

Sebnem Ece Eksi et al.

Nature communications, 12(1), 7292-7292 (2021-12-17)

Identifying precise molecular subtypes attributable to specific stages of localized prostate cancer has proven difficult due to high levels of heterogeneity. Bulk assays represent a population-average, which mask the heterogeneity that exists at the single-cell level. In this work, we

Deorphanizing FAM19A proteins as pan-neurexin ligands with an unusual biosynthetic binding mechanism.

Anna J Khalaj et al.

The Journal of cell biology, 219(9) (2020-07-25)

Neurexins are presynaptic adhesion molecules that organize synapses by binding to diverse trans-synaptic ligands, but how neurexins are regulated is incompletely understood. Here we identify FAM19A/TAFA proteins, "orphan" cytokines, as neurexin regulators that interact with all neurexins, except for neurexin-1γ

Combinatorial expression of neurexins and LAR-type phosphotyrosine phosphatase receptors instructs assembly of a cerebellar circuit.

Alessandra Sclip et al.

Nature communications, 14(1), 4976-4976 (2023-08-18)

Synaptic adhesion molecules (SAMs) shape the structural and functional properties of synapses and thereby control the information processing power of neural circuits. SAMs are broadly expressed in the brain, suggesting that they may instruct synapse formation and specification via a

Neurexophilin4 is a selectively expressed α-neurexin ligand that modulates specific cerebellar synapses and motor functions.

Xiangling Meng et al.

eLife, 8 (2019-09-17)

Neurexophilins are secreted neuropeptide-like glycoproteins, and neurexophilin1 and neurexophilin3 are ligands for the presynaptic cell adhesion molecule α-neurexin. Neurexophilins are more selectively expressed in the brain than α-neurexins, however, which led us to ask whether neurexophilins modulate the function of

RNA sequencing and functional studies of patient-derived cells reveal that neurexin-1 and regulators of this pathway are associated with poor outcomes in Ewing sarcoma.

Elizabeth Ann Roundhill et al.

Cellular oncology (Dordrecht), 44(5), 1065-1085 (2021-08-18)

The development of biomarkers and molecularly targeted therapies for patients with Ewing sarcoma (ES) in order to minimise morbidity and improve outcome is urgently needed. Here, we set out to isolate and characterise patient-derived ES primary cell cultures and daughter

LRRTM4: A Novel Regulator of Presynaptic Inhibition and Ribbon Synapse Arrangements of Retinal Bipolar Cells.

Raunak Sinha et al.

Neuron, 105(6), 1007-1017 (2020-01-25)

LRRTM4 is a transsynaptic adhesion protein regulating glutamatergic synapse assembly on dendrites of central neurons. In the mouse retina, we find that LRRTM4 is enriched at GABAergic synapses on axon terminals of rod bipolar cells (RBCs). Knockout of LRRTM4 reduces

LRRTMs Organize Synapses through Differential Engagement of Neurexin and PTPσ.

Reiko T Roppongi et al.

Neuron, 106(1), 108-125 (2020-01-30)

Presynaptic neurexins (Nrxs) and type IIa receptor-type protein tyrosine phosphatases (RPTPs) organize synapses through a network of postsynaptic ligands. We show that leucine-rich-repeat transmembrane neuronal proteins (LRRTMs) differentially engage the protein domains of Nrx but require its heparan sulfate (HS)

Structural and functional characterization of the IgSF21-neurexin2α complex and its related signaling pathways in the regulation of inhibitory synapse organization.

Nicolas Chofflet et al.

Frontiers in molecular neuroscience, 17, 1371145-1371145 (2024-04-04)

The prevailing model behind synapse development and specificity is that a multitude of adhesion molecules engage in transsynaptic interactions to induce pre- and postsynaptic assembly. How these extracellular interactions translate into intracellular signal transduction for synaptic assembly remains unclear. Here

CA10 regulates neurexin heparan sulfate addition via a direct binding in the secretory pathway.

Laia Montoliu-Gaya et al.

EMBO reports, 22(4), e51349-e51349 (2021-02-16)

Neurexins are presynaptic adhesion molecules that shape the molecular composition of synapses. Diversification of neurexins in numerous isoforms is believed to confer synapse-specific properties by engaging with distinct ligands. For example, a subset of neurexin molecules carry a heparan sulfate

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