Structure of the teneurin-latrophilin complex: Alternative splicing controls synapse specificity by a novel mechanism

Li, Jingxian; Xie, Yuan; Cornelius, Shaleeka; Jiang, Xian Cheng; Kordon, Szymon P.; Sando, Richard; Pan, Man; Leon, Katherine; Südhof, Thomas C.; Zhao, Minglei; Araç, Demet

doi:10.1101/2020.01.13.901090

Cited by 2 publications

(2 citation statements)

References 54 publications

(82 reference statements)

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“…Type II cadherins exhibit binding through their N-terminal cadherin domain (Brasch et al, 2018). FLRT3, latrophilin 3, and teneurin 2 form a ternary complex (Li et al, 2020; also see Del Toro et al, 2020). E. Expression of cell surface proteins in developing synaptic partners.…”

Section: Reviewmentioning

confidence: 99%

Synaptic Specificity, Recognition Molecules, and Assembly of Neural Circuits

Sanes

Zipursky

2020

Cell

257

196

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Developing neurons connect in specific and stereotyped ways to form the complex circuits that underlie brain function. By comparison to earlier steps in neural development, progress has been slow in identifying the cell surface recognition molecules that mediate these synaptic choices, but new high-throughput imaging, genetic, and molecular methods are accelerating progress. Over the past decade, numerous large and small gene families have been implicated in target recognition, including members of the immunoglobulin, cadherin, and leucine-rich repeat superfamilies. We review these advances and propose ways in which combinatorial use of multifunctional recognition molecules enables the complex neuron-neuron interactions that underlie synaptic specificity.

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Section: Reviewmentioning

confidence: 99%

Synaptic Specificity, Recognition Molecules, and Assembly of Neural Circuits

Sanes

Zipursky

2020

Cell

257

196

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“…Cis receptors signal within the same cell on which the receptor resides. Adhesion GPCRs also have additional GPCRindependent trans-cellular "trans" functions mediated by interactions with adhesion receptors on other cells, such as integrins or teneurins (Dunn et al, 2019;Sando et al, 2019;Li et al, 2020;Sreepada et al, 2022). Trans receptors signal by binding receptors on other cells.…”

Section: Discussionmentioning

confidence: 99%

The GPCR properties of polycystin-1- A new paradigm

Maser

Calvet

Parnell

2022

Front. Mol. Biosci.

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Polycystin-1 (PC1) is an 11-transmembrane (TM) domain-containing protein encoded by the PKD1 gene, the most frequently mutated gene leading to autosomal dominant polycystic kidney disease (ADPKD). This large (> 462 kDal) protein has a complex posttranslational maturation process, with over five proteolytic cleavages having been described, and is found at multiple cellular locations. The initial description of the binding and activation of heterotrimeric Gαi/o by the juxtamembrane region of the PC1 cytosolic C-terminal tail (C-tail) more than 20 years ago opened the door to investigations, and controversies, into PC1’s potential function as a novel G protein-coupled receptor (GPCR). Subsequent biochemical and cellular-based assays supported an ability of the PC1 C-tail to bind numerous members of the Gα protein family and to either inhibit or activate G protein-dependent pathways involved in the regulation of ion channel activity, transcription factor activation, and apoptosis. More recent work has demonstrated an essential role for PC1-mediated G protein regulation in preventing kidney cyst development; however, the mechanisms by which PC1 regulates G protein activity continue to be discovered. Similarities between PC1 and the adhesion class of 7-TM GPCRs, most notably a conserved GPCR proteolysis site (GPS) before the first TM domain, which undergoes autocatalyzed proteolytic cleavage, suggest potential mechanisms for PC1-mediated regulation of G protein signaling. This article reviews the evidence supporting GPCR-like functions of PC1 and their relevance to cystic disease, discusses the involvement of GPS cleavage and potential ligands in regulating PC1 GPCR function, and explores potential connections between PC1 GPCR-like activity and regulation of the channel properties of the polycystin receptor-channel complex.

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Structure of the teneurin-latrophilin complex: Alternative splicing controls synapse specificity by a novel mechanism

Cited by 2 publications

References 54 publications

Synaptic Specificity, Recognition Molecules, and Assembly of Neural Circuits

Synaptic Specificity, Recognition Molecules, and Assembly of Neural Circuits

The GPCR properties of polycystin-1- A new paradigm

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