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Teneurins and latrophilins: two giants meet at the synapse.

ABSTRACT: Teneurins and latrophilins are both conserved families of cell adhesion proteins that mediate cellular communication and play critical roles in embryonic and neural development. However, their mechanisms of action remain poorly understood. In the past several years, three-dimensional structures of teneurins and latrophilins have been reported at atomic resolutions and revealed distinct protein folds and unique structural features. In this review, we discuss these structures which, together with structure-guided biochemical and functional analyses, provide hints for the mechanisms of trans-cellular communication at the synapse and other cell-cell contact sites.

SUBMITTER: Arac D

PROVIDER: S-EPMC6677252 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Teneurins and latrophilins: two giants meet at the synapse.

Araç Demet D Li Jingxian J

Current opinion in structural biology 20190201

Teneurins and latrophilins are both conserved families of cell adhesion proteins that mediate cellular communication and play critical roles in embryonic and neural development. However, their mechanisms of action remain poorly understood. In the past several years, three-dimensional structures of teneurins and latrophilins have been reported at atomic resolutions and revealed distinct protein folds and unique structural features. In this review, we discuss these structures which, together with ...[more]

PMID: 30952063

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Project description:Teneurins are type II transmembrane proteins expressed during pattern formation and neurogenesis with an intracellular domain that can be transported to the nucleus and an extracellular domain that can be shed into the extracellular milieu. In Drosophila melanogaster, Caenorhabditis elegans, and mouse the knockdown or knockout of teneurin expression can lead to abnormal patterning, defasciculation, and abnormal pathfinding of neurites, and the disruption of basement membranes. Here, we have identified and analyzed teneurins from a broad range of metazoan genomes for nuclear localization sequences, protein interaction domains, and furin cleavage sites and have cloned and sequenced the intracellular domains of human and avian teneurins to analyze alternative splicing. The basic organization of teneurins is highly conserved in Bilateria: all teneurins have epidermal growth factor (EGF) repeats, a cysteine-rich domain, and a large region identical in organization to the carboxy-half of prokaryotic YD-repeat proteins. Teneurins were not found in the genomes of sponges, cnidarians, or placozoa, but the choanoflagellate Monosiga brevicollis has a gene encoding a predicted teneurin with a transmembrane domain, EGF repeats, a cysteine-rich domain, and a region homologous to YD-repeat proteins. Further examination revealed that most of the extracellular domain of the M. brevicollis teneurin is encoded on a single huge 6,829-bp exon and that the cysteine-rich domain is similar to sequences found in an enzyme expressed by the diatom Phaeodactylum tricornutum. This leads us to suggest that teneurins are complex hybrid fusion proteins that evolved in a choanoflagellate via horizontal gene transfer from both a prokaryotic gene and a diatom or algal gene, perhaps to improve the capacity of the choanoflagellate to bind to its prokaryotic prey. As choanoflagellates are considered to be the closest living relatives of animals, the expression of a primitive teneurin by an ancestral choanoflagellate may have facilitated the evolution of multicellularity and complex histogenesis in metazoa.

Dataset Information

Teneurins and latrophilins: two giants meet at the synapse.

Publications

Teneurins and latrophilins: two giants meet at the synapse.

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