Teneurin

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Teneurin
Identifiers
SymbolTeneurin
PfamPF06484
InterProIPR009471
Membranome1168

Teneurins are single-pass transmembrane proteins. The name refers to "ten-a" (from "tenascin-like protein, accessory") and "neurons", the primary site of teneurin expression. Ten-m refers to tenascin-like protein major are type II transmembrane glycoproteins.

Teneurins are highly conserved between Drosophila, C. elegans and vertebrates. In each species they are expressed by a subset of neurons as well as at sites of pattern formation and morphogenesis. In Drosophila, a teneurin known as ten-m or Odz is a pair-rule gene, and its expression is required for normal development. The knockdown of teneurin (ten-1) expression in C. elegans with RNAi leads to abnormal neuronal pathfinding and abnormal development of the gonads.[1]

The intracellular domain of some, if not all, teneurins can be cleaved and transported to the cell nucleus, where it proposed to act as a transcription factor. A peptide derived from the terminus of the extracellular domain shares structural homology with certain neuropeptides.

There are four teneurin genes in vertebrates named teneurin-1 through -4. Other names found in the literature include Odz-1 through -4 and Tenm-1 through -4.

Homology[edit]

Teneurins are a family of phylogenetically conserved transmembrane glycoproteins expressed during pattern formation and morphogenesis.[2]

History[edit]

Originally discovered as ten-m and ten-a in Drosophila melanogaster, the teneurin family is conserved from Caenorhabditis elegans (ten-1) to vertebrates, in which four paralogs exist (teneurin-1 to -4 or odz-1 to -4). Their distinct protein domain architecture is highly conserved between invertebrate and vertebrate teneurins, particularly in the extracellular part. The intracellular domains of Ten-a, Ten-m/Odz and C. elegans TEN-1 are significantly different, both in size and structure, from the comparable domains of vertebrate teneurins, but the extracellular domains of all of these proteins are remarkably similar.

Function[edit]

Teneurins translocate to the nucleus where they regulate transcriptional activity. Teneurins promote neurite outgrowth and cell adhesion. The intracellular domain interacts with the DNA-binding transcriptional repressors and also regulate the activity of transcription factors.

Additionally, they have been known to interact with the cytoskeleton adaptor protein, CAP/ponsin, suggesting cell signalling roles and regulation of actin organisation.[3]

Teneurin-3 regulates the structural and functional wiring of retinal ganglion cells in the vertebrate visual system.[4]

Structure[edit]

Ten-m1–4, exist as homodimers and undergo homophilic interactions in vertebrates.

C terminal domain[edit]

The large C-terminal extracellular domain consists of eight EGF-like repeats (see PROSITEDOC), a region of conserved cysteines and unique YD-repeats.

N terminal domain[edit]

Teneurin Intracellular Region
Identifiers
SymbolTen_N
PfamPF06484
InterProIPR009471

The teneurin intracellular (IC) domain (∼300–400 aa) is located at the N-terminus and contains a number of conserved putative tyrosine phosphorylation sites, two EF-hand-like calcium-binding motifs, and two polyproline domains. These proline-rich stretches are characteristic of SH3-binding sites. There is considerable divergence between intracellular domains of invertebrate and vertebrate teneurins as well as between different invertebrate proteins.[5][6][7][8][9]

This domain is found in the intracellular N-terminal region of the teneurin family.

Human genes[edit]

Human genes encoded teneurin domain proteins (TENM1-4) are list in the infoboxes.

References[edit]

  1. ^ Drabikowski, Krzysztof; Trzebiatowska, Agnieszka; Chiquet-Ehrismann, Ruth (2005-06-01). "ten-1, an essential gene for germ cell development, epidermal morphogenesis, gonad migration, and neuronal pathfinding in Caenorhabditis elegans". Developmental Biology. 282 (1): 27–38. doi:10.1016/j.ydbio.2005.02.017. ISSN 0012-1606. PMID 15936327.
  2. ^ Tucker RP, Chiquet-Ehrismann R, Chevron MP, Martin D, Hall RJ, Rubin BP (January 2001). "Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8". Dev. Dyn. 220 (1): 27–39. doi:10.1002/1097-0177(2000)9999:9999<::AID-DVDY1084>3.0.CO;2-B. PMID 11146505.
  3. ^ Young TR, Leamey CA (2009). "Teneurins: important regulators of neural circuitry". Int J Biochem Cell Biol. 41 (5): 990–3. doi:10.1016/j.biocel.2008.06.014. PMID 18723111.
  4. ^ Antinucci P, Nikolaou N, Meyer MP, Hindges R (2013). "Teneurin-3 specifies morphological and functional connectivity of retinal ganglion cells in the vertebrate visual system". Cell Rep. 5 (3): 582–92. doi:10.1016/j.celrep.2013.09.045. PMC 3898612. PMID 24183672.
  5. ^ Minet AD, Rubin BP, Tucker RP, Baumgartner S, Chiquet-Ehrismann R (June 1999). "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain". J. Cell Sci. 112 (12): 2019–32. PMID 10341219.
  6. ^ Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R (July 2003). "The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription". J. Cell Sci. 116 (Pt 14): 2957–66. doi:10.1242/jcs.00603. PMID 12783990.
  7. ^ Tucker RP, Chiquet-Ehrismann R (February 2006). "Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development". Dev. Biol. 290 (2): 237–45. doi:10.1016/j.ydbio.2005.11.038. PMID 16406038.
  8. ^ Tucker RP, Kenzelmann D, Trzebiatowska A, Chiquet-Ehrismann R (2007). "Teneurins: transmembrane proteins with fundamental roles in development". Int. J. Biochem. Cell Biol. 39 (2): 292–7. doi:10.1016/j.biocel.2006.09.012. PMID 17095284.
  9. ^ Kenzelmann D, Chiquet-Ehrismann R, Tucker RP (June 2007). "Teneurins, a transmembrane protein family involved in cell communication during neuronal development". Cell. Mol. Life Sci. 64 (12): 1452–6. doi:10.1007/s00018-007-7108-9. PMID 17502993.

Further reading[edit]