{{cs1 config|name-list-style=vanc|display-authors=6}} {{Pfam_box | Symbol = Teneurin | Name = Teneurin | image = | width = | caption = | InterPro= IPR009471 | SMART= | PROSITE = | SCOP = | TCDB = | OPM family= | OPM protein= | Pfam= PF06484 | PDB= | Membranome family= 1168 }}
'''Teneurins''' are a family of phylogenetically conserved single-pass transmembrane glycoproteins expressed during pattern formation and morphogenesis.<ref name="Tucker_2001">{{cite journal | vauthors = Tucker RP, Chiquet-Ehrismann R, Chevron MP, Martin D, Hall RJ, Rubin BP | title = Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8 | journal = Developmental Dynamics | volume = 220 | issue = 1 | pages = 27–39 | date = January 2001 | pmid = 11146505 | doi = 10.1002/1097-0177(2000)9999:9999<::AID-DVDY1084>3.0.CO;2-B | doi-access = free }}</ref> 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.
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.<ref>{{cite journal | vauthors = Drabikowski K, Trzebiatowska A, Chiquet-Ehrismann R | title = ten-1, an essential gene for germ cell development, epidermal morphogenesis, gonad migration, and neuronal pathfinding in Caenorhabditis elegans | journal = Developmental Biology | volume = 282 | issue = 1 | pages = 27–38 | date = June 2005 | pmid = 15936327 | doi = 10.1016/j.ydbio.2005.02.017 }}</ref>
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.
== History ==
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 ==
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.<ref name="Young_2009">{{cite journal | vauthors = Young TR, Leamey CA | title = Teneurins: important regulators of neural circuitry | journal = The International Journal of Biochemistry & Cell Biology | volume = 41 | issue = 5 | pages = 990–993 | date = May 2009 | pmid = 18723111 | doi = 10.1016/j.biocel.2008.06.014 }}</ref>
Teneurin-3 regulates the structural and functional wiring of retinal ganglion cells in the vertebrate visual system.<ref name="Antinucci_2013">{{cite journal | vauthors = Antinucci P, Nikolaou N, Meyer MP, Hindges R | title = Teneurin-3 specifies morphological and functional connectivity of retinal ganglion cells in the vertebrate visual system | journal = Cell Reports | volume = 5 | issue = 3 | pages = 582–592 | date = November 2013 | pmid = 24183672 | pmc = 3898612 | doi = 10.1016/j.celrep.2013.09.045 }}</ref>
== Structure ==
Ten-m1–4, exist as homodimers and undergo homophilic interactions in vertebrates.
=== C terminal domain ===
The large C-terminal extracellular domain consists of eight EGF-like repeats (see [http://expasy.org/prosite/PDOC00021 PROSITEDOC]), a region of conserved cysteines and unique YD-repeats.
=== N terminal domain === {{Infobox protein family | Symbol = Ten_N | Name = Teneurin Intracellular Region | image = | width = | caption = | Pfam = PF06484 | Pfam_clan = | InterPro = IPR009471 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} 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.<ref name="Minet_1999">{{cite journal | vauthors = Minet AD, Rubin BP, Tucker RP, Baumgartner S, Chiquet-Ehrismann R | title = 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 | journal = Journal of Cell Science | volume = 112 | issue = 12 | pages = 2019–2032 | date = June 1999 | pmid = 10341219 | doi = 10.1242/jcs.112.12.2019 }}</ref><ref name="Bagutti_2003">{{cite journal | vauthors = Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R | title = The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription | journal = Journal of Cell Science | volume = 116 | issue = Pt 14 | pages = 2957–2966 | date = July 2003 | pmid = 12783990 | doi = 10.1242/jcs.00603 | s2cid = 30713 }}</ref><ref name="Tucker_2006">{{cite journal | vauthors = Tucker RP, Chiquet-Ehrismann R | title = Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development | journal = Developmental Biology | volume = 290 | issue = 2 | pages = 237–245 | date = February 2006 | pmid = 16406038 | doi = 10.1016/j.ydbio.2005.11.038 | doi-access = free }}</ref><ref name="Tucker_2007">{{cite journal | vauthors = Tucker RP, Kenzelmann D, Trzebiatowska A, Chiquet-Ehrismann R | title = Teneurins: transmembrane proteins with fundamental roles in development | journal = The International Journal of Biochemistry & Cell Biology | volume = 39 | issue = 2 | pages = 292–297 | year = 2007 | pmid = 17095284 | doi = 10.1016/j.biocel.2006.09.012 }}</ref><ref name="Kenzelmann_2007">{{cite journal | vauthors = Kenzelmann D, Chiquet-Ehrismann R, Tucker RP | title = Teneurins, a transmembrane protein family involved in cell communication during neuronal development | journal = Cellular and Molecular Life Sciences | volume = 64 | issue = 12 | pages = 1452–1456 | date = June 2007 | pmid = 17502993 | pmc = 11138457 | doi = 10.1007/s00018-007-7108-9 | s2cid = 1314540 }}</ref>
This domain is found in the intracellular N-terminal region of the teneurin family.
==Human genes==
Human genes encoding proteins that concontain the teneurin domain include:
* TENM1 * TENM2 * TENM3 * TENM4
== References == {{Reflist}}
== Further reading == {{refbegin}} * {{cite journal | vauthors = Baumgartner S, Martin D, Hagios C, Chiquet-Ehrismann R | title = Tenm, a Drosophila gene related to tenascin, is a new pair-rule gene | journal = The EMBO Journal | volume = 13 | issue = 16 | pages = 3728–3740 | date = August 1994 | pmid = 8070401 | pmc = 395283 | doi = 10.1002/j.1460-2075.1994.tb06682.x }} * {{cite journal | vauthors = Levine A, Bashan-Ahrend A, Budai-Hadrian O, Gartenberg D, Menasherow S, Wides R | title = Odd Oz: a novel Drosophila pair rule gene | journal = Cell | volume = 77 | issue = 4 | pages = 587–598 | date = May 1994 | pmid = 7514504 | doi = 10.1016/0092-8674(94)90220-8 | s2cid = 32035939 }} * {{cite journal | vauthors = Tucker RP, Chiquet-Ehrismann R | title = Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development | journal = Developmental Biology | volume = 290 | issue = 2 | pages = 237–245 | date = February 2006 | pmid = 16406038 | doi = 10.1016/j.ydbio.2005.11.038 | doi-access = free }} {{refend}}
{{Membrane proteins}}
Category:Protein families