| 词条 | Teneurin |
| 释义 |
| 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 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. HomologyTeneurins are a family of phylogenetically conserved transmembrane glycoproteins expressed during pattern formation and morphogenesis.[2] HistoryOriginally 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. FunctionTeneurins 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] StructureTen-m1–4, exist as homodimers and undergo homophilic interactions in vertebrates. C terminal domainThe 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{{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.[5][6][7][8][9] This domain is found in the intracellular N-terminal region of the teneurin family. Human genesHuman genes encoded teneurin domain proteins (TENM1-4) are list in the infoboxes. References1. ^{{Cite journal|last=Drabikowski|first=Krzysztof|last2=Trzebiatowska|first2=Agnieszka|last3=Chiquet-Ehrismann|first3=Ruth|date=2005-06-01|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|doi=10.1016/j.ydbio.2005.02.017|issn=0012-1606|pmid=15936327}} 2. ^{{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 = Dev. Dyn. | 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 }} 3. ^{{cite journal|vauthors=Young TR, Leamey CA | title=Teneurins: important regulators of neural circuitry. | journal=Int J Biochem Cell Biol | year= 2009 | volume= 41 | issue= 5 | pages= 990–3 | pmid=18723111 | doi=10.1016/j.biocel.2008.06.014 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=18723111 }} 4. ^{{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 Rep | year= 2013 | volume= 5 | issue= 3 | pages= 582–92 | pmid=24183672 | doi=10.1016/j.celrep.2013.09.045 | pmc=3898612 }} 5. ^{{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 = J. Cell Sci. | volume = 112 | issue = 12| pages = 2019–32 |date=June 1999 | pmid = 10341219 | doi = | url = }} 6. ^{{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 = J. Cell Sci. | volume = 116 | issue = Pt 14 | pages = 2957–66 |date=July 2003 | pmid = 12783990 | doi = 10.1242/jcs.00603 | url = }} 7. ^{{cite journal |vauthors=Tucker RP, Chiquet-Ehrismann R | title = Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development | journal = Dev. Biol. | volume = 290 | issue = 2 | pages = 237–45 |date=February 2006 | pmid = 16406038 | doi = 10.1016/j.ydbio.2005.11.038 | url = }} 8. ^{{cite journal |vauthors=Tucker RP, Kenzelmann D, Trzebiatowska A, Chiquet-Ehrismann R | title = Teneurins: transmembrane proteins with fundamental roles in development | journal = Int. J. Biochem. Cell Biol. | volume = 39 | issue = 2 | pages = 292–7 | year = 2007 | pmid = 17095284 | doi = 10.1016/j.biocel.2006.09.012 | url = }} 9. ^{{cite journal |vauthors=Kenzelmann D, Chiquet-Ehrismann R, Tucker RP | title = Teneurins, a transmembrane protein family involved in cell communication during neuronal development | journal = Cell. Mol. Life Sci. | volume = 64 | issue = 12 | pages = 1452–6 |date=June 2007 | pmid = 17502993 | doi = 10.1007/s00018-007-7108-9 | url = }} Further reading{{refbegin}}
1 : Protein families |
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