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Mutations in this protein are responsible for most cases of [[craniofrontonasal syndrome]].<ref name="pmid17941886">{{cite journal |vauthors=Wieland I, Weidner C, Ciccone R |title=Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome |journal=Clin. Genet. |volume=72 |issue=6 |pages=506–16 |date=December 2007 |pmid=17941886 |doi=10.1111/j.1399-0004.2007.00905.x |url=http://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0009-9163&date=2007&volume=72&issue=6&spage=506|display-authors=etal}}</ref><ref>{{cite journal |vauthors=Twigg SR, Kan R, Babbs C, Bochukova EG, Robertson SP, Wall SA, Morriss-Kay GM, Wilkie AO |title=Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome |journal=Proc Natl Acad Sci U S A |volume=101 |issue=23 |pages=8652–7 |date=Jun 2004 |pmid=15166289 |pmc=423250 |doi=10.1073/pnas.0402819101 }}</ref><ref>{{cite journal |vauthors=Wieland I, Jakubiczka S, Muschke P, Cohen M, Thiele H, Gerlach KL, Adams RH, Wieacker P |title=Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome |journal=Am J Hum Genet |volume=74 |issue=6 |pages=1209–15 |date=Jun 2004 |pmid= 15124102 |pmc=1182084 |doi= 10.1086/421532}}</ref> | Mutations in this protein are responsible for most cases of [[craniofrontonasal syndrome]].<ref name="pmid17941886">{{cite journal |vauthors=Wieland I, Weidner C, Ciccone R |title=Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome |journal=Clin. Genet. |volume=72 |issue=6 |pages=506–16 |date=December 2007 |pmid=17941886 |doi=10.1111/j.1399-0004.2007.00905.x |url=http://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0009-9163&date=2007&volume=72&issue=6&spage=506|display-authors=etal}}</ref><ref>{{cite journal |vauthors=Twigg SR, Kan R, Babbs C, Bochukova EG, Robertson SP, Wall SA, Morriss-Kay GM, Wilkie AO |title=Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome |journal=Proc Natl Acad Sci U S A |volume=101 |issue=23 |pages=8652–7 |date=Jun 2004 |pmid=15166289 |pmc=423250 |doi=10.1073/pnas.0402819101 |bibcode=2004PNAS..101.8652T }}</ref><ref>{{cite journal |vauthors=Wieland I, Jakubiczka S, Muschke P, Cohen M, Thiele H, Gerlach KL, Adams RH, Wieacker P |title=Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome |journal=Am J Hum Genet |volume=74 |issue=6 |pages=1209–15 |date=Jun 2004 |pmid= 15124102 |pmc=1182084 |doi= 10.1086/421532}}</ref> | ||
==Interactions== | ==Interactions== | ||
EFNB1 has been shown to [[Protein-protein interaction|interact]] with [[SDCBP]].<ref name=pmid9920925>{{cite journal |last=Lin |first=D |author2=Gish G D |author3=Songyang Z |author4=Pawson T |date=Feb 1999 |title=The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif |journal=J. Biol. Chem. |volume=274 |issue=6 |pages=3726–33 | EFNB1 has been shown to [[Protein-protein interaction|interact]] with [[SDCBP]].<ref name=pmid9920925>{{cite journal |last=Lin |first=D |author2=Gish G D |author3=Songyang Z |author4=Pawson T |date=Feb 1999 |title=The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif |journal=J. Biol. Chem. |volume=274 |issue=6 |pages=3726–33 | issn = 0021-9258| pmid = 9920925 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.274.6.3726 }}</ref> | ||
==References== | ==References== | ||
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*{{cite journal | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=10.1016/S0163-7258(97)00112-5 }} | *{{cite journal | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=10.1016/S0163-7258(97)00112-5 }} | ||
*{{cite journal | vauthors=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi= }} | *{{cite journal | vauthors=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi= }} | ||
*{{cite | *{{cite book | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue= |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=10.1016/S0074-7696(00)96005-4 |series=International Review of Cytology |isbn=9780123646002 }} | ||
*{{cite journal | vauthors=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond. B Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635 | pmc=1692797 }} | *{{cite journal | vauthors=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond. B Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635 | pmc=1692797 }} | ||
*{{cite journal | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515 }} | *{{cite journal | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515 }} | ||
*{{cite journal | vauthors=Davis S, Gale NW, Aldrich TH |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. |journal=Science |volume=266 |issue= 5186 |pages= 816–9 |year= 1994 |pmid= 7973638 |doi=10.1126/science.7973638 |display-authors=etal}} | *{{cite journal | vauthors=Davis S, Gale NW, Aldrich TH |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. |journal=Science |volume=266 |issue= 5186 |pages= 816–9 |year= 1994 |pmid= 7973638 |doi=10.1126/science.7973638 |display-authors=etal|bibcode=1994Sci...266..816D }} | ||
*{{cite journal | vauthors=Beckmann MP, Cerretti DP, Baum P |title=Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors. |journal=EMBO J. |volume=13 |issue= 16 |pages= 3757–62 |year= 1994 |pmid= 8070404 |doi= | pmc=395287 |display-authors=etal}} | *{{cite journal | vauthors=Beckmann MP, Cerretti DP, Baum P |title=Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors. |journal=EMBO J. |volume=13 |issue= 16 |pages= 3757–62 |year= 1994 |pmid= 8070404 |doi= | pmc=395287 |display-authors=etal}} | ||
*{{cite journal | vauthors=Cerretti DP, Lyman SD, Kozlosky CJ |title=The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3. |journal=Genomics |volume=33 |issue= 2 |pages= 277–82 |year= 1997 |pmid= 8660976 |doi= 10.1006/geno.1996.0192 |display-authors=etal}} | *{{cite journal | vauthors=Cerretti DP, Lyman SD, Kozlosky CJ |title=The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3. |journal=Genomics |volume=33 |issue= 2 |pages= 277–82 |year= 1997 |pmid= 8660976 |doi= 10.1006/geno.1996.0192 |display-authors=etal}} | ||
*{{cite journal | vauthors=Gale NW, Holland SJ, Valenzuela DM |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7 |display-authors=etal}} | *{{cite journal | vauthors=Gale NW, Holland SJ, Valenzuela DM |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7 |display-authors=etal}} | ||
*{{cite journal | vauthors=Böhme B, VandenBos T, Cerretti DP |title=Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24747–52 |year= 1996 |pmid= 8798744 |doi=10.1074/jbc.271.40.24747 |display-authors=etal}} | *{{cite journal | vauthors=Böhme B, VandenBos T, Cerretti DP |title=Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24747–52 |year= 1996 |pmid= 8798744 |doi=10.1074/jbc.271.40.24747 |display-authors=etal}} | ||
*{{cite journal | vauthors=Holland SJ, Gale NW, Mbamalu G |title=Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. |journal=Nature |volume=383 |issue= 6602 |pages= 722–5 |year= 1996 |pmid= 8878483 |doi= 10.1038/383722a0 |display-authors=etal}} | *{{cite journal | vauthors=Holland SJ, Gale NW, Mbamalu G |title=Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. |journal=Nature |volume=383 |issue= 6602 |pages= 722–5 |year= 1996 |pmid= 8878483 |doi= 10.1038/383722a0 |display-authors=etal|bibcode=1996Natur.383..722H |hdl=1807/9444 }} | ||
*{{cite journal | author= Ephnomenclaturecommittee|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0 }} | *{{cite journal | author= Ephnomenclaturecommittee|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0 }} | ||
*{{cite journal | vauthors=Feldman GJ, Ward DE, Lajeunie-Renier E |title=A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1937–41 |year= 1998 |pmid= 9302274 |doi=10.1093/hmg/6.11.1937 |display-authors=etal}} | *{{cite journal | vauthors=Feldman GJ, Ward DE, Lajeunie-Renier E |title=A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1937–41 |year= 1998 |pmid= 9302274 |doi=10.1093/hmg/6.11.1937 |display-authors=etal}} | ||
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Ephrin-B1 is a protein that in humans is encoded by the EFNB1 gene.[1][2]
This gene encodes a member of the ephrin family. The encoded protein is a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. It may play a role in cell adhesion and function in the development or maintenance of the nervous system.[3]
Mutations in this protein are responsible for most cases of craniofrontonasal syndrome.[4][5][6]
Interactions
EFNB1 has been shown to interact with SDCBP.[7]
References
- ↑ Fletcher FA, Huebner K, Shaffer LG, Fairweather ND, Monaco AP, Muller U, Druck T, Simoneaux DK, Chelly J, Belmont JW, et al. (Jul 1995). "Assignment of the gene (EPLG2) encoding a high-affinity binding protein for the receptor tyrosine kinase Elk to a 200-kilobasepair region in human chromosome Xq12". Genomics. 25 (1): 334–5. doi:10.1016/0888-7543(95)80156-G. PMID 7774950.
- ↑ Shotelersuk V, Siriwan P, Ausavarat S (Mar 2006). "A novel mutation in EFNB1, probably with a dominant negative effect, underlying craniofrontonasal syndrome". Cleft Palate Craniofac J. 43 (2): 152–4. doi:10.1597/05-014.1. PMID 16526919.
- ↑ "Entrez Gene: EFNB1 ephrin-B1".
- ↑ Wieland I, Weidner C, Ciccone R, et al. (December 2007). "Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome". Clin. Genet. 72 (6): 506–16. doi:10.1111/j.1399-0004.2007.00905.x. PMID 17941886.
- ↑ Twigg SR, Kan R, Babbs C, Bochukova EG, Robertson SP, Wall SA, Morriss-Kay GM, Wilkie AO (Jun 2004). "Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome". Proc Natl Acad Sci U S A. 101 (23): 8652–7. Bibcode:2004PNAS..101.8652T. doi:10.1073/pnas.0402819101. PMC 423250. PMID 15166289.
- ↑ Wieland I, Jakubiczka S, Muschke P, Cohen M, Thiele H, Gerlach KL, Adams RH, Wieacker P (Jun 2004). "Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome". Am J Hum Genet. 74 (6): 1209–15. doi:10.1086/421532. PMC 1182084. PMID 15124102.
- ↑ Lin, D; Gish G D; Songyang Z; Pawson T (Feb 1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. ISSN 0021-9258. PMID 9920925.
Further reading
- Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annu. Rev. Neurosci. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
- Zhou R (1998). "The Eph family receptors and ligands". Pharmacol. Ther. 77 (3): 151–81. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626.
- Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. PMID 10207129.
- Wilkinson DG (2000). Eph receptors and ephrins: regulators of guidance and assembly. Int. Rev. Cytol. International Review of Cytology. 196. pp. 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN 9780123646002. PMID 10730216.
- Xu Q, Mellitzer G, Wilkinson DG (2001). "Roles of Eph receptors and ephrins in segmental patterning". Philos. Trans. R. Soc. Lond. B Biol. Sci. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993.
- Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. doi:10.1038/35058515. PMID 11256076.
- Davis S, Gale NW, Aldrich TH, et al. (1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science. 266 (5186): 816–9. Bibcode:1994Sci...266..816D. doi:10.1126/science.7973638. PMID 7973638.
- Beckmann MP, Cerretti DP, Baum P, et al. (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". EMBO J. 13 (16): 3757–62. PMC 395287. PMID 8070404.
- Cerretti DP, Lyman SD, Kozlosky CJ, et al. (1997). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.
- Gale NW, Holland SJ, Valenzuela DM, et al. (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474.
- Böhme B, VandenBos T, Cerretti DP, et al. (1996). "Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity". J. Biol. Chem. 271 (40): 24747–52. doi:10.1074/jbc.271.40.24747. PMID 8798744.
- Holland SJ, Gale NW, Mbamalu G, et al. (1996). "Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands". Nature. 383 (6602): 722–5. Bibcode:1996Natur.383..722H. doi:10.1038/383722a0. hdl:1807/9444. PMID 8878483.
- Ephnomenclaturecommittee (1997). "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. doi:10.1016/S0092-8674(00)80500-0. PMID 9267020.
- Feldman GJ, Ward DE, Lajeunie-Renier E, et al. (1998). "A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22". Hum. Mol. Genet. 6 (11): 1937–41. doi:10.1093/hmg/6.11.1937. PMID 9302274.
- Torres R, Firestein BL, Dong H, et al. (1999). "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands". Neuron. 21 (6): 1453–63. doi:10.1016/S0896-6273(00)80663-7. PMID 9883737.
- Lin D, Gish GD, Songyang Z, Pawson T (1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. PMID 9920925.
- Brückner K, Pablo Labrador J, Scheiffele P, et al. (1999). "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains". Neuron. 22 (3): 511–24. doi:10.1016/S0896-6273(00)80706-0. PMID 10197531.
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