Afadin

(Redirected from MLLT4)

Afadin is a protein that in humans is encoded by the AFDN gene.[5]

AFDN
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAFDN, AF6, MLL-AF6, MLLT4, myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4, afadin, adherens junction formation factor, l-afadin
External IDsOMIM: 159559; MGI: 1314653; HomoloGene: 21202; GeneCards: AFDN; OMA:AFDN - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_010806

RefSeq (protein)

NP_034936

Location (UCSC)Chr 6: 167.83 – 167.97 MbChr 17: 13.98 – 14.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998).[supplied by OMIM][6]

Interactions

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Afadin has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130396Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000068036Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Prasad R, Gu Y, Alder H, Nakamura T, Canaani O, Saito H, Huebner K, Gale RP, Nowell PC, Kuriyama K (Dec 1993). "Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation". Cancer Research. 53 (23): 5624–8. PMID 8242616.
  6. ^ "Entrez Gene: MLLT4 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4".
  7. ^ Radziwill G, Erdmann RA, Margelisch U, Moelling K (Jul 2003). "The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain". Molecular and Cellular Biology. 23 (13): 4663–72. doi:10.1128/mcb.23.13.4663-4672.2003. PMC 164848. PMID 12808105.
  8. ^ Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K (Aug 1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proceedings of the National Academy of Sciences of the United States of America. 95 (17): 9779–84. Bibcode:1998PNAS...95.9779H. doi:10.1073/pnas.95.17.9779. PMC 21413. PMID 9707552.
  9. ^ Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
  10. ^ a b c Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  11. ^ a b Yamamoto T, Harada N, Kawano Y, Taya S, Kaibuchi K (May 1999). "In vivo interaction of AF-6 with activated Ras and ZO-1". Biochemical and Biophysical Research Communications. 259 (1): 103–7. doi:10.1006/bbrc.1999.0731. PMID 10334923.
  12. ^ Bégay-Müller V, Ansieau S, Leutz A (Jun 2002). "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Letters. 521 (1–3): 36–8. doi:10.1016/s0014-5793(02)02814-4. PMID 12067721. S2CID 29461336.
  13. ^ Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (May 1999). "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein". The Journal of Cell Biology. 145 (3): 539–49. doi:10.1083/jcb.145.3.539. PMC 2185068. PMID 10225955.
  14. ^ Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y (Apr 2000). "Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities". The Journal of Biological Chemistry. 275 (14): 10291–9. doi:10.1074/jbc.275.14.10291. PMID 10744716.
  15. ^ Reymond N, Borg JP, Lecocq E, Adelaide J, Campadelli-Fiume G, Dubreuil P, Lopez M (Sep 2000). "Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin". Gene. 255 (2): 347–55. doi:10.1016/s0378-1119(00)00316-4. PMID 11024295.
  16. ^ Su L, Hattori M, Moriyama M, Murata N, Harazaki M, Kaibuchi K, Minato N (Apr 2003). "AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1". The Journal of Biological Chemistry. 278 (17): 15232–8. doi:10.1074/jbc.M211888200. hdl:2433/148462. PMID 12590145.
  17. ^ Mandai K, Nakanishi H, Satoh A, Takahashi K, Satoh K, Nishioka H, Mizoguchi A, Takai Y (Mar 1999). "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions". The Journal of Cell Biology. 144 (5): 1001–17. doi:10.1083/jcb.144.5.1001. PMC 2148189. PMID 10085297.
  18. ^ Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (Feb 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". The Journal of Biological Chemistry. 278 (6): 4103–11. doi:10.1074/jbc.M209832200. PMID 12446711.
  19. ^ Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K (Dec 1999). "The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin". Genes to Cells. 4 (12): 757–67. doi:10.1046/j.1365-2443.1999.00297.x. PMID 10620020. S2CID 85747886.
  20. ^ Taya S, Yamamoto T, Kano K, Kawano Y, Iwamatsu A, Tsuchiya T, Tanaka K, Kanai-Azuma M, Wood SA, Mattick JS, Kaibuchi K (Aug 1998). "The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme". The Journal of Cell Biology. 142 (4): 1053–62. doi:10.1083/jcb.142.4.1053. PMC 2132865. PMID 9722616.

Further reading

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