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LEMD3  -  LEM domain containing 3

Homo sapiens

 
 
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Disease relevance of LEMD3

 

High impact information on LEMD3

 

Biological context of LEMD3

 

Anatomical context of LEMD3

 

Physical interactions of LEMD3

  • MAN1 is an integral protein of the inner nuclear membrane that interacts with nuclear lamins and emerin, thus playing a role in nuclear organization [4].
 

Regulatory relationships of LEMD3

  • MAN1 is a vertebrate nuclear inner membrane protein that inhibits Smad signaling downstream of transforming growth factor beta [2].
 

Other interactions of LEMD3

  • Proposed MAN1-emerin complexes are discussed in the context of EDMD disease mechanisms and potential in vivo functions [2].
  • Antibodies against MAN1 were able to co-immunoprecipiate Smad2 from cells, demonstrating that they reside in the same complex in vivo [7].
  • In a yeast two-hybrid screen using the C-terminal domain of MAN1 as bait, eight positive clones were obtained that encoded Smad3 [7].
  • MAN1, through the RNA recognition motif, associates with R-Smads but not Smad4 at the inner nuclear membrane in a ligand-independent manner [10].
  • Here we report the identification of SANE (Smad1 Antagonistic Effector), a novel protein with significant sequence similarity to nuclear envelop proteins such as MAN1 [11].
 

Analytical, diagnostic and therapeutic context of LEMD3

References

  1. Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. Hellemans, J., Preobrazhenska, O., Willaert, A., Debeer, P., Verdonk, P.C., Costa, T., Janssens, K., Menten, B., Van Roy, N., Vermeulen, S.J., Savarirayan, R., Van Hul, W., Vanhoenacker, F., Huylebroeck, D., De Paepe, A., Naeyaert, J.M., Vandesompele, J., Speleman, F., Verschueren, K., Coucke, P.J., Mortier, G.R. Nat. Genet. (2004) [Pubmed]
  2. Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. Mansharamani, M., Wilson, K.L. J. Biol. Chem. (2005) [Pubmed]
  3. Deactivating Germline Mutations in LEMD3 Cause Osteopoikilosis and Buschke-Ollendorff Syndrome, but Not Sporadic Melorheostosis*. Mumm, S., Wenkert, D., Zhang, X., McAlister, W.H., Mier, R.J., Whyte, M.P. J. Bone Miner. Res. (2007) [Pubmed]
  4. The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain. Caputo, S., Couprie, J., Duband-Goulet, I., Kondé, E., Lin, F., Braud, S., Gondry, M., Gilquin, B., Worman, H.J., Zinn-Justin, S. J. Biol. Chem. (2006) [Pubmed]
  5. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. Cai, M., Huang, Y., Ghirlando, R., Wilson, K.L., Craigie, R., Clore, G.M. EMBO J. (2001) [Pubmed]
  6. MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans. Liu, J., Lee, K.K., Segura-Totten, M., Neufeld, E., Wilson, K.L., Gruenbaum, Y. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling. Lin, F., Morrison, J.M., Wu, W., Worman, H.J. Hum. Mol. Genet. (2005) [Pubmed]
  8. Germline LEMD3 mutations are rare in sporadic patients with isolated melorheostosis. Hellemans, J., Debeer, P., Wright, M., Janecke, A., Kjaer, K.W., Verdonk, P.C., Savarirayan, R., Basel, L., Moss, C., Roth, J., David, A., De Paepe, A., Coucke, P., Mortier, G.R. Hum. Mutat. (2006) [Pubmed]
  9. Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane. Wu, W., Lin, F., Worman, H.J. J. Cell. Sci. (2002) [Pubmed]
  10. The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines. Pan, D., Estévez-Salmerón, L.D., Stroschein, S.L., Zhu, X., He, J., Zhou, S., Luo, K. J. Biol. Chem. (2005) [Pubmed]
  11. SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1. Raju, G.P., Dimova, N., Klein, P.S., Huang, H.C. J. Biol. Chem. (2003) [Pubmed]
  12. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. Lin, F., Blake, D.L., Callebaut, I., Skerjanc, I.S., Holmer, L., McBurney, M.W., Paulin-Levasseur, M., Worman, H.J. J. Biol. Chem. (2000) [Pubmed]
 
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