The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

LDB2  -  LIM domain binding 2

Homo sapiens

Synonyms: CLIM-1, CLIM1, Carboxyl-terminal LIM domain-binding protein 1, LDB-2, LDB1, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on LDB2

  • These findings constitute the first molecular definition of LIM-mediated protein-protein interactions and suggest a mechanism by which ldb1 can bind a variety of LIM domains that share low sequence homology [1].
  • These data demonstrate one function for the LIM-binding protein Ldb1 and establish a function for the LIM-only protein Lmo2 as an obligatory component of an oligomeric, DNA-binding complex which may play a role in haematopoiesis [2].
  • We identified Ssdp proteins (previously described as sequence-specific, single-stranded-DNA-binding proteins) as components of Ldb1-associated nuclear complexes in HeLa cells [3].
  • The latter is a phosphoprotein and binds to LMO1 in its phosphorylated state and essentially all the LMO1 and LDB1 protein in the T cell line is part of the complex [4].
  • LMO4 mRNA was amplified in four of six carcinoma tissues and eight of 12 carcinoma cell lines, and LDB1 in three carcinoma tissues and 11 cell lines examined [5].
 

Biological context of LDB2

  • The LMO1 AND LDB1 proteins interact in human T cell acute leukaemia with the chromosomal translocation t(11;14)(p15;q11) [4].
  • Through a combination of bioinformatics and analysis of gene-trapped mouse clones, Enkhmandakh et al. were able to deduce the modular function for a part of Ssdp1, a crucial component of the Ldb1 transcriptional complex, which plays a central role in mammalian head development [6].
  • The conditioned state of a precipitation membrane with its particular properties exists within a limited range of membrane potentials and requires certain minimum concentrations, Clim, of the generating ions in the adjoining solutions [7].
  • The farnesylation consensus motif CLIM is located in the PEX19 domain D3 [8].
  • Urodynamic assessment and quantification of prostatic obstruction before and after transurethral resection of the prostate: standardization with the aid of the computer program CLIM [9].
 

Analytical, diagnostic and therapeutic context of LDB2

  • These findings form strong arguments for including CLIM parameters in the preoperative assessment to perform a TURP [9].

References

  1. Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4. Deane, J.E., Mackay, J.P., Kwan, A.H., Sum, E.Y., Visvader, J.E., Matthews, J.M. EMBO J. (2003) [Pubmed]
  2. The LIM-only protein Lmo2 is a bridging molecule assembling an erythroid, DNA-binding complex which includes the TAL1, E47, GATA-1 and Ldb1/NLI proteins. Wadman, I.A., Osada, H., Grütz, G.G., Agulnick, A.D., Westphal, H., Forster, A., Rabbitts, T.H. EMBO J. (1997) [Pubmed]
  3. Ssdp proteins interact with the LIM-domain-binding protein Ldb1 to regulate development. Chen, L., Segal, D., Hukriede, N.A., Podtelejnikov, A.V., Bayarsaihan, D., Kennison, J.A., Ogryzko, V.V., Dawid, I.B., Westphal, H. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. The LMO1 AND LDB1 proteins interact in human T cell acute leukaemia with the chromosomal translocation t(11;14)(p15;q11). Valge-Archer, V., Forster, A., Rabbitts, T.H. Oncogene (1998) [Pubmed]
  5. The LIM-only protein, LMO4, and the LIM domain-binding protein, LDB1, expression in squamous cell carcinomas of the oral cavity. Mizunuma, H., Miyazawa, J., Sanada, K., Imai, K. Br. J. Cancer (2003) [Pubmed]
  6. Proline-rich regions in transcriptional complexes: heading in many directions. Neduva, V., Russell, R.B. Sci. STKE (2007) [Pubmed]
  7. Precipitation membranes: III. Reversible changes of membrane properties induced by alterations in ionic concentrations. Hirsch-Ayalon, P. J. Membr. Biol. (1979) [Pubmed]
  8. Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly. Mayerhofer, P.U., Kattenfeld, T., Roscher, A.A., Muntau, A.C. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  9. Urodynamic assessment and quantification of prostatic obstruction before and after transurethral resection of the prostate: standardization with the aid of the computer program CLIM. Rollema, H.J., van Mastrigt, R., Janknegt, R.A. Urologia internationalis. (1991) [Pubmed]
 
WikiGenes - Universities