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DYNLL2  -  dynein, light chain, LC8-type 2

Homo sapiens

Synonyms: 8 kDa dynein light chain b, DLC2, DLC8b, DNCL1B, Dlc2, ...
 
 
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Disease relevance of DYNLL2

  • Several years after the isolation of deleted in liver cancer 1 (DLC-1), a gene that encodes a Rho GTPase activating protein, the closely related DLC-2 gene was identified [1].
  • Using cancer-profiling arrays, we detected for the first time down-regulation of DLC-1 expression in renal, uterine and rectal cancers and down-regulation of DLC-2 expression in lung, ovarian, renal, breast, uterine, gastric, colon and rectal tumors [1].
  • We examined DLC-2 expression in DLC-1-negative cell lines derived from human breast, non-small cell lung, and hepatocellular carcinomas, that could be rendered less or non-tumorigenic by ectopic expression of DLC-1 [1].
 

High impact information on DYNLL2

  • S. pombe contains a homolog of the 8-kDa dynein light chain, Dlc2 [2].
  • We investigated the effect of DYNLL2 binding on the structure of a myosin Va heavy chain fragment that contains the DYNLL2 binding site and flanking sequence, only parts of which are strongly predicted to form a coiled coil [3].
  • The Binding of DYNLL2 to Myosin Va Requires Alternatively Spliced Exon B and Stabilizes a Portion of the Myosin's Coiled-Coil Domain [3].
  • Co-localization experiments in a transfected mammalian cell line confirm our finding that exon B is essential for DLC2 binding [4].
  • Bmf-II and Bmf-III were characterized as two splice variants, lacking the BH3 domain but retaining the DLC2 binding domain [5].
 

Biological context of DYNLL2

  • Copurification and pull-down experiments showed that the heavy chain contains a single DYNLL2 binding site and that this site resides within a discontinuity in the myosin's central coiled-coil domain [3].
  • Expression profile of the tumor suppressor genes DLC-1 and DLC-2 in solid tumors [1].
  • Since DLC-1 and -2 are located at chromosome regions that are commonly deleted in cancer cells and have been found to function as tumor suppressor genes, we sought to compare their expression profiles in several common types of cancer and to determine whether dlc1 and dlc2 proteins cooperate in tumor development [1].
 

Anatomical context of DYNLL2

  • Co-localization and biochemical fractionation studies revealed that DLC2 localized to mitochondria [6].
 

Regulatory relationships of DYNLL2

  • This result shows that DLC2 promotes the assembly of the coiled-coil domains of myosin Va [4].
 

Analytical, diagnostic and therapeutic context of DYNLL2

  • Circular dichroism measurements revealed a DYNLL2-induced change in the secondary structure of this dimeric myosin fragment that is consistent with an increase in alpha-helical coiled-coil content [3].
  • Analytical ultracentrifugation yielded an apparent association constant of approximately 3 x 10(6) M(-1) for the interaction of DYNLL2 with the dimeric myosin fragment [3].
  • Fragments of the human myosin Va tail and the DLC2 isoform were expressed, and their complex formation was analyzed by pull-down assays, gel filtration, and spectroscopic methods [4].
  • Using quantitative RT-PCR we detected a significantly lower expression of DLC-1 and DLC-2 in high percentage of tumors, suggesting that deficiency of either DLC gene facilitates dissemination of breast carcinoma cells to secondary sites [1].

References

  1. Expression profile of the tumor suppressor genes DLC-1 and DLC-2 in solid tumors. Ullmannova, V., Popescu, N.C. Int. J. Oncol. (2006) [Pubmed]
  2. The 14-kDa dynein light chain-family protein Dlc1 is required for regular oscillatory nuclear movement and efficient recombination during meiotic prophase in fission yeast. Miki, F., Okazaki, K., Shimanuki, M., Yamamoto, A., Hiraoka, Y., Niwa, O. Mol. Biol. Cell (2002) [Pubmed]
  3. The Binding of DYNLL2 to Myosin Va Requires Alternatively Spliced Exon B and Stabilizes a Portion of the Myosin's Coiled-Coil Domain. Wagner, W., Fodor, E., Ginsburg, A., Hammer, J.A. Biochemistry (2006) [Pubmed]
  4. Alternatively spliced exon B of Myosin va is essential for binding the tail-associated light chain shared by Dynein. H??di, Z., N??meth, A.L., Radnai, L., Het??nyi, C., Schlett, K., Bodor, A., Perczel, A., Nyitray, L. Biochemistry (2006) [Pubmed]
  5. Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. Morales, A.A., Olsson, A., Celsing, F., Osterborg, A., Jondal, M., Osorio, L.M. Leukemia (2004) [Pubmed]
  6. Mitochondrial targeting of growth suppressor protein DLC2 through the START domain. Ng, D.C., Chan, S.F., Kok, K.H., Yam, J.W., Ching, Y.P., Ng, I.O., Jin, D.Y. FEBS Lett. (2006) [Pubmed]
 
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