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DYNLL1  -  dynein, light chain, LC8-type 1

Homo sapiens

Synonyms: 8 kDa dynein light chain, DLC1, DLC8, DNCL1, DNCLC1, ...
 
 
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Disease relevance of DYNLL1

 

High impact information on DYNLL1

  • We screened an expression library for proteins that bind the PTH mRNA 3'-UTR, and the sequence of 1 clone was identical to that of the dynein light chain LC8, a component of the dynein complexes that translocate cytoplasmic components along microtubules [2].
 

Chemical compound and disease context of DYNLL1

 

Biological context of DYNLL1

  • The LC8-binding domain was mapped to a short peptide segment immediately N-terminal to the kinetochore localization region of 53BP1 [4].
  • We have performed a fine mapping of the 8 kDa dynein light chain (LC8) binding sites throughout the development of a library of consecutive synthetic dodecapeptides covering the amino acid sequences of the various proteins known to interact with this dynein member according to the yeast two hybrid system [5].
  • The structure provides key insights into dimerization of and peptide binding by the multifunctional PIN/LC8 protein [6].
  • The N-terminal domain of the intermediate chain, IC1-289, contains the binding sites for the light chains, and is a highly disordered monomer but gains helical structure upon binding to light chains LC8 and Tctex-1 [7].
 

Anatomical context of DYNLL1

  • Interestingly, we found that LC8a co-localizes with TRPS1 in dot-like structures in the cell nucleus [8].
  • The cytoskeletal organization and dynamics of this syncytium are poorly understood, but predominant motor components are the LC8 class of cytoplasmic dynein light chains (DLC) [9].
 

Associations of DYNLL1 with chemical compounds

  • Yeast two-hybrid analysis has revealed that in brain, LC8 associates directly with several proteins such as neuronal nitric oxide synthase, guanylate kinase domain-associated protein and gephyrin [10].
 

Physical interactions of DYNLL1

  • The LC8-binding domain is completely separated from the p53-binding domain in 53BP1 [4].
 

Other interactions of DYNLL1

 

Analytical, diagnostic and therapeutic context of DYNLL1

References

  1. Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. Jacob, Y., Badrane, H., Ceccaldi, P.E., Tordo, N. J. Virol. (2000) [Pubmed]
  2. Dynein light chain binding to a 3'-untranslated sequence mediates parathyroid hormone mRNA association with microtubules. Epstein, E., Sela-Brown, A., Ringel, I., Kilav, R., King, S.M., Benashski, S.E., Yisraeli, J.K., Silver, J., Naveh-Many, T. J. Clin. Invest. (2000) [Pubmed]
  3. Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique. Martínez-Moreno, M., Navarro-Lérida, I., Roncal, F., Albar, J.P., Alonso, C., Gavilanes, F., Rodríguez-Crespo, I. FEBS Lett. (2003) [Pubmed]
  4. The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation. Lo, K.W., Kan, H.M., Chan, L.N., Xu, W.G., Wang, K.P., Wu, Z., Sheng, M., Zhang, M. J. Biol. Chem. (2005) [Pubmed]
  5. Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique. Rodríguez-Crespo, I., Yélamos, B., Roncal, F., Albar, J.P., Ortiz de Montellano, P.R., Gavilanes, F. FEBS Lett. (2001) [Pubmed]
  6. Structure of the PIN/LC8 dimer with a bound peptide. Liang, J., Jaffrey, S.R., Guo, W., Snyder, S.H., Clardy, J. Nat. Struct. Biol. (1999) [Pubmed]
  7. Heteronuclear NMR identifies a nascent helix in intrinsically disordered Dynein intermediate chain: implications for folding and dimerization. Benison, G., Nyarko, A., Barbar, E. J. Mol. Biol. (2006) [Pubmed]
  8. Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1. Kaiser, F.J., Tavassoli, K., Van den Bemd, G.J., Chang, G.T., Horsthemke, B., Möröy, T., Lüdecke, H.J. Hum. Mol. Genet. (2003) [Pubmed]
  9. The cellular distribution and stage-specific expression of two dynein light chains from the human blood fluke Schistosoma japonicum. Zhang, L.H., McManus, D.P., Sunderland, P., Lu, X.M., Ye, J.J., Loukas, A., Jones, M.K. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  10. Proteomic identification of brain proteins that interact with dynein light chain LC8. Navarro-Lérida, I., Martínez Moreno, M., Roncal, F., Gavilanes, F., Albar, J.P., Rodríguez-Crespo, I. Proteomics (2004) [Pubmed]
  11. 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]
  12. Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. Dick, T., Ray, K., Salz, H.K., Chia, W. Mol. Cell. Biol. (1996) [Pubmed]
 
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