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Gene Review

dyn-1  -  Protein DYN-1

Caenorhabditis elegans

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High impact information on dyn-1

  • With sequenced genomes from Homo sapiens, Drosophila melanogaster, Caenorhabditis elegans, yeast species and Arabidopsis thaliana, we now have a complete picture of the members of the dynamin superfamily from different organisms [1].
  • Thus, ehs-1 and dyn-1 interact genetically [2].
  • Taken together, our results indicate that EHS-1 acts in synaptic vesicle recycling and that its function might be linked to that of dynamin [2].
  • Impairment of EHS-1 function in dyn-1(ky51) worms, which express a mutant form of dynamin and display a temperature-sensitive locomotion defect, resulted in a worsening of the dyn-1 phenotype and uncoordination at the permissive temperature [2].
  • These dyn-1 proteins are highly similar in amino acid sequence, structure, and size to the Drosophila and mammalian dynamins: they contain an N-terminal GTPase, a pleckstrin homology domain, and a C-terminal proline-rich domain [3].

Biological context of dyn-1


Anatomical context of dyn-1

  • Abnormal vesicle structures accumulate in engulfing cells upon dyn-1 inactivation. dyn-1 and ced-1 mutations block the recruitment of intracellular vesicles to pseudopods and phagosomes [5].
  • In Caenorhabditis elegans, dynamin localized to newly formed cleavage furrow membranes and accumulated at the midbody of dividing embryos in a manner similar to dynamin localization in mammalian cells [4].
  • Our results suggest that different dynamin domains contribute to axonal transport and the sequestration of a pool of dynamin molecules in synaptic cytosol [6].

Associations of dyn-1 with chemical compounds

  • Overexpression of a dominant-negative dynamin mutant (DynK44A), but not of a dominant-negative beta-arrestin mutant (Arr319-418), substantially inhibited carbachol-induced internalization of GAR-3 [7].

Other interactions of dyn-1

  • Thus, these data suggest that GAR-3 undergoes agonist-induced internalization via a clathrin- and dynamin-dependent but beta-arrestin-independent pathway [7].

Analytical, diagnostic and therapeutic context of dyn-1


  1. The dynamin superfamily: universal membrane tubulation and fission molecules? Praefcke, G.J., McMahon, H.T. Nat. Rev. Mol. Cell Biol. (2004) [Pubmed]
  2. The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. Salcini, A.E., Hilliard, M.A., Croce, A., Arbucci, S., Luzzi, P., Tacchetti, C., Daniell, L., De Camilli, P., Pelicci, P.G., Di Fiore, P.P., Bazzicalupo, P. Nat. Cell Biol. (2001) [Pubmed]
  3. A dynamin GTPase mutation causes a rapid and reversible temperature-inducible locomotion defect in C. elegans. Clark, S.G., Shurland, D.L., Meyerowitz, E.M., Bargmann, C.I., van der Bliek, A.M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  4. The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis. Thompson, H.M., Skop, A.R., Euteneuer, U., Meyer, B.J., McNiven, M.A. Curr. Biol. (2002) [Pubmed]
  5. C. elegans Dynamin mediates the signaling of phagocytic receptor CED-1 for the engulfment and degradation of apoptotic cells. Yu, X., Odera, S., Chuang, C.H., Lu, N., Zhou, Z. Dev. Cell (2006) [Pubmed]
  6. Contribution of the GTPase domain to the subcellular localization of dynamin in the nematode Caenorhabditis elegans. Labrousse, A.M., Shurland, D.L., van der Bliek, A.M. Mol. Biol. Cell (1998) [Pubmed]
  7. Agonist-induced internalization of the Caenorhabditis elegans muscarinic acetylcholine receptor GAR-3 in Chinese hamster ovary cells. Choi, B., Park, Y.S., Cho, N.J. Neurochem. Res. (2006) [Pubmed]
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