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Dnm1l  -  dynamin 1-like

Rattus norvegicus

Synonyms: DLP1, Dlp1, Dnml1, Drp1, Dynamin-1-like protein, ...
 
 
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High impact information on Dnm1l

  • Molecular manipulations of dynamin-like GTPases Drp1 and OPA1 that reduce dendritic mitochondria content lead to loss of synapses and dendritic spines, whereas increasing dendritic mitochondrial content or mitochondrial activity enhances the number and plasticity of spines and synapses [1].
  • DLP1 is enriched in subcellular membrane fractions of cytoplasmic vesicles and endoplasmic reticulum [2].
  • A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells [2].
  • Here, we have tested if novel dynamin-like proteins are expressed in mammalian cells to support vesicle trafficking processes at cytoplasmic sites distinct from the plasma membrane [2].
  • These results suggest that hFis1 participates in mitochondrial fission through an interaction that recruits DLP1 from the cytosol [3].
 

Biological context of Dnm1l

 

Anatomical context of Dnm1l

 

Associations of Dnm1l with chemical compounds

  • In addition, immunoblot analysis revealed the presence of DLP1 in highly purified peroxisomal fractions from rat liver and an increase of DLP1 after treatment of rats with the peroxisome proliferator bezafibrate [7].
 

Other interactions of Dnm1l

  • Transcript levels of gene products involved in mtDNA maintenance (Tfam), mitochondrial protein degradation (LON protease), fusion (fuzzy onion homolog), and fission (dynamin-like protein, synaptojanin-2alpha) were also unchanged [8].
  • However, the side chains known to be functionally important in beta-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function [9].
 

Analytical, diagnostic and therapeutic context of Dnm1l

References

  1. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Li, Z., Okamoto, K., Hayashi, Y., Sheng, M. Cell (2004) [Pubmed]
  2. A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. Yoon, Y., Pitts, K.R., Dahan, S., McNiven, M.A. J. Cell Biol. (1998) [Pubmed]
  3. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Yoon, Y., Krueger, E.W., Oswald, B.J., McNiven, M.A. Mol. Cell. Biol. (2003) [Pubmed]
  4. The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Pitts, K.R., Yoon, Y., Krueger, E.W., McNiven, M.A. Mol. Biol. Cell (1999) [Pubmed]
  5. Three rat brain alternative splicing dynamin-like protein variants: interaction with the glycogen synthase kinase 3beta and action as a substrate. Chen, C.H., Hwang, S.L., Howng, S.L., Chou, C.K., Hong, Y.R. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  6. Mammalian dynamin-like protein DLP1 tubulates membranes. Yoon, Y., Pitts, K.R., McNiven, M.A. Mol. Biol. Cell (2001) [Pubmed]
  7. Dynamin-like protein 1 is involved in peroxisomal fission. Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M.A., Schrader, M. J. Biol. Chem. (2003) [Pubmed]
  8. Bioenergetic remodeling of heart during treatment of spontaneously hypertensive rats with enalapril. Leary, S.C., Michaud, D., Lyons, C.N., Hale, T.M., Bushfield, T.L., Adams, M.A., Moyes, C.D. Am. J. Physiol. Heart Circ. Physiol. (2002) [Pubmed]
  9. Solution structure of a defensin-like peptide from platypus venom. Torres, A.M., Wang, X., Fletcher, J.I., Alewood, D., Alewood, P.F., Smith, R., Simpson, R.J., Nicholson, G.M., Sutherland, S.K., Gallagher, C.H., King, G.F., Kuchel, P.W. Biochem. J. (1999) [Pubmed]
 
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