DNM1

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Protein-coding gene in the species Homo sapiens

title: "DNM1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/DNM1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.

Function

Dynamin possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the dynamin, which can also self-assemble leading to stimulation of GTPase activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the genome, particularly on chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described.

Role in disease

De novo mutations in DNM1 have been associated with a severe form of childhood epilepsy called developmental and epileptic encephalopathy. Most pathogenic variants are missense variants, and have been shown to impair synaptic vesicle endocytosis in a dominant negative manner.

Interactions

DNM1 has been shown to interact with:

References

References

  1. (October 1990). "Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins". Nature.
  2. (July 1997). "Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis". Genomics.
  3. "Entrez Gene: DNM1 dynamin 1".
  4. (June 2015). "Epileptic encephalopathy-causing mutations in DNM1 impair synaptic vesicle endocytosis". Neurology. Genetics.
  5. (October 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem..
  6. (October 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Mol. Biol. Cell.
  7. (August 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett..
  8. (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem..
  9. (May 1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence". J. Biol. Chem..
  10. (September 2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem..
  11. (February 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem..
  12. (January 1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer.
  13. (January 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal..
  14. (December 2000). "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis". J. Cell Sci..
  15. (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem..

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