DNM1

From Wikipedia, the free encyclopedia

Dynamin 1

PDB rendering based on 1dyn.

Available structures: 1dyn, 2aka, 2dyn

Identifiers

Symbol(s)

DNM1; DNM

External IDs

OMIM: 602377 MGI: 107384 HomoloGene: 68397

Gene ontology
Molecular Function:	• nucleotide binding • motor activity • GTPase activity • protein binding • GTP binding • kinase activity • transferase activity • hydrolase activity
Cellular Component:	• microtubule • coated pit
Biological Process:	• endocytosis • receptor-mediated endocytosis • synaptic transmission

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001005336 (mRNA)
NP_001005336 (protein)

NM_010065 (mRNA)
NP_034195 (protein)

Location

Chr 9: 130.01 - 130.06 Mb

Chr 2: 32.13 - 32.18 Mb

Pubmed search

[1]

[2]

Dynamin 1, also known as DNM1, is a human gene.

This gene encodes a member of the dynamin subfamily of GTP-binding proteins. The encoded protein 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 encoded protein, 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.^[1]

[edit] References

^ Entrez Gene: DNM1 dynamin 1.

[edit] Further reading

Sever S (2003). "Dynamin and endocytosis.". Curr. Opin. Cell Biol. 14 (4): 463-7. PMID 12383797.
Wiejak J, Wyroba E (2003). "Dynamin: characteristics, mechanism of action and function.". Cell. Mol. Biol. Lett. 7 (4): 1073-80. PMID 12511974.
Orth JD, McNiven MA (2003). "Dynamin at the actin-membrane interface.". Curr. Opin. Cell Biol. 15 (1): 31-9. PMID 12517701.
Obar RA, Collins CA, Hammarback JA, et al. (1990). "Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins.". Nature 347 (6290): 256-61. doi:10.1038/347256a0. PMID 2144893.
Timm D, Salim K, Gout I, et al. (1995). "Crystal structure of the pleckstrin homology domain from dynamin.". Nat. Struct. Biol. 1 (11): 782-8. PMID 7634088.
Downing AK, Driscoll PC, Gout I, et al. (1995). "Three-dimensional solution structure of the pleckstrin homology domain from dynamin.". Curr. Biol. 4 (10): 884-91. PMID 7850421.
Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB (1994). "Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin.". Cell 79 (2): 199-209. PMID 7954789.
van der Bliek AM, Redelmeier TE, Damke H, et al. (1993). "Mutations in human dynamin block an intermediate stage in coated vesicle formation.". J. Cell Biol. 122 (3): 553-63. PMID 8101525.
Miki H, Miura K, Matuoka K, et al. (1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain.". J. Biol. Chem. 269 (8): 5489-92. PMID 8119878.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Sontag JM, Fykse EM, Ushkaryov Y, et al. (1994). "Differential expression and regulation of multiple dynamins.". J. Biol. Chem. 269 (6): 4547-54. PMID 8308025.
Newman-Smith ED, Shurland DL, van der Bliek AM (1997). "Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis.". Genomics 41 (2): 286-9. doi:10.1006/geno.1996.4596. PMID 9143509.
Grabs D, Slepnev VI, Songyang Z, et al. (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. 272 (20): 13419-25. PMID 9148966.
Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform.". J. Biol. Chem. 272 (26): 16700-6. PMID 9195986.
Ringstad N, Nemoto Y, De Camilli P (1997). "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain.". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8569-74. PMID 9238017.
McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin.". FEBS Lett. 413 (2): 319-22. PMID 9280305.
Wigge P, Köhler K, Vallis Y, et al. (1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis.". Mol. Biol. Cell 8 (10): 2003-15. PMID 9348539.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Witke W, Podtelejnikov AV, Di Nardo A, et al. (1998). "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly.". EMBO J. 17 (4): 967-76. doi:10.1093/emboj/17.4.967. PMID 9463375.
Slepnev VI, Ochoa GC, Butler MH, et al. (1998). "Role of phosphorylation in regulation of the assembly of endocytic coat complexes.". Science 281 (5378): 821-4. PMID 9694653.