Dynamin: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


The GTPase domain of DNM 1 contains 5 nucleotide binding motifs all of which interact with the bound GDP.  <scene name='80/808513/Cv/2'>Motif #1 GGQSAGKS</scene> residues 38-45; motif #2 is residue T65; Motif #3 DLPG residues 136-139; Motif #4 TKLD residues 205-208; Motif #5 NRSQKDIDGKK reidues 236-246<ref>PMID:26612256</ref>.  
The GTPase domain of DNM 1 contains 5 nucleotide binding motifs all of which interact with the bound GDP.  <scene name='80/808513/Cv/6'>Motif #1 GGQSAGKS</scene> residues 38-45; motif #2 is residue T65; Motif #3 DLPG residues 136-139; <scene name='80/808513/Cv/7'>Motif #4 TKLD</scene> residues 205-208; <scene name='80/808513/Cv/8'>Motif #5 NRSQKDIDGKK</scene> reidues 236-246<ref>PMID:26612256</ref>. <scene name='80/808513/Cv/9'>Whole binding site</scene>.  


==Dynamin 3D structures==
==Dynamin 3D structures==

Revision as of 16:05, 19 February 2019


Function

Dynamin (DNM) is a GTPase which mediates endocytosis in membrane scission[1] and organelle division. Dynamin 1-like mediates outer mitochondrial membrane fission[2]. DNM is a multidomain GTPase. Mammalian genomes contain 3 DNM genes which show ca. 80% homology. DNM 1 is localized to neurons, DNM 2 is expressed ubiquitously and DNM 3 is found predominantly in the brain[3]. The DNM 1 domain structure includes GTPase, middle, Plextrin homology, GTPase effector and proline- and arginine-rich (PRD) domains.

Disease

Mutations in DNM-2 cause centronuclear myopathy[4].

Structural highlights

The GTPase domain of DNM 1 contains 5 nucleotide binding motifs all of which interact with the bound GDP. residues 38-45; motif #2 is residue T65; Motif #3 DLPG residues 136-139; residues 205-208; reidues 236-246[5]. .

Dynamin 3D structures

See Dynamin 3D structures

Human dynamin 1 GTPase+GTPase effector domains complex with GDP and ethylene glycol (PDB code 5d3q)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Taylor MJ, Lampe M, Merrifield CJ. A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis. PLoS Biol. 2012;10(4):e1001302. doi: 10.1371/journal.pbio.1001302. Epub 2012 Apr , 10. PMID:22505844 doi:http://dx.doi.org/10.1371/journal.pbio.1001302
  2. Frank S, Gaume B, Bergmann-Leitner ES, Leitner WW, Robert EG, Catez F, Smith CL, Youle RJ. The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev Cell. 2001 Oct;1(4):515-25. PMID:11703942
  3. Ferguson SM, De Camilli P. Dynamin, a membrane-remodelling GTPase. Nat Rev Mol Cell Biol. 2012 Jan 11;13(2):75-88. doi: 10.1038/nrm3266. PMID:22233676 doi:http://dx.doi.org/10.1038/nrm3266
  4. Bitoun M, Maugenre S, Jeannet PY, Lacene E, Ferrer X, Laforet P, Martin JJ, Laporte J, Lochmuller H, Beggs AH, Fardeau M, Eymard B, Romero NB, Guicheney P. Mutations in dynamin 2 cause dominant centronuclear myopathy. Nat Genet. 2005 Nov;37(11):1207-9. Epub 2005 Oct 16. PMID:16227997 doi:ng1657
  5. Anand R, Eschenburg S, Reubold TF. Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state. Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256 doi:http://dx.doi.org/10.1016/j.bbrc.2015.11.074

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