| Structural highlights
2pqn is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Related: | 2pqr |
| Gene: | FIS1, MDV2 (ATCC 18824), MDV1, FIS2, GAG3, NET2 (ATCC 18824) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FIS1_YEAST] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.[1] [2] [3] [4] [MDV1_YEAST] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.[5] [6] [7] [8] [9] [10] [11]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using crystallographic analysis of adaptor-Fis1 complexes, we show that these adaptors use two helices to bind to both the concave and convex surfaces of the Fis1 TPR domain. Fis1 therefore contains two interaction interfaces, a binding mode that, to our knowledge, has not been observed previously for TPR domains. Genetic and biochemical studies indicate that both binding interfaces are important for binding of Mdv1 and Caf4 to Fis1 and for mitochondrial fission activity in vivo. Our results reveal how Fis1 recruits the mitochondrial fission complex and will facilitate efforts to manipulate mitochondrial fission.
Structural basis for recruitment of mitochondrial fission complexes by Fis1.,Zhang Y, Chan DC Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537[12]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000 Oct 16;151(2):367-80. PMID:11038183
- ↑ Tieu Q, Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J Cell Biol. 2000 Oct 16;151(2):353-66. PMID:11038182
- ↑ Tieu Q, Okreglak V, Naylor K, Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002 Aug 5;158(3):445-52. Epub 2002 Aug 5. PMID:12163467 doi:http://dx.doi.org/10.1083/jcb.200205031
- ↑ Jakobs S, Martini N, Schauss AC, Egner A, Westermann B, Hell SW. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J Cell Sci. 2003 May 15;116(Pt 10):2005-14. Epub 2003 Apr 1. PMID:12679388 doi:http://dx.doi.org/10.1242/jcs.00423
- ↑ Tieu Q, Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J Cell Biol. 2000 Oct 16;151(2):353-66. PMID:11038182
- ↑ Fekkes P, Shepard KA, Yaffe MP. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J Cell Biol. 2000 Oct 16;151(2):333-40. PMID:11038180
- ↑ Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000 Oct 16;151(2):367-80. PMID:11038183
- ↑ Tieu Q, Okreglak V, Naylor K, Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002 Aug 5;158(3):445-52. Epub 2002 Aug 5. PMID:12163467 doi:http://dx.doi.org/10.1083/jcb.200205031
- ↑ Karren MA, Coonrod EM, Anderson TK, Shaw JM. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J Cell Biol. 2005 Oct 24;171(2):291-301. PMID:16247028 doi:http://dx.doi.org/10.1083/jcb.200506158
- ↑ Naylor K, Ingerman E, Okreglak V, Marino M, Hinshaw JE, Nunnari J. Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J Biol Chem. 2006 Jan 27;281(4):2177-83. Epub 2005 Nov 4. PMID:16272155 doi:http://dx.doi.org/10.1074/jbc.M507943200
- ↑ Bhar D, Karren MA, Babst M, Shaw JM. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J Biol Chem. 2006 Jun 23;281(25):17312-20. Epub 2006 Apr 6. PMID:16601120 doi:http://dx.doi.org/10.1074/jbc.M513530200
- ↑ Zhang Y, Chan DC. Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537
|
