Structural Basis for Recruitment of Mitochondrial Fission Complexes By Fis1

Journal Article · Thu Jun 04 04:00:00 EDT 2009 · Proc. Nat. Acad. Sci. 104:18526,2007

OSTI ID:953915

Zhang, Y; Chan, D C

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.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 953915
• Report Number(s): SLAC-REPRINT-2009-477
• Journal Information: Proc. Nat. Acad. Sci. 104:18526,2007, Journal Name: Proc. Nat. Acad. Sci. 104:18526,2007 Journal Issue: 47 Vol. 104; ISSN 0027-8424; ISSN PNASA6
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
APOPTOSIS
COMPLEXES
FISSION
GENETICS
IN VIVO
INTERACTIONS
INTERFACES
MEMBRANE PROTEINS
MITOCHONDRIA
Other
OTHER
PHYSIOLOGY
SHAPE
SURFACES
YEASTS