Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. J Biol Chem 2007 Nov 16;282(46):33769-33775
Date
09/22/2007Pubmed ID
17884824Pubmed Central ID
PMC3046406DOI
10.1074/jbc.M700807200Scopus ID
2-s2.0-36348930592 (requires institutional sign-in at Scopus site) 52 CitationsAbstract
Recruitment of a dynamin-like GTPase (Drp1/Dlp1/Dnm1) to membranes requires the mitochondrial dynamics protein Fis1. Mdv1 has been proposed to act as an adaptor between Fis1 and Dnm1 in Saccharomyces cerevisiae. We show that S. cerevisiae Fis1 binds directly to Dnm1 and to Mdv1. Two Fis1 regions have been previously implicated in Mdv1 recruitment: an N-terminal "arm" and a concave surface formed by evolutionarily conserved residues in the tetratricopeptide repeat domain. Perturbing either Fis1 region does not affect Mdv1 binding, but both regions influence Dnm1 binding. Fis1 lacking its N-terminal arm binds tightly to Dnm1, and binding is abolished by mutations to the Fis1 concave surface. The Fis1-Dnm1 interaction decreases more than 100-fold in the presence of the Fis1 arm, suggesting that the arm acts in an autoinhibitory manner to restrict access to the Dnm1 binding site on Fis1. Our data indicate that the concave surface of the Fis1 tetratricopeptide repeat-like domain is evolutionarily conserved to bind the dynamin-like GTPase Dnm1 and not Mdv1 as previously predicted.
Author List
Wells RC, Picton LK, Williams SCP, Tan FJ, Hill RBMESH terms used to index this publication - Major topics in bold
Adaptor Proteins, Signal TransducingBinding Sites
Carrier Proteins
Dynamins
Evolution, Molecular
Fungal Proteins
GTP Phosphohydrolases
Mitochondrial Proteins
Models, Molecular
Molecular Conformation
Mutagenesis, Site-Directed
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
