Intradimer/Intermolecular interactions suggest autoinhibition mechanism in endophilin A1.

ABSTRACT: Endophilin A1 is a homodimeric membrane-binding endocytic accessory protein with a high dimerization affinity. Its function has been hypothesized to involve autoinhibition. However, the autoinhibition mechanism, as well as the physicochemical basis for the high dimerization affinity of endophilin in solution, have remained unclear. In this contribution, we use a Förster resonance energy transfer (FRET) method to investigate the homodimerization mechanism and intradimer molecular interactions in endophilin. For the endophilin N-BAR domain (which lacks the SH3 domain including a linker region of the full length protein), we observe a large temperature dependence of the dimerization affinity and dimer dissociation kinetics, implying large dimerization enthalpy and dissociation activation enth

SUBMITTER: Chen Z 

PROVIDER: S-EPMC3985530 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature