Insights into EB1 structure and the role of its C-terminal domain for discriminating microtubule tips from the lattice.

ABSTRACT: End-binding proteins (EBs) comprise a conserved family of microtubule plus end-tracking proteins. The concerted action of calponin homology (CH), linker, and C-terminal domains of EBs is important for their autonomous microtubule tip tracking, regulation of microtubule dynamics, and recruitment of numerous partners to microtubule ends. Here we report the detailed structural and biochemical analysis of mammalian EBs. Small-angle X-ray scattering, electron microscopy, and chemical cross-linking in combination with mass spectrometry indicate that EBs are elongated molecules with two interacting CH domains, an arrangement reminiscent of that seen in other microtubule- and actin-binding proteins. Removal of the negatively charged C-terminal tail did not affect the overall conformation of EBs; h

SUBMITTER: Buey RM 

PROVIDER: S-EPMC3154886 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature