Abstract
Mammalian Diaphanous (Dia)-related formins initiate the assembly of filamentous actin downstream of Rho GTPases to regulate cellular processes such as cytokinesis, cell polarity, cell motility and adhesion. In this work, we show that Neurochondrin (NC) is a novel Dia1 interacting protein. NC specifically binds to the formin homology 3 (FH3), but not to the FH1 or FH2 domain of Dia1. Both proteins show a partial co-localization in dissociated primary rat hippocampal neurons. Ectopic expression of both proteins induced neurite outgrowth in Neuro2A cells. Using a series of deletion mutants of NC we could show that the first 100 amino acids were responsible for its effect on neurite outgrowth, whereas the C-terminal part of NC had no neurite outgrowth promoting activity. Moreover, co-expression of the C terminus of NC with Dia1ΔDAD resulted in a dramatic reduction of Dia1-induced neurite outgrowth. On the basis of actin fractionation assays, SRF-activity assays as well as microtubule stabilization assays, we could demonstrate that the C terminus of NC does not influence the actin polymerizing activity of Dia1, indicating a more specific function of NC in the modulation of Dia1 activity.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
