The tail domain of the Aspergillus fumigatus class V myosin MyoE orchestrates septal localization and hyphal growth.

ABSTRACT: Myosins are critical motor proteins that contribute to the secretory pathway, polarized growth, and cytokinesis. The globular tail domains of class V myosins have been shown to be important for cargo binding and actin cable organization. Additionally, phosphorylation plays a role in class V myosin cargo choice. Our previous studies on the class V myosin MyoE in the fungal pathogen Aspergillus fumigatus confirmed its requirement for normal morphology and virulence. However, the domains and molecular mechanisms governing the functions of MyoE remain unknown. Here, by analyzing tail mutants, we demonstrate that the tail is required for radial growth, conidiation, septation frequency and MyoE's location at the septum. Furthermore, MyoE is phosphorylated at multiple residues in vivo</

SUBMITTER: Renshaw H 

PROVIDER: S-EPMC5826042 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature