Frontiers in Molecular Life Sciences

By: John Copeland, University of Ottawa

Title: INF1 acts at the Golgi-Derived Microtubule Network to Regulate Golgi Morphology

Our laboratory studies the function of the formin homology family of cytoskeletal remodeling proteins. These proteins carry out both structural and signaling roles to govern cell morphology through their effects on actin and microtubule dynamics. Using cultured cells as a model, we study the cellular roles of formins by applying a powerful combination of molecular, cellular and microscopy-based assays. My current work focuses on the novel formin INF1.  INF1 is unique among formins in its ability to bind directly to the microtubule (MT) network through its C-terminal MT binding domain.  Through the action of the C-terminal MTBD and the N-terminal FH2 domain, INF1 is able to connect the two major cytoskeletal systems: actin filaments and the microtubule network. Our results suggest that this aspect of INF1 activity is essential for normal assembly of the Golgi apparatus. We are investigating the requirement for INF1 in Golgi assembly and its downstream effects on cell polarity.

Host: Roger Karlsson