Professor Folma Buss

I aim to understand how myosin motor proteins - such as myosin VI and myosin 1C - function in intracellular transport processes, cell signalling and membrane dynamics, and how defects in these molecular machines are linked to human diseases.

Myosin VI is a unique retrograde motor that moves along actin filaments and functions in membrane trafficking pathways associated with secretion, endocytosis and autophagy. These diverse roles of myosin VI are mediated by its interaction with a wide range of distinct adaptor proteins that connect it to different cargoes. We are using a variety of cellular, molecular and structural approaches to determine how cargo attaches to and regulates the activity and motor properties of this myosin.

Mutations, overexpression, or the absence of myosin VI have been linked to diverse pathological processes such as cancer, cardiomyopathy and deafness. Currently our main objective is to understand the role of this myosin and its cargo adaptor molecules in autophagy, a critical lysosomal degradation pathway. We have recently established that myosin VI directly interacts with autophagy receptors such as NDP52, optineurin and T6BP and loss of myosin VI activity impairs autophagy.

In another project we focus on myosin 1c and have demonstrated that it associates with cholesterol-enriched lipid rafts and facilitates their recycling from intracellular compartments to the cell surface. Absence of functional Myo1c protein causes the accumulation of cholesterol-enriched membranes in the perinuclear recycling compartment and leads to a defect in autophagosome/lysosome fusion.