An asymmetric pattern of PAR proteins

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We recently showed that PAR proteins are highly dynamic, reversibly switching between a rapidly diffusing cytoplasmic state, and a more slowly diffusing membrane-associated state (Goehring et alJCB 2011).

This dynamic behaviour has important implications for how these molecules can be segregated into opposing halves of the cell membrane. What features of these proteins are responsible for such dynamic properties? How do proteins associate with the membrane? How is this association regulated in time and space?

We aim to tackle these questions using a combination of biophysical measurement, genetic and chemical manipulations, and biochemistry.