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BMS Seminar by Professor Andrew Carter, MRC Laboratory of Molecular Biology, University of Cambridge

Location: GLT3, Warwick Medical School

Abstract: Cell organization and internal movement depends on motor proteins. My lab studies cytoplasmic dynein and its cofactor dynactin. The 2.4MDa dynein/dynactin complex was, until recently, the least understood of all the cytoskeletal motors. Our interest focuses on how a single dynein carries almost all of the minus-end-directed microtubule transport in our cells. It is becoming clear that there is a large family of cargo adaptors that contain long coiled coils and can activate dynein’s long distance movement. We used cryo-electron microscopy (cryoEM) to show how these adaptors recruit dynein to the filament of actin-related protein (Arp1) in dynactin. We revealed how formation of this complex activates dynein. We also discovered that dynactin can recruit two dyneins side-by-side resulting in a faster moving complex. Our future goal is to understand how the core dynein/dynactin/adaptor complexes are recruited to the many cargos that depend on dynein for their transport.

BiograpProfessor Andrew Carterhy: Andrew became interested in structural biology as an undergraduate at the University of Oxford. Which led to start a PhD in 1999 with Venki Ramakrishnan at the MRC Laboratory of Molecular Biology in Cambridge. Working as part of the team that determined the X-ray crystal structure of the small (30S) ribosomal subunit. In addition I solved structures of the ribosome bound to antibiotics and the protein initiation factor IF1. He spent an extra year in Cambridge as a junior research fellow at Clare College, before moving in 2003 to Ron Vale's lab at the University of California where he started working on dynein. Together with Sam Reck Peterson I used S.cerevisiae to express a recombinant dynein motor for biophysical studies (2006). I collaborated with the group of Ian Gibbons to solve the structure of dynein's microtubule binding domain (2008) and together with Carol Cho produced the first crystal structure of the dynein motor domain (2010). In 2008 I returned to the MRC-LMB which I started in August 2010. My group pushed the yeast motor domain structure to high resolution and solved the structure of a human dynein motor domain (dynein-2) bound to the transition state analog ADP.vanadate, which revealed how ATP hydrolysis drives the conformational changes in dynein that generate movement. In 2015 we published used cryo electron microscopy to determine the structure of the dynactin complex and how it bound to dynein.

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