Professor Pete Cullen

Research summary

The endosomal network comprises a series of interconnected membrane bound compartments that in regulating the sorting and signaling of proteinaceous cargoes including receptors, transporters and adhesion molecules, orchestrates and fine-tunes numerous cellular processes. A major challenge is to achieve a thorough molecular description of how this network operates, and in so doing, how defects contribute to the pathoetiology of human disease.

To date our understanding of endosomal sorting has been restricted by a tendency to focus on individual ‘model’ cargoes, and the ‘isolated’ characterization of protein complexes that define individual sorting events. To achieve a thorough understanding we must break ...

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Links

• Wellcome Trust Senior Investigator Award
•   Biochemical Society Webcast

Selected publications

• McGough, IJ, Steinberg, F, Jia, D, Barbuti, PA, McMillan, KJ, Heesom, KJ, Whone, AL, Caldwell, MA, Billadeau, DD, Rosen, MK & Cullen, PJ, 2014, ‘Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation’. Current Biology, vol 24., pp. 1670-1676
• Gallon, MJ, Clairfeuille, T, Steinberg, F, Mas, C, Ghai, R, Sessions, RB, Teasdale, RD, Collins, BM & Cullen, PJ, 2014, ‘A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer.’. Proceedings of the National Academy of Sciences of the United States of America.

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Recent publications

• Simonetti, B & Cullen, PJ, 2019, ‘Actin-dependent endosomal receptor recycling’. Current Opinion in Cell Biology, vol 56., pp. 22-33
• Cullen, P, 2019, ‘Editorial overview: Membrane trafficking’. Current Opinion in Cell Biology, vol 59.

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View complete publications list in the University of Bristol publications system