Sharon A. Tooze - Selected Publications#
https://scholar.google.com/citations?hl=en&user=Mdq0YxYAAAAJ
h-index 82
https://pubmed.ncbi.nlm.nih.gov/?term=tooze+SA&sort=date
10. Zhang W, Nishimura T, Gahlot D, Saito C, Davis C, Jefferies HBJ, Schreiber A, Thukral L, Tooze, S. A. (2023) Autophagosome membrane expansion is mediated by the N-terminus and cis-membrane association of human ATG8s. Elife. Jun 8;12:e89185. doi: 10.7554/eLife.89185.PMID: 37288820.
We demonstrate an unanticipated role for the N-terminal region of ATG8s in membrane expansion. Our work was highlighted by an unsolicited editorial by the editor in the Journal Autophagy in October 2023. This supports the importance of our work to the field.
9. van Vliet, A. R., Chiduza, G.C., Maslen, S.L., Pye, V. E., Joshi, D., De Tito, S., Jefferies, H.B.J., Christodoulou, E., Roustan, C., Punch, E., Hervás, J., O’Reilly, N., Skehel, J. M., Cherepanov, P., Tooze, S.A. (2022) ATG9A and ATG2A form a heteromeric complex essential for autophagosome formation. Molecular Cell, Nov 17; 4324-4339.e8. doi: 10.1016/j.molcel.2022.10.017.
Cited 32 times. Using HDX-MS and cryo-EM we identified the docking site and functional importance of the interaction between ATG9A and ATG2A in autophagy.
8. Mercer TJ, Ohashi Y, Boeing S, Jefferies HBJ, De Tito S, Flynn H, Tremel S, Zhang W, Wirth M, Frith D, Snijders AP, Williams RL,Tooze, S.A. (2021) Phosphoproteomic identification of ULK substrates reveals VPS15-dependent ULK/VPS34 interplay in the regulation of autophagy. EMBO J. 2021 Jul 15;40(14):e105985. doi: 10.15252/embj.2020105985.
Cited 31 times. Using silac based MS and genetic codon expansion approaches we identified a novel ULK1 phosphorylation site in VPS15. This contributes to our knowledge of the role of ULK1 kinase.
7. Wirth, M., Zhang, W. Razi, M. Nyoni, L. Joshi, D., O’Reilly, N., Johansen, T., Tooze, S.A. (2019) Molecular determinants regulating selective binding of autophagy adapters and receptors to ATG8 proteins. Nat Comms. 10(1):2055. Doi:10.1038/s41467-019-10059-6.
Cited 115 times. Here using structure-function approaches we define how LIR motif binding to the LIR-docking site is family (LC3 versus GABARAP) specific and regulated by phosphorylation.
6. Judith, D., Jefferies, H.B.J., Boeing, S., Frith, D., Snijders, A.P., Tooze, S.A. (2019) ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIβ. J Cell Biol. 218(5):1634-1652. doi: 10.1083/jcb.201901115.
Cited 143 times. Purification of ATG9A vesicles identified a route for transfer of a lipid kinase (PI4K3β) in the production of PI4P, and recruitment of effectors, on growing autophagosomes.
5. Martinez-Martin, N., Maldonado, P., Gasparrini, F., Frederico, B., Aggarwal, S., Gaya, M., Tsui, C., Burbage, M., Keppler, S.J., Montaner, B., Jefferies, H.B., Nair, U., Zhao, Y.G., Domart, M.C., Collinson, L., Bruckbauer, A., Tooze, S.A., Batista, F.D. (2017) A switch from canonical to noncanonical autophagy shapes B cell responses. Science, 355:641-647. DOI: 10.1126/science.aal3908.
Cited 97 times. We discovered that a PI3P-effector WIPI2, characterized in my lab, was required for B cells to undergo activation.
4. Joachim, J., Jefferies, H.B.J, Razi, M., Frith, D., Snijders, A.P., Chakravarty, P., Tooze, S.A. (2015) Activation of ULK Kinase and Autophagy by GABARAP Trafficking from the Centrosome Is Regulated by WAC and GM130. Molecular Cell, 60:899-913. doi: 10.1016/j.molcel.2015.11.018.
Cited 137 times. We here discovered that control of autophagy at later expansion stages is regulated by a pool of GABARAP which is a substrate for ULK1, is resident at centrioles.
3. Dooley, H.C., Razi, M., Polson, H.E.J., Stephen E. Girardin, S.E., Michael I. Wilson, M.I., Tooze, S.A. (2014) WIPI2 Links LC3-Conjugation with PI3P, Autophagosome Formation and Pathogen Clearance by Recruiting Atg12–5-16L1. Molecular Cell, 55:238-52. doi: 10.1016/j.molcel.2014.05.021.
Cited 770 times. Elucidation of critical role that WIPI2 has in the activity of E3 ligase, ATG12-5-16L1. Identification of the binding site on WIPI2 for ATG16L1 has led to a major advance in understanding the role of PI3P and progression of autophagy.
2. Chan, E.Y.W., Longatti, A., McKnight, N.C., Tooze, S.A. (2009) Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domain using an Atg13-independent mechanism. Molecular and Cellular Biology, 29:157-171.
Cited 510 times. Following up on our identification of ULK1 as the canonical autophagy-initiating kinase we here discover a member of the ULK1 complex, ATG13.
1. Young, A., Chan, E.Y.W., Hu, X. W., Köchl, R., Cranshaw, S.G., High, S., Haley, D., Lippincott-Schwartz, J., Tooze, S.A. (2006) Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. Journal of Cell Science, 119:3888-3900.
Cited 944 times. The first identification and characterization of mammalian ATG9A, a key ATG protein, and the only multi-spanning membrane protein. We show that ATG9A trafficking is regulated by starvation through ULK1 activity.
