- Ph.D., Brown University, 1989
- B.A., Wellesley College, 1982
Our goal is to understand the dynamic structural properties of dynamins and correlate them with their diverse cellular functions.
- Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.
- Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, Bernstein HD.
- Cell (2022 Mar 31) 185:1143-1156.e13. Abstract/Full Text
- Dynamin regulates the dynamics and mechanical strength of the actin cytoskeleton as a multifilament actin-bundling protein.
- Zhang R, Lee DM, Jimah JR, Gerassimov N, Yang C, Kim S, Luvsanjav D, Winkelman J, Mettlen M, Abrams ME, Kalia R, Keene P, Pandey P, Ravaux B, Kim JH, Ditlev JA, Zhang G, Rosen MK, Frost A, Alto NM, Gardel M, Schmid SL, Svitkina TM, Hinshaw JE, Chen EH.
- Nat Cell Biol (2020 Jun) 22:674-688. Abstract/Full Text
Research in Plain Language
Animal cells are protected from their surrounding environment by a lipid membrane. However, the membrane must allow external materials, such as nutrients and chemical messengers, to get into the cell. One way this is achieved is through a process called endocytosis, where a small part of the cell membrane folds inward into a pit that pinches off, forming a sack that is free to move through the cell. The protein dynamin is crucial for this process. Our studies and others have shown that dynamin wraps around and constricts the necks of the membrane pits, which helps seal the free-moving sacks.