Jenny E. Hinshaw, Ph.D.
- Section Chief: Structural Cell Biology Section, Laboratory of Cell & Molecular Biology
- Director: Cryo-Electron Microscopy (Cryo-EM) Core, NIDDK, Cores & Support Services
- Director: Cryo-Electron Microscopy (Cryo-EM) Core, Multi-Institute (MICEF), Cores & Support Services
- Director: NICE-NIH Intramural Cryo-EM Consortium
Professional Experience
- Ph.D., Brown University, 1989
- B.A., Wellesley College, 1982
Research Goal
Our goal is to understand the dynamic structural properties of dynamins and correlate them with their diverse cellular functions.
Select Publications
- OPA1 helical structures give perspective to mitochondrial dysfunction.
- Nyenhuis SB, Wu X, Strub MP, Yim YI, Stanton AE, Baena V, Syed ZA, Canagarajah B, Hammer JA, Hinshaw JE.
- Nature (2023 Aug) 620:1109-1116. Abstract/Full Text
- 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
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.
The energy producing organelle in cells are mitochondria. Mitochondria undergo constant reshaping to maintain and deliver energy throughout the cell. Mitochondrial reshaping is achieved by a balance of mitochondrial scission or fusion. Our lab solved the structure of the protein OPA1 involved in the fusion of the inner mitochondrial membrane and revealed the mechanism of how several of the OPA1 mutations may lead to Dominate Optic Atrophy, the leading cause of childhood blindness.