Diversity Committee Member
(PhD – Princeton Univ.)
structural biology, membrane trafficking, cancer biology, cryo-EM methods development. Our research aims to understand the molecular mechanisms of membrane trafficking.
We use the tools of cryo electron microscopy (cryo-EM) to study how protein complexes assemble on membranes to bud and fuse vesicles. Specialties: cryo-EM, X-ray crystallography, biochemistry, protein purification.
A hallmark of eukaryotic cell biology is a complex and dynamic organellar architecture. The process of forming and maintaining this architecture requires a regulated cycle of budding and fusion events and is broadly called membrane trafficking. The Baker lab is interested in understanding the machines that catalyze and regulate membrane trafficking events, with a particular focus on studying systems in their native, membrane-bound state.
A primary focus of the Baker lab is a membrane trafficking event called endocytosis, which allows cells to constantly modulate the composition of their plasma membrane. As cells communicate with their environment through their plasma membrane, precise control of its structure and composition underpins many processes including signaling, synaptic transmission, and host-pathogen interactions. There is emerging evidence that subversion of membrane traffic at the cell surface is a hallmark of many human diseases. In particular, misregulation of signaling proteins at the cell surface (TGF-beta receptor, etc.) may play a pivotal role in cancer development and progression. The Baker lab is interested in understanding the molecular underpinnings of disease, notably cancer, and is a member of the Lineberger Comprehensive Cancer Center (LCCC).
In the Baker lab, we use a variety of techniques to understand these systems in molecular detail, including high-resolution cryo-EM, X-ray crystallography, single-molecule TIRF, and biochemical reconstitution. We are also involved in cryo-EM methods development centered on novel methods for high-resolution structures of membrane-bound proteins, and novel grid supports to overcome resolution limitations of challenging samples. Additionally, we collaborate with several groups that use a variety of model systems, including Saccharomyces and C. elegans, and experimental approaches like unbiased genetic screens, fitness assays, and live cell microscopy, enabling us to study these systems in a highly interdisciplinary and collaborative manner.
The Baker lab is committed to providing a safe and inclusive training environment that celebrates the diverse backgrounds, viewpoints, and contributions of all lab members.
- Partlow EA, Cannon K, Hollopeter G, Baker RW. (2022). Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nature Structure & Molecular Biology. 29(4):1-19. PMID:35347313
- Partlow EA*, Baker RW*, Beacham GM, Chappie JS, Leschziner AE, Hollopeter G. (2019). A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex. 2019 Aug 29;8. PMCID: PMC6739873. *equal contribution.
- Baker RW, Jeffrey PD, Zick M, Phillips BP, Wickner WT, Hughson FM. (2015). A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science. 4;349(6252):1111-4. PMCID:
- Baker RW, Hughson FM. (2016). Chaperoning SNARE assembly and disassembly. Nature Reviews Molecular and Cell Biology. Aug;17(8):465-79. PMCID:
120 Mason Farm Rd
3049E GENETIC MEDICINE, Baker lab
Chapel Hill, NC 27599-7260
3046 GENETIC MEDICINE