Ryan Baldridge, Ph.D.

Assistant Professor, Biological Chemistry

Office: 3220E MSRB III
Lab: 3200, 3240 MSRB III
1150 W. Medical Center Drive
Ann Arbor, MI 48109-5606


Office: (734) 763-4008; Lab: (734) 936-3440

Areas of Interest

Membrane biology, protein quality control, ubiquitination 

We are interested in the basic mechanisms of membrane-bound protein-quality control systems. We plan to determine how membrane-bound systems select substrates to identify cellular pathways regulated by these systems (including ERAD). These systems are important in pathologies related to cell stress, protein misfolding, and protein misregulation. Some of the human conditions linked to these problems include Parkinson’s disease, Alzheimer’s disease, and various cancers. One of our long-term goals is to define mammalian pathways regulated by membrane-bound quality control systems to understand how changing conditions target substrate proteins to these systems. Eventually, we would like to develop a screening platform to identify activators and inhibitors of these various quality control systems. Understanding these systems using novel assays should allow screening for, and refinement of, therapeutics with value in a wide range of pathologies.

Honors & Awards

Dale F. Frey Award For Breakthrough Scientists, Damon Runyon Cancer Research Foundation, 2018–2019
Biological Sciences Scholar, University of Michigan Medical School, 2017
Damon Runyon Postdoctoral Fellowship Award, Damon Runyon Cancer Research Foundation, 2014–2017

Published Articles or Reviews

Recent Publications

The ERAD system is restricted by elevated ceramides.
Hwang J, Peterson BG, Knupp J, Baldridge RD.
Sci Adv. 2023; 9: eadd8579.

Cycles of autoubiquitination and deubiquitination regulate the ERAD ubiquitin ligase Hrd1.
Peterson BG, Glaser ML, Rapoport TA, Baldridge RD.
Elife. 2019; 8: e50903.

Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.
Baldridge RD, Rapoport TA.
Cell. 2016; 166: 394–407.

Role of flippases, scramblases and transfer proteins in phosphatidylserine subcellular distribution.
Hankins HM, Baldridge RD, Xu P, Graham TR.
Traffic. 2015; 16: 35–47.

Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport.
Xu P, Baldridge RD, Chi RJ, Burd CG, Graham TR.
J Cell Biol. 2013; 202: 875–86.

Type IV P-type ATPases distinguish mono- versus diacyl phosphatidylserine using a cytofacial exit gate in the membrane domain.
Baldridge RD, Xu P, Graham TR.
J Biol Chem. 2013; 288: 19516–27.

Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases.
Baldridge RD, Graham TR.
Proc Natl Acad Sci USA. 2013; 110: E358–67.

For a list of publications from Pubmed, click HERE

Web Sites