Graduate Studies Faculty

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Fred L. Robinson, Ph.D.

Assistant Professor
Assistant Investigator
Admin Unit: Jungers Center
Phone: 503-494-8783
Office: BRB 409
Mail Code: L623
Biochemistry & Molecular Biology
Neuroscience Graduate Program
Program in Molecular & Cellular Biosciences
Research Interests:
phosphoinositide phosphatases, myotubularin, cellular signaling, myelin homeostasis, membrane trafficking and dynamics, cellular and molecular neuroscience, neuropathy, axonal degeneration, Charcot-Marie-Tooth disease, Neurobiology of Disease » Click here for more about Dr. Robinson's research » PubMed Listing
Preceptor Rotations
Dr. Robinson has not indicated availability for preceptor rotations at this time.
Faculty Mentorship
Dr. Robinson has not indicated availability as a mentor at this time.



After completeing undergraduate work in Biology and Genetics at Oregon State University, Robinson earned a master’s degree in Biological Sciences from the University of Nebraska-Lincoln. In 2002, he received his Ph.D. in Biochemistry from The University of Texas Southwestern Medical Center at Dallas and did postdoctoral research at the University of California, San Diego, where he received an NIH-NINDS Pathway to Independence Award in 2007. Robinson joined the Jungers Center as an Assistant Scientist and Assistant Professor of Neurology in August 2009. He holds a joint appointment in the Vollum Institute.


Summary of Current Research

The overall goal of our research is to determine how disturbances in phosphoinositide signaling lead to cellular dysfunction and human disease. Mutations in phosphoinositide (PI) phosphatases cause a number of human neurological diseases, including conditions affecting the central and peripheral nervous systems. For example, mutations in several members of the myotubularin family of PI 3-phosphatases lead to Charcot-Marie-Tooth (CMT) peripheral neuropathy, one of most common inherited neurological disorders, which affects about 1 in 2500 worldwide. CMT causes progressive degeneration of muscles in the extremities as well as loss of sensory function.

We are investigating how mutations in members of the myotubularin family of PI 3-phosphatases disrupt PI signaling, and thus cause alterations in endosomal-lysosomal membrane trafficking that lead to peripheral neuropathy. In addition, we are investigating the functions of phosphoinositide signaling in the central nervous system. Myotubularin PI 3-phosphatases specifically dephosphorylate PtdIns3P and PtdIns(3,5)P2, two PIs that regulate membrane traffic within the endosomal-lysosomal pathway. Mutations in the genes for either myotubularin related protein 2 (MTMR2) or MTMR13 cause type 4B CMT (CMT4B), a severe form of the disease characterized by abnormal myelin sheaths and secondary axonal degeneration.

Our work will provide novel insights into how dysregulation of PtdIns3P and PtdIns(3,5)P2 leads to cellular dysfunction and neurological disease. This work also has the potential to lead to therapies for peripheral neuropathies and other diseases of myelin. Understanding how the Schwann cell endosomal-lysosomal pathway is altered by the dysregulation of 3-phosphoinositides is critical to the design of an appropriate pharmacological intervention in CMT4B. In addition, the identification of downstream targets of Mtmr2-Mtmr13 may allow us to define novel signaling pathways, both in the peripheral and central nervous system.


Selected Publications

Ng, A.A., Logan, A.M., Schmidt, E.J. and Robinson F.L. (2013). The CMT4B disease-causing phosphatases Mtmr2 and Mtmr13 localize to the Schwann cell cytoplasm and endomembrane compartments, where they depend upon each other to achieve wild-type levels of protein expression. Hum. Mol. Genet. 22:1493-1506.

Jean, S., Cox, S., Schmidt, E.J., Robinson, F.L. and Kiger, A. (2012). Sbf/MTMR13 coordinates PI(3)P and Rab21 regulation in endocytic control of cellular remodeling. Mol. Biol. Cell. 23:2723-2740.

Robinson, F.L., Niesman, I.R., Beiswenger, K.K. and Dixon, J.E. (2008). Loss of the inactive myotubularin-related phosphatase Mtmr13 leads to a Charcot-Marie-Tooth 4B2-like peripheral neuropathy in mice. Proc. Natl. Acad. Sci. USA. 105:4916-4921.

Robinson, F.L. and Dixon, J.E. (2006). Myotubularin phosphatases: Policing 3-phosphoinositides. Trends Cell Biol. 16:403-412.

Robinson, F.L. and Dixon, J.E. (2005). The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease. J. Biol. Chem. 280:31699-31707.