Ellen J. Tisdale (aa4106)

University information

Title: Associate Professor
Unit: Pharmacology
Department: School of Medicine

Contact information

6360 Scott Hall
Detroit, 48202

Academic Senate

Phone: 7-1007
Department: Pharmacology
Thru Year: 2026
College/Division: Medicine
Faculty Affairs Committee Note: Member
Ellen J. Tisdale


Title: Associate Professor
Office Address:

Scott Hall Rm 6360  
540 E. Canfield
Detroit MI 48201

Office Phone:


Office Fax: 313-577-6739

The research of the Tisdale lab pertains to identifying and characterizing the molecular machinery and the regulatory mechanism(s) that control retrograde membrane transport from vesicular tubular clusters (VTCs) back to the endoplasmic reticulum (ER). VTCs are pleomorphic structures composed of clusters of vesicles and tubules located between the cis Golgi compartment and the ER (the early secretory pathway). These structures sort cargo to the anterograde pathway for transport to the Golgi complex from recycling proteins retrieved to the ER. This process is carefully regulated because defects in the trafficking machinery have profound pathological consequences.

The laboratory makes use of a combination of molecular biology, microscopy, biochemistry, and protein chemistry to identify putative components of the trafficking machinery that are ultimately introduced into a battery of in vivo transport assays, and in vitro binding, morphological, and transport reconstitution assays. Utilizing these assays, we have shown that the ras related small GTPase Rab2 plays a critical role at the VTC by promoting the formation of retrograde-directed vesicles. Rab2 is one of more than sixty members of the Rab family of proteins that participate in compartment specific transport events of both the endocytic and the exocytic pathways through recruitment and interaction with effectors molecules that promote vesicle formation, cytoskeletal interaction/motility and vesicle docking and fusion. Rab2 requires unique effector molecules for this activity including Src, atypical protein kinase C iota (aPKCi) and GAPDH. Our long term research goal is to understand the mechanism of protein sorting, targeting, and recycling from the VTC.



B.S., Ashland University, Ashland, OH
Biology/Comprehensive Science

M.S., Clemson University, Clemson, SC    
Advisor: Dr. Carolyn Brown

Ph.D., Case Western Reserve University, Cleveland, OH
Experimental Pathology/Cell Biology
Advisor: Dr. Alan Tartakoff


Case Western Reserve University, Cleveland, OH
Laboratory of Dr. John C. Schimenti
Post-Doctoral training in Molecular Biology

The Scripps Research Institute, La Jolla, CA
Laboratory of Dr. Bill Balch
Research Fellow training in Membrane Trafficking/Cell Biology

  • Tisdale, E. J. (2003) Rab2 Interacts Directly with Atypical Protein Kinase C i/l and Inhibits aPKCi/l-Dependent GAPDH Phosphorylation, J. Biol. Chem. 278:52524-52530.
  • Tisdale, E.J., Kelly, C., and Artalejo, C.R. (2004), GAPDH Interacts with Rab2 and Plays an Essential Role in ER to Golgi Transport Exclusive of its Glycolytic Activity,
    J. Biol. Chem.279:54046-54052.
  • Tisdale, E.J., and Artalejo, C.R. (2006) Src-Dependent aPKC i/l Tyrosine Phosphorylation is Required for aPKC i/l Association with Rab2 and Glyceraldehyde-3-phosphate Dehydrogenase on Pre-Golgi Intermediates, J. Biol. Chem., 281:8436-8442.
  • Tisdale, E.J., and Artalejo, C.R. (2007) A GAPDH Mutant Defective in Src-Dependent Tyrosine Phosphorylation Impedes Rab2-Mediated Events, Traffic, 8;733-741.
  • Ikonomov OC, Sbrissa D, Venkatareddy M, Tisdale E, Garg P, Shisheva A. (2015) Class III PI 3-kinase is the main source of PtdIns3P substrate and membrane recruitment signal for PIKfyve constitutive function in podocyte endomembrane homeostasis.Biochim Biophys Acta. 1853:1240-50.

Search PubMed for publications from the Tisdale Lab

Faculty Status: Cell Biology
Ellen J. Tisdale

Courses taught by Ellen J. Tisdale

Winter Term 2024 (current)

Winter Term 2023

Winter Term 2022

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