Our research addresses the mechanism and consequences of protein S-palmitoylation, a reversible posttranslational modification of proteins that regulates membrane association, protein trafficking, and protein stability. Discovered in 2002, the DHHC (Asp-His-His-Cys) protein S-acyltransferases are responsible for palmitoylation of proteins on the cytoplasmic leaflet of cell membranes. Our recent studies have revealed the catalytic mechanism of DHHC proteins and current work is focused on understanding how DHHC proteins are regulated by posttranslational modifications and oligomerization. We also have a longstanding interest in lipidation of cell signaling proteins and we have recently identified an alternative CaaX processing pathway for Cdc42 and Ral GTPases. Work is ongoing to elucidate how the alternatively processed isoforms bypass conventional CaaX processing and how they are functionally distinct from the conventionally processed isoforms. A third project is to determine the molecular mechanisms that underlie a syndromic form of X-linked intellectual disability caused by mutations in the ZDHHC9 gene. The objectives are to identify the substrates of DHHC9 by comparing the palmitoylomes of wild type and ZDHHC9 knockout mice and determine if ZDHHC9 knockout mice display altered behaviors in assays of cognitive, sensory, and motor functions.

• PhD, Molecular and Cell Biology, University of Texas at Dallas, 1987
• Medical Technology Internship Program, St. Joseph Mercy Hospital, 1977
• BSc, Medical Technology, Michigan State University, 1976

• 2009-Present, Professor and Chair, Department of Molecular Medicine, Cornell University
• 2006-2009, Professor, Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis
• 1999-2006, Associate Professor, Department of Cell Biology and Physiology, Washington University School of Medicine
• 1993-1999, Assistant Professor, Department of Cell Biology and Physiology, Washington University School of Medicine
• 1991-1993, Instructor, Department of Pharmacology, University of Texas Southwestern Medical Center
• 1989-1991, Assistant Instructor, Department of Pharmacology, University of Texas Southwestern Medical Center
• 1987-1989, Research Fellow, Department of Pharmacology, University of Texas, Southwestern Medical Center

1. Gottlieb CD, Shang Z, and Linder ME (2015) The cysteine-rich domain of the DHHC3 palmitoyltransferase is palmitoylated and contains tightly bound zinc. J. Biol. Chem. 290:29259-69.
2. Yeste-Velasco M, Linder ME, and Lu, Y-J (2015) Protein S-Palmitoylation and cancer. BBA Cancer Reviews 1856:107-120.
3. Lai J and Linder ME (2013) Oligomerization of DHHC-S-Acyltransferases.  J. Biol. Chem. 288:22862-70.
4. Nishimura A and Linder ME (2013); A novel prenyl,palmitoyl CaaX modification of Cdc42 regulates RhoGDI binding and signaling activity.  Mol. Cell. Biol. 33:1417-29.

5. Jennings BC and Linder ME (2012) DHHC protein S-acyltransferases use a similar ping-pong kinetic mechanism but display different acyl-CoA specificities.  J. Biol. Chem. 287:7236-45.

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• 2009, Academic Women’s Network Mentor Award
• 2009, Fellow, American Association for the Advancement of Science
• 2001-2004, Established Investigator, American Heart Association
• 2001, Special Recognition – Outstanding Faculty Mentor Awards

• 2009, American Society for American Society for Pharmacology and Experimental Therapeutics
• 1993, American Society for Biochemistry and Molecular Biology
• 1993, American Society for Cell Biology