The Golgi complex has an unusual structure, particularly in vertebrates, where stacks of cisternal membranes are clustered into a ribbon structure near the nucleus. One of Dr. Machamer's research goals is to understand the role of this structure in Golgi function. Toward this goal, she and her team are studying the targeting and function of resident Golgi proteins. They are interested in the contribution of the lipid bilayer to targeting of transmembrane Golgi proteins, and in the function of a group of peripheral Golgi membrane proteins called golgins.
Dr. Machamer's other research interest is the assembly mechanism of coronaviruses, enveloped viruses that bud into Golgi compartments. The recent emergence of severe acute respiratory syndrome (SARS), which is caused by a novel coronavirus, has sparked much interest in this group of viruses. Her lab is addressing how coronaviruses target their envelope proteins to Golgi membranes, and how they interact with each other at the virus assembly site. They are also exploring how coronaviruses are exocytosed after they bud into the Golgi lumen. Their long-term goal is to understand the advantages of intracellular assembly for coronaviruses; this should lead to novel strategies for antiviral therapeutics.
Lab Website: Carolyn Machamer, Ph.D.
Gilbert CE, Zuckerman DM, Currier PL, and Machamer CE. 2014. "Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking." Int. J. Mol. Sci.15:2929-45.
Machamer CE. "Accommodation of large cargo within Golgi cisternae." Histochem Cell Biol. 2013 Sep;140(3):261-9. doi: 10.1007/s00418-013-1120-y. Epub 2013 Jul 3.
Chandran S, and Machamer CE. 2012. "Inactivation of ceramide transfer protein during proapoptotic stress by Golgi disassembly and caspase cleavage." Biochem. J., 442:391-402.
Ruch TR, and Machamer CE. 2012. "The coronavirus E protein: assembly and beyond." Viruses 4:363-382.
Ruch TR, and Machamer CE. 2012. "A single polar residue and distinct membrane topologies impact the function of the infectious bronchitis coronavirus E protein." PLoS Pathogens 8(5):e1002674.