Charles K. Barlowe, PhD
Chair and Professor of Biochemistry & Cell Biology
James C. Chilcott 1920 Professor
Biochemistry & Cell Biology
College of William & Mary, B.S. 1983
University of Texas at Austin, Ph.D. 1990
After postdoctoral work at University of California-Berkeley, Dr. Barlowe joined the Department of Biochemistry and Cell Biology at Geisel School of Medicine in 1994
Molecular and Cellular Biology Graduate Programs
Geisel School of Medicine
Department of Biochemistry and Cell Biology
Hanover NH 03755
Office: Remsen 414
Our current focus is on molecular mechanisms of protein and lipid trafficking between the endoplasmic reticulum (ER) and the Golgi complex in. Several of the genes involved in this process have been identified and their function may be assessed in cell-free assays that reproduce transport. Through a combined genetic and biochemical approach, the mechanisms underlying secretory cargo selection and vesicle budding from the ER as well as vesicle targeting and fusion with the Golgi complex are under study. This intracellular transport step is essential for cellular function and our studies are basic for understanding numerous health related issues including cholesterol regulation, cystic fibrosis and diabetes.
Conserved juxtamembrane domains in the yeast golgin Coy1 drive assembly of a megadalton-sized complex and mediate binding to tethering and SNARE proteins.
Lysophospholipids Facilitate COPII Vesicle Formation.
The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.
Cargo Capture and Bulk Flow in the Early Secretory Pathway.
Overexpression of Sly41 suppresses COPII vesicle-tethering deficiencies by elevating intracellular calcium levels.
Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins.
Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion.
Membrane trafficking: ER export encounters dualism.
The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins.
ER-Golgi transport: authors' response.