Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM052549-02
Application #
2191620
Study Section
Molecular Cytology Study Section (CTY)
Project Start
1995-05-01
Project End
1999-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Dartmouth College
Department
Biochemistry
Type
Schools of Medicine
DUNS #
041027822
City
Hanover
State
NH
Country
United States
Zip Code
03755
Anderson, Nadine S; Mukherjee, Indrani; Bentivoglio, Christine M et al. (2017) The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs. Mol Biol Cell :
Margulis, Neil G; Wilson, Joshua D; Bentivoglio, Christine M et al. (2016) Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins. Traffic 17:191-210
Flanagan, John J; Mukherjee, Indrani; Barlowe, Charles (2015) Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion. J Biol Chem 290:10657-66
Shibuya, Aya; Margulis, Neil; Christiano, Romain et al. (2015) The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins. J Cell Biol 208:197-209
Brandizzi, Federica; Barlowe, Charles (2013) Organization of the ER-Golgi interface for membrane traffic control. Nat Rev Mol Cell Biol 14:382-92
Wilson, Joshua D; Thompson, Sarah L; Barlowe, Charles (2011) Yet1p-Yet3p interacts with Scs2p-Opi1p to regulate ER localization of the Opi1p repressor. Mol Biol Cell 22:1430-9
Lorente-Rodríguez, Andrés; Barlowe, Charles (2011) Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments. Mol Biol Cell 22:216-29
Barlowe, Charles (2010) ER sheets get roughed up. Cell 143:665-6
Miller, Elizabeth A; Barlowe, Charles (2010) Regulation of coat assembly--sorting things out at the ER. Curr Opin Cell Biol 22:447-53
Wilson, Joshua D; Barlowe, Charles (2010) Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy. J Biol Chem 285:18252-61

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