A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes. Academic Article

abstract

• SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate that SEC14p specifically functions to maintain a reduced phosphatidylcholine content in Golgi membranes and indicate that overproduction of SEC14p markedly reduces the apparent rate of phosphatidylcholine biosynthesis via the CDP-choline pathway in vivo. We suggest that SEC14p serves as a sensor of Golgi membrane phospholipid composition through which the activity of the CDP-choline pathway in Golgi membranes is regulated such that a phosphatidylcholine content that is compatible with the essential secretory function of these membranes is maintained.

authors

• Bankaitis, Vytas

published proceedings

• J Cell Biol

altmetric score

• 3

author list (cited authors)

• McGee, T. P., Skinner, H. B., Whitters, E. A., Henry, S. A., & Bankaitis, V. A.

citation count

• 155

complete list of authors

• McGee, TP||Skinner, HB||Whitters, EA||Henry, SA||Bankaitis, VA

publication date

• February 1994

publisher

• Rockefeller University Press  Publisher

published in

• The Journal of Cell Biology  Journal

keywords

• Carrier Proteins
• Cytidine Diphosphate Choline
• Golgi Apparatus
• Intracellular Membranes
• Membrane Proteins
• Models, Biological
• Mutation
• Phosphatidylcholines
• Phosphatidylinositols
• Phospholipid Transfer Proteins
• Phospholipids
• Saccharomyces Cerevisiae Proteins
• Yeasts

PubMed Central ID

• 8294512

Digital Object Identifier (DOI)

• 10.1083/jcb.124.3.273

start page

• 273

end page

• 287

volume

• 124

issue

• 3

URL

• http://dx.doi.org/10.1083/jcb.124.3.273