Essential role for diacylglycerol in protein transport from the yeast Golgi complex.

Abstract:

:Yeast phosphatidylinositol transfer protein (Sec14p) is required for the production of secretory vesicles from the Golgi. This requirement can be relieved by inactivation of the cytosine 5'-diphosphate (CDP)-choline pathway for phosphatidylcholine biosynthesis, indicating that Sec14p is an essential component of a regulatory pathway linking phospholipid metabolism with vesicle trafficking (the Sec14p pathway). Sac1p (refs 7 and 8) is an integral membrane protein related to inositol-5-phosphatases such as synaptojanin, a protein found in rat brain. Here we show that defects in Sac1p also relieve the requirement for Sec14p by altering phospholipid metabolism so as to expand the pool of diacylglycerol (DAG) in the Golgi. Moreover, although short-chain DAG improves secretory function in strains with a temperature-sensitive Sec14p, expression of diacylglycerol kinase from Escherichia coli further impairs it. The essential function of Sec14p may therefore be to maintain a sufficient pool of DAG in the Golgi to support the production of secretory vesicles.

journal_name

Nature

journal_title

Nature

authors

Kearns BG,McGee TP,Mayinger P,Gedvilaite A,Phillips SE,Kagiwada S,Bankaitis VA

doi

10.1038/387101a0

subject

Has Abstract

pub_date

1997-05-01 00:00:00

pages

101-5

issue

6628

eissn

0028-0836

issn

1476-4687

journal_volume

387

pub_type

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