Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Abstract Text:

Xinmin Li,Marcos P Rivas,Min Fang,Jennifer Marchena,Bharat Mehrotra,Anu Chaudhary,Li Feng,Glenn D Prestwich,Vytas A Bankaitis,

Oxysterol binding proteins (OSBPs) comprise a large conserved family of proteins in eukaryotes. Their ubiquity notwithstanding, the functional activities of these proteins remain unknown. Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p. We now demonstrate that Kes1p is a peripheral membrane protein of the yeast Golgi complex, that localization to the Golgi complex is required for Kes1p function in vivo, and that targeting of Kes1p to the Golgi complex requires binding to a phosphoinositide pool generated via the action of the Pik1p, but not the Stt4p, PtdIns 4-kinase. Localization of Kes1p to yeast Golgi region also requires function of a conserved motif found in all members of the OSBP family. Finally, we present evidence to suggest that Kes1p may regulate adenosine diphosphate-ribosylation factor (ARF) function in yeast, and that it may be through altered regulation of ARF that Kes1p interfaces with Sec14p in controlling Golgi region secretory function.

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Publishing Authors By Initials

X Li,MP Rivas,M Fang,J Marchena,B Mehrotra,A Chaudhary,L Feng,GD Prestwich,VA Bankaitis,

For similar fungi: yeasts research abstracts see: fungi: yeasts research

PUBMED ID PMID:

MEDLINE DATE:

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of cell biology

VOLUME: 157

Page Numbers: 63-77

Journal Abbreviation: J. Cell Biol.

ISSN: 0021-9525

DAY: 26

MONTH: 03

YEAR: 2002

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 375356

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Keywords Mesh Terms:

KEYWORDS: Yeasts

MESH TERMS: genetics

Chemical & Substance for Abstract: Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Information

Substance Name: ADP-Ribosylation Factors

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.

AFFILIATION: Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Country: United States

AGENCY: United States NINDS

GRANT: NS29632

ACRONYM: NS

MEDLINETA: J Cell Biol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex Related Publications

• Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.
• Conformational dynamics of the major yeast phosphatidylinositol transfer protein sec14p: insight into the mechanisms of phospholipid exchange and diseases of sec14p-like protein deficiencies.
• Evidence for an intrinsic toxicity of phosphatidylcholine to Sec14p-dependent protein transport from the yeast Golgi complex.
• Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily.
• Lipid metabolism and regulation of membrane trafficking.
• Local polarity and hydrogen bonding inside the Sec14p phospholipid-binding cavity: high-field multi-frequency electron paramagnetic resonance studies.
• The chemistry of phospholipid binding by the Saccharomyces cerevisiae phosphatidylinositol transfer protein Sec14p as determined by EPR spectroscopy.
• The pathologies associated with functional titration of phosphatidylinositol transfer protein alpha activity in mice.
• The sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals.