Deleting the yeast phospholipase d spo14 augments homotypic vacuole fusion

Ejub, Sabit; Starr, Matthew L.

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https://hdl.handle.net/2142/103385 Copy

Description

Title

Deleting the yeast phospholipase d spo14 augments homotypic vacuole fusion

Author(s)

• Ejub, Sabit
• Starr, Matthew L.

Contributor(s)

Fratti, Rutilio A.

Issue Date

2018-04-19

Keyword(s)

• Biochemistry
• spo14
• phospholipase
• membrane fusion
• vacuole fusion
• lipid modification

Abstract

Membrane fusion is a necessary process that allows eukaryotic cells to carry and deliver cargo between organelles. The mechanisms and machinery involved in membrane fusion are conserved throughout eukaryotes, so the yeast vacuole provides an ideal model system to study. Yeast vacuole fusion proceeds through a series of stages that include priming, tethering, docking, and fusion. Phosphatidic acid (PA) is a glycerophospholipid present throughout eukaryotic organelle membranes. The conversion of PA to diacyglerol (DAG) has been shown to play an important role in the activity and recruitment of vacuole fusion protein factors during the priming and tethering stages. Increased PA levels at the vacuole have been shown to significantly inhibit each of these stages. In yeast, phospholipase D (Spo14) catalyzes the hydrolysis of phosphatidylcholine into choline and PA making it a protein of interest in our system. Spo14p activity has been shown to play a vital role in numerous cellular pathways, including signal transduction, membrane trafficking, and regulation of mitosis. Here we aim to identify a role for Spo14 activity in the regulation of yeast vacuolar membrane fusion. To date, we have demonstrated that deleting SPO14 causes a marked increase in vacuole fusion that may be attributed to a decrease in phosphatidic acid levels at the yeast vacuole.

Type of Resource

image

Language

en

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http://hdl.handle.net/2142/103385

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