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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Coat Assembly and GTPases01:33

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Golgi Matrix Proteins01:12

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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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Golgi Apparatus01:49

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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
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Updated: Jun 21, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Published on: March 14, 2021

Lysophosphatidic acid acyltransferase 3 regulates Golgi complex structure and function.

John A Schmidt1, William J Brown

  • 1Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.

The Journal of Cell Biology
|July 29, 2009
PubMed
Summary

Lysophosphatidic acid-specific acyltransferase 3 (LPAAT3) regulates Golgi structure and protein trafficking by remodeling membrane phospholipids. This study reveals LPAAT3

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Last Updated: Jun 21, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

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Published on: March 14, 2021

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13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)
13:02

Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)

Published on: March 18, 2011

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Golgi complex organization is crucial for cellular function.
  • Phospholipid remodeling enzymes are implicated in Golgi complex organization.

Purpose of the Study:

  • To identify and characterize novel enzymes involved in Golgi complex functional organization.
  • To elucidate the role of lysophosphatidic acid-specific acyltransferase 3 (LPAAT3) in regulating Golgi membrane dynamics and protein trafficking.

Main Methods:

  • Identification of integral membrane proteins.
  • In vivo and in vitro assays for Golgi membrane tubule formation.
  • Analysis of protein trafficking using overexpression and siRNA knockdown of LPAAT3.
  • Assessment of Golgi morphology through microscopy.

Main Results:

  • LPAAT3 was identified as a lysophosphatidic acid-specific acyltransferase regulating Golgi membrane phospholipids.
  • Overexpression of LPAAT3 inhibited Golgi membrane tubule formation.
  • LPAAT3 modulated both anterograde and retrograde protein trafficking.
  • LPAAT3 knockdown resulted in Golgi fragmentation, indicating its role in maintaining Golgi structure.

Conclusions:

  • LPAAT3 directly regulates Golgi membrane tubule formation, protein trafficking, and overall organelle structure.
  • This study establishes a direct link between phospholipid remodeling and Golgi complex organization and function.