Related Experiment Video
Updated: Oct 3, 2025

13:08
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
11.0K
Glycan processing in the Golgi as optimal information coding that constrains cisternal number and enzyme specificity
Alkesh Yadav1, Quentin Vagne2, Pierre Sens2
1Raman Research Institute, Bangalore, India.
Elife
|February 17, 2022
Summary
Synthesizing complex cell surface glycans requires multiple Golgi cisternae and specific enzymes. Optimal enzyme specificity balances complexity and fidelity for accurate glycan code realization.
Area of Science:
- Biochemistry
- Cell Biology
- Systems Biology
Background:
- Proteins modified in the Golgi apparatus form cell identity markers on the plasma membrane.
- These modifications involve sequential enzymatic reactions, creating a complex 'glycan code'.
- The accuracy of this glycan code is crucial for cellular function and communication.
Purpose of the Study:
- To quantitatively analyze the trade-offs in Golgi apparatus function for glycan synthesis.
- To determine the relationship between Golgi structure, enzyme properties, and glycan synthesis fidelity.
- To understand the constraints on Golgi cisternal number and enzyme specificity based on glycan complexity.
Main Methods:
- Development of a simplified chemical synthesis model for Golgi glycosylation.
- Quantitative analysis of parameters including cisternal number, enzyme number, and enzyme specificity.
- Investigation of the 'fidelity landscape' to assess robustness and identify optimal configurations.
Main Results:
- Complex glycan distributions necessitate multiple Golgi cisternae and precise enzyme localization.
- For a fixed number of enzymes and cisternae, an optimal enzyme specificity (or promiscuity) exists for high-fidelity synthesis.
- The fidelity landscape reveals robust and sensitive directions in the parameter space.
Conclusions:
- The complexity of target glycan structures imposes functional constraints on Golgi apparatus design.
- Golgi cisternal number and enzyme specificity are critical factors for achieving accurate glycan coding.
- This model provides insights into the evolutionary and functional optimization of cellular glycosylation machinery.
Related Concept Videos
Golgi Matrix Proteins
2.1K
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.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.1K
Oligosaccharide Assembly
3.0K
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...
Multiple sugar molecules that may or may...
3.0K
Golgi Apparatus
16.9K
Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
16.9K
Transport Across the Golgi
4.6K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
4.6K
Protein Glycosylation
7.5K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
7.5K
Protein Folding Quality Check in the RER
4.0K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
4.0K

