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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.
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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.
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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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...
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Glycosylation in Axonal Guidance.

Sampada P Mutalik1, Stephanie L Gupton1

  • 1Department of Cell Biology and Physiology, University of North Carolina, Chapel Hill, NC 27514, USA.

International Journal of Molecular Sciences
|June 2, 2021
PubMed
Summary

Glycosylation, a protein modification, is crucial for guiding axons to their targets during neuronal development. This review explores how sugar chains on guidance molecules and receptors impact axon pathfinding and motility.

Keywords:
attractionaxonal guidancechemotaxischondroitin sulfateglycosaminoglycanglycosylationhaptotaxisheparan sulfate proteoglycanhyaluronanrepulsion

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Area of Science:

  • Neuroscience
  • Developmental Biology
  • Molecular Biology

Background:

  • Axon pathfinding during development is guided by molecular cues, but the diversity of responses is not fully understood.
  • Mechanisms like differential receptor expression and cue patterning diversify axon guidance pathways.
  • Posttranslational modifications, particularly glycosylation, represent an understudied area in regulating protein function for axon guidance.

Purpose of the Study:

  • To review the major classes of glycosylation and their roles in axonal pathfinding.
  • To discuss the functional implications of glycosylation on guidance cues and receptors in axonal outgrowth and navigation.
  • To highlight current challenges and future perspectives in glycosylation pathways for neuronal development.

Main Methods:

  • Literature review synthesizing existing research on glycosylation and axon guidance.
  • Analysis of studies investigating the role of glycoproteins in neuronal development.
  • Discussion of glycosylation's impact on guidance molecules, receptors, and downstream signaling.

Main Results:

  • Glycosylation significantly modulates the function of guidance cues and receptors.
  • Specific glycosylation patterns influence axonal motility and precise pathfinding towards synaptic targets.
  • This modification adds another layer of complexity to the mechanisms governing neuronal wiring.

Conclusions:

  • Glycosylation is an emerging and critical factor in regulating axonal guidance and neuronal development.
  • Further research into glycosylation pathways is essential for a comprehensive understanding of how axons navigate.
  • Understanding these processes opens new avenues for therapeutic strategies in neurological disorders.