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Videos de Conceptos Relacionados

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Protein Glycosylation01:25

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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.
Glycosylation occurs in...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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Proteoglycans01:05

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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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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Other Glycolytic Pathways01:24

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The pentose phosphate pathway (PPP) operates in parallel with glycolysis, facilitating the metabolism of both pentoses and glucose. This pathway consists of two distinct phases: the oxidative and non-oxidative phases. While it does not directly generate ATP, the intermediates formed during the process can integrate into glycolysis, contributing to cellular energy metabolism when required.Oxidative Phase: NADPH ProductionThe oxidative phase of the pentose phosphate pathway is primarily...
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SnapShot: Rutas de procesamiento de N-glucosilación a través de los reinos

Cheng-Yu Chung1, Natalia I Majewska1, Qiong Wang1

  • 1Department of Chemical and Biomolecular Engineering, The Johns Hopkins University, Baltimore, MD 21218, USA.

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Resumen

Este estudio explora la glicosilación de proteínas, un proceso clave en el que se agregan carbohidratos a las proteínas. Comprender estas vías es crucial para descifrar la función y la localización de proteínas en diversos organismos.

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Área de la Ciencia:

  • La bioquímica
  • Biología molecular
  • Biología celular

Sus antecedentes:

  • La modificación post-traducional (PTM) de las proteínas tiene un impacto significativo en sus funciones biológicas.
  • La glicosilación de proteínas, la adición de fracciones de carbohidratos, es un PTM crítico que afecta la localización y la función de las proteínas.
  • La variabilidad y la complejidad de los glicanos presentan desafíos para comprender sus funciones precisas.

Objetivo del estudio:

  • Para presentar una visión concisa de las vías centrales involucradas en la glicosilación de proteínas.
  • Para resaltar los mecanismos conservados y divergentes de instalación de glicano en diferentes organismos.
  • Proporcionar un recurso fundamental para los investigadores que estudian la glucosilación de proteínas.

Principales métodos:

  • Revisión y síntesis de la literatura existente sobre las vías de glicosilación de proteínas.
  • Análisis comparativo de los mecanismos de glicosilación en varios organismos modelo.
  • Centrarse en el mecanismo enzimático responsable de la síntesis y transferencia de glicano.

Principales resultados:

  • Identificación de las vías centrales conservadas para la síntesis de precursores de glicano.
  • Descripción de diversas estrategias enzimáticas para el alargamiento y la ramificación de la cadena de glicanos.
  • Destacando las variaciones específicas del organismo en las estructuras de glicano y su ensamblaje.

Conclusiones:

  • Las vías de glicosilación de proteínas son fundamentales para los procesos celulares.
  • Comprender estas vías es esencial para interpretar la función y la localización de las proteínas.
  • Esta visión general sirve como una guía para la complejidad de la biosíntesis de glicanos en toda la vida.