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Videos de Conceptos Relacionados

The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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In Vitro Analysis of E3 Ubiquitin Ligase Function
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In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Los E2 secuenciales impulsan el ensamblaje de la cadena de poliubiquitina en los objetivos de APC.

Monica C Rodrigo-Brenni1, David O Morgan

  • 1Department of Physiology, University of California, San Francisco, CA 94158, USA.

Cell
|July 17, 2007
PubMed
Resumen

El complejo promotor de anafase (APC) utiliza enzimas E2 secuenciales, Ubc4 y Ubc1, para el ensamblaje de la cadena de ubiquitina. Este mecanismo es crucial para la progresión del ciclo celular y la destrucción proteasomal de las proteínas diana.

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Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología Molecular Biología Molecular
  • La bioquímica es la bioquímica.

Sus antecedentes:

  • El complejo promotor de anafase (APC/C), una ligasa de ubiquitina E3 crucial, regula la progresión del ciclo celular al dirigirse a las proteínas clave para la degradación.
  • Los mecanismos precisos por los cuales APC/C y otras ligasas E3 catalizan distintas reacciones de ubiquitinación para el ensamblaje en cadena de la poliubiquitina siguen siendo incompletamente entendidos.

Objetivo del estudio:

  • Para dilucidar las funciones de diferentes enzimas E2 ubiquitina-conjugantes en la formación de la cadena poliubiquitina mediada por APC/C.
  • Identificar enzimas E2 específicas que colaboran con APC/C y caracterizar sus distintas actividades enzimáticas.

Principales métodos:

  • Cribado in vitro de todas las enzimas E2 de la levadura en ciernes como coenzimas APC/C.
  • Análisis de las interacciones APC/C-E2 y las actividades enzimáticas.
  • Evaluación funcional de las cepas de levadura deficientes en enzimas E2 específicas.

Principales resultados:

  • Identificó a Ubc4 y Ubc1 como socios clave de E2 para la levadura en ciernes APC/C.
  • Se demostró que Ubc4 cataliza la monoubiquitinación rápida de objetivos APC/C, mientras que Ubc1 media la extensión de la cadena de poliubiquitina vinculada a K48.
  • Se ha observado pérdida de la función mitotica APC/C en levaduras que carecen tanto de Ubc1 como de Ubc4.
  • Se demostró que el E2-25K humano, un homólogo de Ubc1, también promueve la extensión de la cadena dependiente de APC/C.

Conclusiones:

  • Propuso un modelo donde la acción secuencial de distintas enzimas E2 (Ubc4 y Ubc1) impulsa la poliubiquitinación ligada a K48 de objetivos APC/C.
  • Este mecanismo E2 secuencial facilita la degradación proteasomal oportuna de los sustratos APC/C, asegurando la progresión adecuada del ciclo celular.