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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
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Combinatorial gene control is the synergistic action of several transcriptional factors to regulate the expression of a single gene. The absence of one or more of these factors may lead to a significant difference in the level of gene expression or repression.
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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.
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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...
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Regulación dual de BACH1 por las ligasas E3 del tipo SCF complementarias

Benedikt Goretzki1, Maryam Khoshouei1, Martin Schröder1

  • 1Discovery Sciences, Novartis Biomedical Research, Basel, Switzerland.

Cell
|December 10, 2024
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Resumen

Este estudio revela cómo la proteína BACH1, un regulador del estrés oxidativo y el oncogén, es controlada por dos ligasas de ubiquitina. Un mecanismo de conmutación permite que FBXO22 o FBXL17 se unan a BACH1 dependiendo de su estado estructural, impactando el cáncer y los trastornos por estrés oxidativo.

Palabras clave:
BACH1 (en inglés)Las ligasas Cullin-RINGCaja FEn el caso de las personas físicas:En el caso de los vehículos de motor:Hemo por nitrosilación de SModificación de la cisteínaInterruptor de ligasaEl estrés oxidativo

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Área de la Ciencia:

  • La bioquímica
  • Biología molecular
  • Biología celular

Sus antecedentes:

  • El dominio de amplio complejo, tramtrack y bric-à-brac (BTB) y el homólogo CNC 1 (BACH1) es un regulador clave del estrés oxidativo celular y un oncogén.
  • BACH1 está regulado post-traducionalmente por las ligasas de ubiquitina SCFFBXO22 y SCFFBXL17, pero el mecanismo de reconocimiento bajo estrés oxidativo es desconocido.

Objetivo del estudio:

  • Aclarar el mecanismo por el cual FBXO22 y FBXL17 reconocen BACH1 en condiciones de estrés oxidativo.
  • Comprender el mecanismo de conmutación de la ligasa que controla la regulación post-traducional de BACH1.

Principales métodos:

  • Análisis estructural del dimer BACH1 BTB y su interacción con FBXO22.
  • Investigar el impacto de las mutaciones asociadas al cáncer y las modificaciones de la cisteína en la estabilidad de BACH1 y la unión a la ligasa.
  • Caracterización del reconocimiento de BACH1 por FBXL17 como monómero.

Principales resultados:

  • FBXO22 reconoce un degrón cuaternario dentro de una hoja β intercambiada por dominio del dimero BACH1 BTB.
  • Las mutaciones en el cáncer y las modificaciones en la cisteína desestabilizan el degrón FBXO22, deteriorando la unión.
  • Estas modificaciones exponen un degradón distinto en la interfaz del dímero, permitiendo que FBXL17 se una al monómero BACH1.

Conclusiones:

  • Un mecanismo de conmutación de ligasa regula BACH1 por FBXO22 y FBXL17 basado en la estabilidad del dominio BTB.
  • Estos hallazgos proporcionan información mecanicista sobre la respuesta al estrés oxidativo.
  • El estudio puede informar estrategias terapéuticas para los trastornos relacionados con el estrés oxidativo y el cáncer.