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Microtubule Formation01:23

Microtubule Formation

Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation of...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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.
Microtubule Instability02:17

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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Instability02:17

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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

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Las EB reconocen una tapa estructural dependiente de nucleótidos en los extremos de microtúbulos en crecimiento.

Sebastian P Maurer1, Franck J Fourniol, Gergő Bohner

  • 1Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.

Cell
|April 17, 2012
PubMed
Resumen

Las proteínas de unión final (EBs) rastrean los extremos de los microtúbulos en crecimiento al unirse a estructuras específicas. Este estudio revela cómo el Mal3 EB

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Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología Estructural Biología estructural.
  • La bioquímica es la bioquímica.

Sus antecedentes:

  • Los extremos de los microtúbulos en crecimiento son sitios de unión cruciales para las proteínas que regulan la dinámica de los microtúbulos.
  • Las proteínas de unión final (EB) identifican y se unen a estos extremos dinámicos de microtúbulos, reclutando otros factores.
  • La base estructural precisa para el reconocimiento de EB de los extremos de microtúbulos en crecimiento sigue siendo en gran medida desconocida.

Objetivo del estudio:

  • Determinar el modelo pseudoatómico de cómo el dominio de homología de calponina (CH) de la levadura de fisión EB Mal3 se une a los extremos de microtúbulos en crecimiento.
  • Para aclarar las características estructurales de la región del extremo del microtúbulo reconocido por EBs.
  • Comprender la relación entre la estructura de los extremos de los microtúbulos, la unión EB y la dinámica de los microtúbulos.

Principales métodos:

  • Microscopía cryoelectrónica (cryo-EM) para la determinación estructural de alta resolución.
  • Reconstrucción de una sola partícula subnanométrica para construir el modelo pseudoatómico.
  • Imágenes de fluorescencia para validar la unión y la dinámica in situ.

Principales resultados:

  • Se generó un modelo pseudoatómico del dominio Mal3 CH unido a los extremos de microtúbulos en crecimiento.
  • Se observó que el dominio Mal3 CH conecta los protofilamentos de microtúbulos, excluyendo la costura.
  • La unión se produce cerca del sitio de unión de GTP, lo que sugiere sensibilidad al estado de los nucleótidos.

Conclusiones:

  • La estructura revela cómo las EB reconocen y se unen a los extremos dinámicos de los microtúbulos.
  • La unión EB está vinculada espacialmente al sitio de unión de nucleótidos del microtúbulo, lo que potencialmente puede detectar su estado.
  • Esto proporciona un vínculo estructural entre la inestabilidad dinámica de los microtúbulos y el mecanismo de seguimiento final de los EB.