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Microtubule Instability02:17

Microtubule Instability

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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...
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Microtubule Instability02:17

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Microtubules01:18

Microtubules

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Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer....
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Microtubules01:35

Microtubules

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There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.
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Microtubules are dynamic structures that undergo cycles of catastrophe and rescue. The microtubules play a central role in cell division by forming the spindle apparatus for segregating the chromosomes. This makes them ideal targets for regulating dividing cells in tumors and malignant cancer cells. Microtubule stabilizing drugs help stabilize the microtubule formation and promote its polymerization. Paclitaxel was the first microtubule stabilizing agent used as anticancer drug in chemotherapy...
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Microtubule Formation01:23

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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...
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Updated: Apr 12, 2026

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
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Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles

Published on: November 5, 2020

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Descifrando el código de la tubulina.

Stefan Raunser1, Christos Gatsogiannis1

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Cell
|May 23, 2015
PubMed
Resumen
Este resumen es generado por máquina.

Los investigadores revelaron la estructura de las enzimas similares a la tubulina tirosina ligasa (TTLL), cruciales para la modificación de los microtúbulos. Esto proporciona nuevos conocimientos sobre cómo estas enzimas interactúan con los microtúbulos para regular las funciones celulares.

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Área de la Ciencia:

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

Sus antecedentes:

  • Los microtúbulos son componentes esenciales del citoesqueleto involucrados en varios procesos celulares.
  • Las modificaciones posttraducionales, como la glutamilación, regulan la función de los microtúbulos.
  • La familia de enzimas similares a la tubulina tirosina ligasa (TTLL) cataliza la glutamilación de los microtúbulos.

Objetivo del estudio:

  • Para determinar la base estructural de la actividad de la enzima TTLL.
  • Para dilucidar el mecanismo por el cual las enzimas TTLL interactúan con los microtúbulos.
  • Para entender cómo la glutamilación marca los microtúbulos para las interacciones de proteínas específicas.

Principales métodos:

  • Se utilizó la cristalografía de rayos X para obtener la estructura de una proteína TTLL.
  • Se empleó la microscopía crioectrónica (cryo-EM) para visualizar los complejos TTLL-microtubulares.
  • Se realizaron ensayos bioquímicos para evaluar la actividad enzimática y la unión al sustrato.

Principales resultados:

  • Se determinó la primera estructura atómica de una enzima TTLL.
  • Las estructuras de las enzimas TTLL en complejo con los microtúbulos revelaron interfaces de interacción clave.
  • El estudio aclaró el mecanismo catalítico de la glutamilación mediada por TTLL.

Conclusiones:

  • Las ideas estructurales y mecanicistas avanzan en nuestra comprensión de la regulación de los microtúbulos.
  • Este trabajo proporciona una base para una mayor investigación sobre las TTLL y sus roles en la salud y la enfermedad.
  • Los hallazgos abren caminos para el desarrollo de nuevas estrategias terapéuticas dirigidas a la dinámica de los microtúbulos.