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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 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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Visualizing microtubule structural transitions and interactions with associated proteins.

Eva Nogales1, Rui Zhang2

  • 1Molecular and Cell Biology Department and QB3 Institute, UC Berkeley, CA 94720, United States; Howard Hughes Medical Institute, UC Berkeley, CA 94720, United States; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States.

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Cryo-electron microscopy (cryo-EM) reveals microtubule (MT) structure and function at atomic detail. This technique visualizes tubulin interactions, conformational changes, and associated protein binding, advancing our understanding of cellular processes.

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Area of Science:

  • Structural Biology
  • Cell Biology
  • Biophysics

Background:

  • Microtubules (MTs) are crucial cytoskeletal components studied using cryo-electron microscopy (cryo-EM).
  • MTs present unique challenges like seams and lattice disorder for high-resolution imaging.
  • Advances in cryo-EM are overcoming these challenges, yielding detailed structural insights.

Purpose of the Study:

  • To highlight recent advancements in cryo-EM for microtubule structural studies.
  • To showcase the visualization of molecular interactions and conformational dynamics within microtubules.
  • To emphasize the role of cryo-EM in understanding microtubule-associated proteins (MAPs) and their functions.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for high-resolution imaging of microtubules.
  • Advanced image processing techniques to resolve MT lattice disorder and features like the MT seam.
  • Structural analysis of tubulin subunit interactions and conformational states.

Main Results:

  • Atomic-detail visualization of lateral contacts between tubulin subunits.
  • Elucidation of conformational changes associated with GTP hydrolysis and MT lattice strain.
  • Detailed description of interactions between microtubules and microtubule-associated proteins (MAPs).

Conclusions:

  • Cryo-EM provides unprecedented insights into microtubule structure, dynamics, and interactions.
  • Understanding MT structure is key to deciphering their roles in cellular processes.
  • MAP interactions revealed by cryo-EM are critical for regulating MT functions like dynamic instability and cargo transport.