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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.
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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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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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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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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Structural basis for CRMP2-induced axonal microtubule formation.

Shinsuke Niwa1, Fumio Nakamura2,3, Yuri Tomabechi4

  • 1Frontier Research Institute for Interdisciplinary Sciences and Department of Life Sciences, Tohoku University, Aoba-ku, Sendai, 980-8578, Japan.

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Collapsin response mediator protein 2 (CRMP2) promotes axon formation by interacting with tubulin dimers. This interaction, mediated by CRMP2's H19 helix, drives microtubule assembly crucial for axon development.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Collapsin response mediator protein 2 (CRMP2) is a key regulator of neuronal polarity and axonal growth.
  • The precise mechanism by which CRMP2 influences microtubule dynamics during axonogenesis remains unclear.

Purpose of the Study:

  • To elucidate the structural basis of CRMP2 interaction with tubulin and microtubules.
  • To understand how CRMP2 binding affects microtubule behavior to promote axon formation.

Main Methods:

  • X-ray crystallography to determine the structure of CRMP2 bound to tubulin.
  • In vitro biochemical and functional assays to assess microtubule assembly dynamics.
  • Genetic manipulation of CRMP2 in neuronal models (chick neurons, C. elegans).

Main Results:

  • The H19 helix of CRMP2 directly interacts with soluble tubulin dimers, distinct from microtubule-bound interactions.
  • CRMP2's H19-mediated interaction accelerates the formation of GTP-tubulin polymers, characteristic of axonal microtubules.
  • Mutations in the H19 region disrupt axon elongation and microtubule structure in vivo.

Conclusions:

  • CRMP2 utilizes its H19 helix to interact with tubulin dimers, initiating the formation of axonal microtubules.
  • This H19-mediated mechanism is essential for effective axonogenesis and neuronal development.