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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
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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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Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
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A Tubulin Binding Switch Underlies Kip3/Kinesin-8 Depolymerase Activity.

Hugo Arellano-Santoyo1, Elisabeth A Geyer2, Ema Stokasimov1

  • 1Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA.

Developmental Cell
|July 12, 2017
PubMed
Summary
This summary is machine-generated.

Kinesin-8 motors, like Kip3, disassemble microtubules by sensing tubulin curvature at the plus end. This mechanism regulates microtubule size by suppressing ATPase activity and promoting disassembly.

Keywords:
depolymerizationkinesinsmicrotubule associated proteinsmicrotubule dynamicsspindle scaling

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Area of Science:

  • Cell Biology
  • Molecular Motors
  • Cytoskeleton Dynamics

Background:

  • Kinesin-8 motors regulate microtubule size through length-dependent plus-end accumulation.
  • The precise depolymerase mechanism of kinesin-8 remains under investigation.

Purpose of the Study:

  • To investigate an alternative tubulin curvature-sensing model for microtubule depolymerization by the yeast kinesin-8, Kip3.
  • To elucidate the regulatory mechanism controlling cellular microtubule structure size.

Main Methods:

  • Biochemical assays to study Kip3's ATPase activity and microtubule binding.
  • Structural analysis to identify Kip3 elements involved in plus-end binding and depolymerase activity.
  • Mutational analysis of α-tubulin to identify residues critical for Kip3 interaction.

Main Results:

  • Kip3's ATPase activity is suppressed upon binding to curved tubulin at the microtubule plus end.
  • This suppression prolongs Kip3 binding, stabilizes protofilament curvature, and promotes microtubule disassembly.
  • Specific Kip3 structural elements and an α-tubulin residue essential for this interaction were identified.

Conclusions:

  • The tubulin curvature-sensing model provides a new framework for understanding kinesin-8 depolymerase activity.
  • Kip3's regulated interaction with curved tubulin is a key mechanism for controlling microtubule length.
  • This study reveals a critical regulatory mechanism governing cellular microtubule dynamics.