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Related Concept Videos

The Mitotic Spindle02:27

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The mitotic spindle—or spindle apparatus—is a eukaryotic, cytoskeletal structure made up of long protein fibers called microtubules. Formed during cell division, the spindle separates sister chromatids and moves them to opposite ends of a parental cell, where the now individual chromosomes are distributed to two daughter cell nuclei.
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The assembly and positioning of the mitotic spindle depend on the combined forces generated by microtubule dynamics, motor proteins and cross-linkers. Here we present our recently developed methods in which the geometrical confinement of spherical emulsion droplets is used for the bottom-up reconstitution of basic mitotic...
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Here we present a protocol to assess the dynamics of spindle formation and mitotic progression. Our application of time-lapse imaging enables the user to identify cells at various stages of mitosis, track and identify mitotic defects, and analyze spindle dynamics and mitotic cell fate upon exposure to anti-mitotic...
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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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Here, we present a protocol for specific siRNA-mediated mRNA depletion followed by immunofluorescence analysis to evaluate meiotic spindle assembly and organization in mouse oocytes. This protocol is suitable for in vitro depletion of transcripts and functional assessment of different spindle and/or MTOC-associated factors in...
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Related Experiment Video

Updated: Jan 20, 2026

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets
10:52

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Published on: August 13, 2016

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HMMR/RHAMM recruits SACK1D/FAM83D-CK1α complex at the mitotic spindle to control spindle alignment.

Tyrell N Cartwright1, Naveen K Nakarakanti1, Karen Dunbar1

  • 1Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.

Iscience
|January 19, 2026
PubMed
Summary

Hyaluronan-mediated motility receptor (HMMR) is crucial for the SACK1D-CK1α complex assembly at the mitotic spindle. HMMR binding stabilizes SACK1D, which is degraded upon mitotic exit through hyperphosphorylation.

Keywords:
Cell biologyMolecular biology

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Related Experiment Videos

Last Updated: Jan 20, 2026

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Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

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Organization of the Mitotic Spindle
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Live Cell Imaging to Assess the Dynamics of Metaphase Timing and Cell Fate Following Mitotic Spindle Perturbations
07:14

Live Cell Imaging to Assess the Dynamics of Metaphase Timing and Cell Fate Following Mitotic Spindle Perturbations

Published on: September 20, 2019

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The SACK1D/FAM83D-CK1α complex plays a role in mitotic spindle positioning and accurate cell division.
  • The precise mechanisms governing the assembly and disassembly of this complex during the cell cycle are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying the assembly and regulation of the SACK1D-CK1α complex at the mitotic spindle.
  • To identify novel factors involved in the complex's function and stability during mitosis.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • Immunofluorescence microscopy to visualize protein localization during mitosis.
  • Site-directed mutagenesis to investigate the role of specific protein domains.

Main Results:

  • Hyaluronan-mediated motility receptor (HMMR) is essential for SACK1D-CK1α complex formation and spindle alignment.
  • HMMR binds to the C-terminal α-helix of SACK1D, stabilizing the protein.
  • Mitotic hyperphosphorylation of SACK1D targets it for destruction upon mitotic exit, requiring the C-terminal α-helix.

Conclusions:

  • HMMR is a key regulator of SACK1D-CK1α complex assembly and function at the mitotic spindle.
  • SACK1D stability during mitosis is regulated by HMMR binding and subsequent hyperphosphorylation-mediated degradation.