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Related Concept Videos

Microtubule Formation01:23

Microtubule Formation

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 of...
Microtubules01:18

Microtubules

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. These αβ-heterodimers...
Microtubules01:35

Microtubules

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.
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
Microtubule Instability02:17

Microtubule Instability

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 assembly and...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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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Related Experiment Video

Updated: May 8, 2026

High-resolution Imaging and Analysis of Individual Astral Microtubule Dynamics in Budding Yeast
10:23

High-resolution Imaging and Analysis of Individual Astral Microtubule Dynamics in Budding Yeast

Published on: April 20, 2017

Structure-function analysis of yeast tubulin.

Anna Luchniak1, Yusuke Fukuda, Mohan L Gupta

  • 1Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.

Methods in Cell Biology
|August 27, 2013
PubMed
Summary
This summary is machine-generated.

Budding yeast provides a powerful system for studying microtubule dynamics and tubulin mutations. This research details methods to analyze how specific tubulin mutations impact microtubule stability and cellular functions.

Keywords:
Microtubule dynamicsMicrotubule structureMicrotubule structure–functionMutant tubulinTubulinTubulin mutationsTubulin structureTubulin structure–functionYeast tubulin

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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

Area of Science:

  • Cell Biology
  • Biochemistry
  • Genetics

Background:

  • Microtubules are crucial for cell division, motility, and transport, with function dependent on tubulin dynamics and associated proteins.
  • Studying tubulin structure-function is challenging due to difficulties in obtaining functional proteins and isotype heterogeneity in higher eukaryotes.

Purpose of the Study:

  • To present techniques for generating and analyzing site-specific tubulin mutations in Saccharomyces cerevisiae.
  • To assess the impact of these mutations on cell viability, microtubule stability, dynamic instability, and interactions with microtubule-associated proteins.

Main Methods:

  • Utilized Saccharomyces cerevisiae as a model system due to its single beta-tubulin gene and controllable alpha-isotype expression.
  • Employed site-directed mutagenesis at endogenous loci under native promoters.
  • Developed assays to measure cell viability, overall microtubule stability, dynamic instability parameters, and protein interactions.

Main Results:

  • Established methods for generating homogeneous populations of yeast cells with specific tubulin mutations.
  • Demonstrated the ability to link observed changes in microtubule properties to specific cellular functions.

Conclusions:

  • Saccharomyces cerevisiae is an advantageous system for detailed tubulin structure-function analysis.
  • The presented techniques enable comprehensive investigation of how tubulin mutations affect microtubule behavior and cellular processes.