Related Experiment Video

Updated: Apr 28, 2026

Self-Assembly of Microtubule Tactoids
08:49

Self-Assembly of Microtubule Tactoids

Published on: June 23, 2022

4.6K

Promoting microtubule assembly: A hypothesis for the functional significance of the +TIP network

Kamlesh K Gupta1, Emily O Alberico, Inke S Näthke

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|June 20, 2014
PubMed

Insights

Microtubule (MT) dynamics are crucial for cells. We propose that microtubule plus-end tracking proteins (+TIPs) form a superstructure, acting as a polymerization chaperone to promote MT assembly.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Microtubule (MT) dynamics are vital for cellular functions.
  • The machinery regulating MT dynamics is not fully understood.
  • +TIPs are proteins that track growing MT ends and regulate MT dynamics.

Purpose of the Study:

  • To investigate the function of the +TIP network.
  • To propose a mechanistic hypothesis for +TIP interactions.
  • To explore how +TIPs influence MT assembly.

Main Methods:

  • Analysis of protein-protein interactions within the +TIP network.
  • Investigating the structural role of +TIPs at MT plus-ends.
  • Hypothesizing a 'polymerization chaperone' function for +TIPs.

Main Results:

  • +TIPs form a complex network of interactions.
  • This network may create a superstructure at the MT tip.
  • This superstructure could constrain MT tip fluctuations.

Conclusions:

  • +TIP interactions may serve to stabilize MT ends.
  • +TIPs might act as polymerization chaperones, promoting MT assembly.
  • This chaperone function offers a new perspective on MT dynamics regulation.
Keywords:
APCCLIP-170EB1light scattering assaymicrotubule bundlingpolymerization chaperone

More Related Videos

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends12:20

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

Published on: March 15, 2014

13.9K
Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy07:20

Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy

Published on: February 18, 2022

2.2K

Related Concept Videos

Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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.
2.1K
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...
6.3K
Spindle Assembly02:50

Spindle Assembly

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.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
3.3K
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...
17.3K
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....
7.9K
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.
74.6K