Related Experiment Video

Updated: Jul 9, 2026

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
08:33

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis

Published on: December 5, 2017

The nucleoporin Nup358 associates with and regulates interphase microtubules

Jomon Joseph1, Mary Dasso

  • 1National Centre for Cell Science, Ganeshkhind, Pune 411 007, India. josephj@nccs.res.in

FEBS Letters
|December 12, 2007
PubMed

Insights

The nucleoporin Nup358 interacts with interphase microtubules, influencing their organization and stability. Depletion of Nup358 impairs microtubule stabilization during cell migration.

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Nucleoporins (Nups) are essential components of the nuclear pore complex (NPC).
  • Nup358 is known to be involved in kinetochore-microtubule interactions during cell division.

Purpose of the Study:

  • To investigate the role of Nup358 in regulating interphase microtubules.
  • To identify the Nup358 region responsible for microtubule interaction.

Main Methods:

  • Overexpression and ectopic expression of Nup358 domains.
  • Microtubule stability assays using nocodazole.
  • RNA interference (RNAi) mediated depletion of Nup358.
  • Analysis of microtubule acetylation and organization.

Main Results:

  • Nup358 interacts with interphase microtubules via its N-terminal region (BPN).
  • Overexpression of Nup358 or its BPN domain increases microtubule bundling, stability, and acetylation.
  • Nup358 depletion disrupts polarized microtubule stabilization during cell migration.

Conclusions:

  • Nup358 plays a crucial role in regulating interphase microtubule organization and dynamics.
  • The N-terminal region of Nup358 is critical for its interaction with microtubules.

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

Related Concept Videos

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...
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...
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...
Anaphase A and B01:39

Anaphase A and B

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.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
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...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

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...