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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.
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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 microtubule array...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Related Experiment Video

Updated: May 23, 2026

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments
06:53

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

IκBα is not required for axon initial segment assembly.

Shelly A Buffington1, Jürgen M Sobotzik, Christian Schultz

  • 1Department of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA.

Molecular and Cellular Neurosciences
|March 27, 2012
PubMed
Summary
This summary is machine-generated.

Phosphorylated inhibitor of NF-κB alpha (pIκBα) is not enriched at the axon initial segment (AIS). pIκBα is not required for AIS assembly or the clustering of key AIS proteins like ankyrinG and Na(+) channels.

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A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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Methods for the Modulation and Analysis of NF-κB-dependent Adult Neurogenesis

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Related Experiment Videos

Last Updated: May 23, 2026

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments
06:53

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
11:27

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

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Methods for the Modulation and Analysis of NF-κB-dependent Adult Neurogenesis
14:58

Methods for the Modulation and Analysis of NF-κB-dependent Adult Neurogenesis

Published on: February 13, 2014

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • The inhibitor of NF-κB alpha (IκBα) regulates NF-κB signaling.
  • IκBα is implicated in neuronal processes like neurite outgrowth and survival.
  • A phosphorylated form, pIκBα (Ser32/36), was hypothesized to be crucial for axon initial segment (AIS) assembly.

Purpose of the Study:

  • To investigate the role of pIκBα in AIS assembly and protein localization.
  • To validate the proposed function of pIκBα upstream of ankyrinG in AIS formation.
  • To determine if pIκBα is enriched at the AIS in vivo and in vitro.

Main Methods:

  • Analysis of ankyrinG and Na(+) channel clustering in IκBα knockout mice.
  • Immunofluorescence labeling of AIS using phospho-specific pIκBα antibodies in knockout and wild-type neurons.
  • shRNA-mediated knockdown of AIS proteins in cultured hippocampal neurons.

Main Results:

  • AnkyrinG and Na(+) channel clustering at the AIS is normal in IκBα knockout mice.
  • Phospho-specific pIκBα antibodies exhibit non-specific AIS labeling in knockout neurons.
  • Knockdown of most AIS proteins does not abolish pIκBα antibody labeling.
  • pIκBα antibodies cross-react with a non-membrane-associated cytoskeletal protein.

Conclusions:

  • pIκBα is not specifically enriched at the AIS.
  • pIκBα is not required for the assembly of the AIS or the recruitment of key AIS proteins.
  • The previously reported enrichment and function of pIκBα at the AIS are likely due to antibody cross-reactivity.