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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Cytoplasm01:24

Cytoplasm

The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The cytosol is a rich broth of water, ions, salts, and various organic molecules.
Protein Folding and Misfolding
The cytoplasm is the location for several cellular processes, including protein synthesis and folding. The aqueous nature of the cytosol promotes protein folding such that the hydrophobic amino acid side chains are buried in the protein...

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Related Experiment Video

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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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The cytoplasmic AID complex.

Julien Häsler1, Cristina Rada, Michael S Neuberger

  • 1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. julien.hasler@gmail.com

Seminars in Immunology
|June 16, 2012
PubMed
Summary
This summary is machine-generated.

Most Activation Induced Deaminase (AID) protein resides in the cytoplasm, forming a complex with translation elongation factor 1α (eEF1A). This review explores the cytoplasmic AID complex and its potential roles in regulating nuclear import.

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Activation Induced Deaminase (AID) is crucial for antibody gene diversification.
  • Despite its nuclear function, significant AID protein is localized in the cytoplasm.
  • The cytoplasmic localization of AID suggests regulatory mechanisms controlling its nuclear access.

Purpose of the Study:

  • To review current knowledge on the cytoplasmic AID complex.
  • To discuss the composition and characteristics of the cytoplasmic AID complex.
  • To explore potential functions of the cytoplasmic AID complex in regulating AID nuclear import.

Main Methods:

  • Literature review of studies on AID localization and function.
  • Analysis of data regarding the size and composition of the cytoplasmic AID complex.
  • Speculative analysis of protein-protein interactions involving AID and chaperones.

Main Results:

  • The cytoplasmic AID complex is estimated to be 300-500 kDa (10-11S).
  • Translation elongation factor 1α (eEF1A) is a major component of the cytoplasmic AID complex.
  • Interactions with chaperones are implicated in AID regulation.

Conclusions:

  • The cytoplasmic AID complex, including eEF1A, likely plays a role in regulating AID's localization.
  • This complex may control the retention of AID in the cytoplasm and its subsequent release for nuclear import.
  • Understanding the cytoplasmic AID complex is key to elucidating the regulation of antibody gene diversification.