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Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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Updated: Jun 25, 2026

Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
06:58

Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling

Published on: October 7, 2021

E and ID proteins branch out.

Barbara L Kee1

  • 1Department of Pathology, University of Chicago, Chicago, Illinois 60637, USA. bkee@bsd.uchicago.edu

Nature Reviews. Immunology
|February 26, 2009
PubMed
Summary
This summary is machine-generated.

E and inhibitor of DNA binding (ID) proteins regulate gene expression during development. Recent studies show these proteins are crucial for lymphoid lineage differentiation and have new roles in hematopoietic stem cells.

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Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Immunology

Background:

  • E proteins and inhibitor of DNA binding (ID) proteins are key transcriptional regulators.
  • E2A proteins are vital for B- and T-cell lineage commitment and differentiation.
  • ID proteins modulate the function of E proteins in lymphoid lineages.

Purpose of the Study:

  • To review recent studies on the role of E and ID proteins in lymphoid lineage differentiation.
  • To explore novel functions of E and ID proteins in hematopoietic stem cells and their progeny.

Main Methods:

  • Literature review of recent studies.
  • Analysis of transcriptional regulatory networks.
  • Examination of protein functions in stem cells and differentiated lineages.

Main Results:

  • E and ID proteins have broader roles in the differentiation of multiple lymphoid lineages.
  • New functions identified for E and ID proteins in hematopoietic stem cells.
  • These proteins also impact lymphoid-primed multipotent progenitor cells.

Conclusions:

  • E and ID proteins are essential regulators in diverse lymphoid differentiation pathways.
  • Their roles extend beyond mature lymphocytes to stem and progenitor cells.
  • Further research into these proteins could reveal new therapeutic targets in hematopoiesis.