Related Experiment Video

Updated: Aug 8, 2026

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
07:09

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells

Published on: July 31, 2012

An associated molecule, p64, with IL-2 receptor beta chain. Its possible involvement in the formation of the

T Takeshita1, K Ohtani, H Asao

  • 1Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.

Journal of Immunology (Baltimore, Md. : 1950)
|April 1, 1992
PubMed

Insights

The membrane molecule p64 associates with the Interleukin-2 Receptor beta-chain (IL-2R beta) and is crucial for forming a functional IL-2 receptor complex. This finding sheds light on IL-2R complex assembly and signaling.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The Interleukin-2 Receptor (IL-2R) is critical for T cell function.
  • A previously identified membrane molecule, p64, co-precipitates with the IL-2R beta-chain in human T cells.

Purpose of the Study:

  • To investigate the biological significance of p64 in the formation of the functional IL-2R complex.
  • To examine the relationship between p64 association with IL-2R beta, IL-2 binding, and receptor functionality.

Main Methods:

  • Utilized cell lines transfected with Interleukin-2 Receptor alpha and/or beta-chain cDNAs.
  • Assessed IL-2 binding ability and p64 co-precipitation with IL-2R beta.
  • Compared two MOLT4-derived subclones (MOLT beta-11 and MOLT beta-12) expressing varying levels of IL-2R beta.

Main Results:

  • MOLT beta-11 and MOLT beta-12 cells expressed similar IL-2R beta levels but differed in IL-2 binding sites.
  • The amount of p64 co-precipitated with IL-2R beta was proportional to the number of IL-2 binding sites.
  • p64 co-precipitation and IL-2 binding were not detected in HeLa and COS7 cells transfected with IL-2R beta alone or with both IL-2R alpha and beta chains.

Conclusions:

  • p64 associates with IL-2R beta.
  • p64 plays a significant role in the formation of the functional IL-2 receptor complex.
  • The findings suggest p64 is essential for IL-2R-mediated signaling.

More Related Videos

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation12:09

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
T Cell Activation and Clonal Selection01:22

T Cell Activation and Clonal Selection

T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...