TAP分子の構造的特徴:T細胞受容体/T3複合体とTy-1複合体と区別される,フォスファディチルイノシトール結合グリコタンパク質
Cell
|November 7, 1986
まとめ
T細胞活性化タンパク質 (TAP) は,細胞表面のグリコタンパク質である. Thy-1分子に似た脂質アンカーを介して細胞膜に結合し,信号伝達における役割を示唆しています.
科学分野:
- 免疫学 免疫学とは
- 分子生物学は分子生物学である.
- 細胞生物学 細胞生物学
背景:
- T細胞活性化タンパク質 (TAP) は,T細胞活性化に関与するLy-6遺伝子産物である.
- T細胞活性化の分子メカニズムを理解することは,免疫学と疾患治療において極めて重要です.
研究 の 目的:
- T細胞活性化タンパク質 (TAP) を特徴づけるために.
- TAPの細胞表面発現と膜固定を調査する.
- 膜信号伝導におけるTAPの潜在的な役割を調査する.
主な方法:
- 細胞のメタボリックラベル付け.
- TAPの降水と特徴.
- 削減条件と非削減条件下でTAPの分析.
- フォスファティディル・イノシトール固有のフォスフォリファーゼC (PI-PLC) による治療.
主要な成果:
- TAPは,分子量10-12kd (非減少) と15-18kd (減少) のグリコプロテインとして識別されました.
- 3つのTAP帯のうち2つは,細胞表面に発現した.
- TAPはPI-PLC治療後に細胞スーパーナタンから回収され,脂質膜の付着を示した.
- このアンカージングメカニズムは,Thy-1分子と共有されています.
結論:
- TAPは,細胞表面のグリコタンパク質で,フォスファディチルニノシトール脂質を介して細胞膜に固定されています.
- TAPの脂質アンカリングメカニズムは,Thy-1.1のメカニズムに似ています.
- この発見は,T細胞における膜信号伝導のための潜在的に新しい結合を示唆している.
さらに関連する動画
関連する概念動画
Phosphoinositides and PIPs
7.7K
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...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
7.7K
Tail-anchoring of Proteins in the ER Membrane
2.8K
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...
2.8K
Assembly of Signaling Complexes
4.7K
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
4.7K
Receptor Tyrosine Kinases
15.6K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
15.6K
Intracellular Signaling Affects Focal Adhesions
2.8K
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...
Some...
2.8K
Transducer Mechanism: Enzyme-Linked Receptors
4.4K
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include:
4.4K


