超膜タンパク質によるシグナル伝達は,ギアをシフトさせます
1Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA. inouye@umdnj.edu
Cell
|September 9, 2006
まとめ
多くのプロカリオットタンパク質に含まれるHAMPドメインは信号を伝達する. Hulko et al. ハルコと仲間たち NMR構造を決定し,4ヘリクスのコイル回転による信号伝導を明らかにしました.
科学分野:
- バイオケミストリー バイオケミストリー
- 構造生物学 構造生物学とは
- 微生物学 微生物学とは
背景:
- HAMPドメインは,多くのプロカリオットのトランスメブランタンパク質に存在する保存されたシグナリングモジュールです.
- これらのタンパク質には,ヒスティジンキナーゼ,アデニリルサイクラゼ,ケモタキシス受容体,リン酸塩酵素などの必須成分が含まれ,ドメインの幅広い機能的重要性を強調しています.
研究 の 目的:
- HAMPドメインによって媒介される信号伝導の構造的基礎を解明する.
- 核磁共振 (NMR) スペクトロスコピーを使用してHAMPドメインの3次元構造を決定する.
主な方法:
- 核磁共振 (NMR) スペクトロスコピーは,HAMPドメインの原子レベルの構造を決定するために使用されました.
- ドメインのアーキテクチャと潜在的な作用メカニズムを理解するために,構造データを分析しました.
主要な成果:
- NMR構造は,HAMPドメインの4ヘリックス並列のコイル配列を明らかにした.
- データによると,シグナル伝導は,この巻き巻き構造の回転メカニズムを通して発生する.
結論:
- HAMPドメインは,プロカリオットのトランスメブランタンパク質の信号トランスデューサーとして機能します.
- 4ヘリクスのコイルを単純に回転させることが,信号伝達のための提案されたメカニズムです.
関連する概念動画
Signal Transduction: Overview
Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
Typically, signal transduction involves three...
Amplifying Signals via Second Messengers
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Intracellular Signaling Cascades
Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Intracellular Signaling Cascades
Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
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...
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...


