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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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,...
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Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

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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...
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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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...
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Anchoring Junctions01:03

Anchoring Junctions

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Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Updated: May 3, 2026

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 19, 2009

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セマフォリンがプレキシン受容体を通して信号を送る構造的基礎.

Terukazu Nogi1, Norihisa Yasui, Emiko Mihara

  • 1Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

Nature
|October 1, 2010
PubMed
まとめ

セマフォリン-プレキシンのシグナル伝達には,ホモダイマーからヘテロテトラマーへの構造的なスイッチが含まれ,細胞表面受容体活性化がどのように細胞内部にシグナルを送信するかを明らかにします.

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Use of pHluorin to Assess the Dynamics of Axon Guidance Receptors in Cell Culture and in the Chick Embryo
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A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors
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関連する実験動画

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Use of pHluorin to Assess the Dynamics of Axon Guidance Receptors in Cell Culture and in the Chick Embryo
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A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors
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科学分野:

  • 分子生物学は分子生物学である.
  • 細胞シグナル伝達 細胞信号伝達
  • 構造生物学 構造生物学とは

背景:

  • セマフォリンとプレキシンは,様々な生物学的プロセスとヒトの病気に関与する重要な細胞シグナル伝達分子です.
  • プレキシン受容体へのリガンド結合は,細胞内GTPase活性化タンパク質 (GAP) の活性性を活性化しますが,構造的メカニズムは不明です.

研究 の 目的:

  • セマフォリン・プレキシン受容体活性化の構造的メカニズムを解明する.
  • セマフォリン6A (Sema6A) とプレキシンA2 (PlxnA2) の構造を,結合前の状態と結合後の状態で決定する.

主な方法:

  • X線結晶学を使用して,Sema6AとPlxnA2の断片の構造を決定しました.
  • Sema6A-PlxnA2の複雑な構造を分析した.
  • 変異したリガンド/受容体による細胞ベースの活性アッセイが実施されました.

主要な成果:

  • Sema6Aは"対面"ホモジマーを形成し,PlxnA2は結合前に"ヘッドオン"ホモジマー配列を採用した.
  • Sema6A-PlxnA2複合体は2:2ヘテロテトラマーを形成し,PlxnA2はSema6Aホモダイマーに分離してドッキングすることによって"パートナー交換"をします.
  • Sema6Aの"対面"ホモディマー配列は生理学的に関連しており,シグナル伝達中に維持されます.

結論:

  • プレキシンホモジマーからヘテロジマーへの移行は,信号伝送の鍵です.
  • これらの移行は,プレキシンの分子軸を方向転換し,シグナルのシトプラズマ領域への伝達を促進し,GAPドメインの活性化を誘導します.