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The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
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関連する実験動画

Updated: Oct 17, 2025

Identification of Functional Protein Regions Through Chimeric Protein Construction
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ALKファミリー受容体のサイトカイン媒介活性化の構造的基礎

Steven De Munck1,2, Mathias Provost1,2, Michiko Kurikawa3

  • 1Unit for Structural Biology, Department of Biochemistry and Microbiology, Ghent University, Ghent, Belgium.

Nature
|October 14, 2021
PubMed
まとめ

アナプラスティックリンパ腫キナーゼ (ALK) と白血球チロシンキナーゼ (LTK) の構造的な洞察は,新しいサイトカイン結合機構を明らかにする. これらの発見は,ALKファミリー受容体複合体とその様々な疾患における役割を理解するための青写真を提供します.

さらに関連する動画

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

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Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity
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Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity

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関連する実験動画

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A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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科学分野:

  • 構造生物学
  • 受容体チロシンキナーゼの分子機構

背景:

  • アナプラスティックリンパ腫キナーゼ (ALK) と白血球チロシンキナーゼ (LTK) は,神経発育,がん,自己免疫疾患に関与する受容体チロシンキナーゼである.
  • これらのキナーゼは エネルギー消費と体重増加の調節にも 役割を果たします
  • 機能的重要性と治療的関連性にもかかわらず,ALK,LTK,およびそれらのサイトカイン相互作用に関する構造情報は限られている.

研究 の 目的:

  • ALKとLTKの相互作用の構造的基礎を,その関連サイトカインであるALKAL1とALKAL2と解明する.
  • リガンド媒介の受容体二分化と活性化のメカニズムを理解する.
  • ALKファミリー受容体複合体の構造設計図を提供する.

主な方法:

  • ヒトALKとLTKのサイトカイン結合セグメントの構造を決定するために,X線結晶学を用いた.
  • ALK/LTK-サイトカイン複合体の構造分析により,新しい構造特性と二分化インターフェースが明らかになった.
  • 構造・機能研究では,細胞ホルモンの好みにおける膜近接EGFのようなドメインの役割を調査した.

主要な成果:

  • ALKとLTKのサイトカイン結合セグメントは,変異したTNFのようなモジュールとグリシン豊富なサブドメインの新しいキメラを特徴としています.
  • ALKAL1とALK2は,二重対称性を持つALK/LTKの二次組成を誘導する単体三ヘリックスバンドルです.
  • ALKの膜近接EGFのようなドメインは,特定のサイトカインを好むことを決定する.

結論:

  • ALKファミリーの受容体-サイトカイン複合体の詳細な構造とメカニズム設計図が確立されています.
  • この研究は,受容体チロシンキナーゼのリガンド媒介型二分化メカニズムを明らかにした.
  • この発見は,ALK/LTKのシグナル伝達経路に関する理解を深め,治療開発への影響を及ぼします.