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mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

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The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
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PI3K/mTOR/AKT Signaling Pathway01:22

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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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.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Updated: Mar 28, 2026

A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation
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人間のmTOR複合体1のアーキテクチャ

Christopher H S Aylett1, Evelyn Sauer2, Stefan Imseng2

  • 1Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.

Science (New York, N.Y.)
|December 19, 2015
PubMed
まとめ

研究者は,ヒトのmTORC1複合体の構造を,FKBP-ラパミシンと結合させた. この構造は,どのように複雑な

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科学分野:

  • 分子生物学
  • セルラー信号
  • 構造生物学

背景:

  • ラパミシン (TOR) の標的は,TORC1とTORC2という2つの複合体で存在する細胞成長の主要な調節剤です.
  • 哺乳類のTOR (mTOR) 信号の調節不良は,癌,糖尿病,神経変性などの病気と関連しています.

研究 の 目的:

  • FKBP-ラパミシンに結合するヒトmTORC1複合体の高解像度構造を決定する.
  • mTORC1の調節と基板の相互作用の基礎となる構造的メカニズムを解明する.

主な方法:

  • クリオ電子顕微鏡 (cryo-EM) で 5. 9 アングストームの解像度.
  • チャエトミウム・サーモフィラム・ラプターの結晶学的な研究 4.3 アングストーム解像度.

主要な成果:

  • この研究は,ヒトのmTORC1の構造,そのサブユニットであるRaptorとmLST8をFKBP-ラパミシンと複合的に解明した.
  • 決定された構造は,FKBP-ラパミシンとmTORC1のアーキテクチャが活性部位へのアクセスを制限することを説明します.
  • ラプターの保存されたアミノ末端領域はキナーゼ活性部位の近くに位置し,基質認識における役割を示唆している.

結論:

  • 解明された構造は,mTORC1活動の調節に関する重要な洞察を提供します.
  • mTORC1の構造を理解することは,mTORC1の調節不良に関連した疾患を標的とした治療戦略の開発に不可欠です.