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GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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関連する実験動画

Updated: May 11, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Gドメインの二分化により,ダイナミンのアセンブリ刺激によるGTPアゼ活性が制御されます.

Joshua S Chappie1, Sharmistha Acharya, Marilyn Leonard

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, Maryland 20892, USA.

Nature
|April 30, 2010
PubMed
まとめ

細胞膜分裂に不可欠なGTPaseであるダイナミンは,結晶構造を用いて研究されました. これは,ダイナミンがいかに力強いかを明らかにしています.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 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:

  • ダイナミンは,クラトリン媒介性エンドサイトーシス中の膜分裂に不可欠な非典型のGTPaseである.
  • ダイナミンの基礎およびアセンブリ刺激によるGTP水解を制御する正確なメカニズムは,ほとんど不明のままです.
  • GTPaseエフェクター領域 (GED) は,ダイナミンのGTPase活性に間接的に影響することが知られている.

研究 の 目的:

  • ダイナミンのGTPase活性とその調節の構造的基礎を解明する.
  • ディナミンの組立刺激によるGTP水解のメカニズムを理解するために.
  • ダイナミン触媒による膜分裂に関する洞察を提供するために.

主な方法:

  • ヒトのダイナミン1由来最小のGTPase-GED融合タンパク質の2.0 Å解像度の結晶構造を決定しました.
  • GDP.AlFを真似した移行状態を利用して,タンパク質の二次元形を安定させました.
  • ネズミのダイナミンのG領域と構造を比較した.

主要な成果:

  • 結晶構造は,GDPの存在下でGTPase-GED融合タンパク質の二次元状態を明らかにした.

さらに関連する動画

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
10:19

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Published on: January 24, 2025

関連する実験動画

Last Updated: May 11, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
10:19

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Published on: January 24, 2025

  • この構造はダイナミンの触媒機構を明らかにし,アセンブリ刺激によるGTP水解のメカニズムとしてGドメイン二極化を示した.
  • 活性部位にナトリウムイオンが特定され,アルギニン指が存在しない場合の移行状態の安定化におけるその役割を示唆した.

    • 結論:

    • この研究は,ダイナミンがGドメインの二分化によって,アセンブリ刺激によるGTP水解をどのように達成するかの構造的な説明を提供します.
    • この発見は,移行状態の安定化のための活性部位におけるカチオンの役割を強調しています.
    • 提示された構造は,ダイナミン媒介による膜分裂の基礎となる分子メカニズムに関する重要な洞察を提供します.