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Videos de Conceptos Relacionados

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.
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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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Video Experimental Relacionado

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

La dimerización del dominio G controla la actividad de la GTPasa estimulada por el ensamblaje de la dinamina.

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
Resumen

La dinamina, una GTPasa crucial para la fisión de la membrana celular, fue estudiada utilizando una estructura cristalina. Esto revela cómo funciona la dinámica.

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Last Updated: May 11, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • Biología celular Biología celular.

Sus antecedentes:

  • La dinamina es una atípica GTPasa esencial para la fisión de la membrana durante la endocitosis mediada por clatrina.
  • Los mecanismos precisos que rigen la hidrólisis de GTP basal y estimulada por ensamblaje de la dinamina siguen siendo en gran medida desconocidos.
  • Se sabe que el dominio del efector de la GTPasa (GED) influye indirectamente en la actividad de la GTPasa de la dinamina.

Objetivo del estudio:

  • Para aclarar la base estructural de la actividad de la dinamina GTPasa y su regulación.
  • Para comprender el mecanismo de la hidrólisis de GTP estimulada por el ensamblaje en dinamina.
  • Para proporcionar información sobre la fisión de la membrana catalizada por dinamina.

Principales métodos:

  • Se determinó la estructura cristalina de resolución de 2,0 Å de una proteína de fusión mínima GTPasa-GED derivada de la dinamina 1 humana.
  • Utilizó el estado de transición que imita GDP.AlF ((4)) para estabilizar la forma dimérica de la proteína.
  • Se realizaron comparaciones estructurales con el dominio G de dinamina G de la rata.

Principales resultados:

  • La estructura cristalina reveló el estado dimérico de la proteína de fusión GTPasa-GED en presencia de GDP.AlF(4)(-).
  • La estructura aclaró la maquinaria catalítica de la dinamina y demostró la dimerización del dominio G como el mecanismo para la hidrólisis de GTP estimulada por ensamblaje.
  • Se identificó un ion de sodio en el sitio activo, lo que sugiere su papel en la estabilización del estado de transición en ausencia de un dedo de arginina.

Conclusiones:

  • El estudio proporciona una explicación estructural de cómo la dinamina logra la hidrólisis de GTP estimulada por ensamblaje a través de la dimerización del dominio G.
  • Los hallazgos destacan el papel de un catión en el sitio activo para la estabilización del estado de transición.
  • La estructura presentada ofrece una visión significativa de los mecanismos moleculares subyacentes a la fisión de la membrana mediada por dinamina.