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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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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,...
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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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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...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Related Experiment Video

Updated: Aug 23, 2025

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
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Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

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G3BP2: Structure and function.

Ge Jin1, Zhen Zhang2, Jingjing Wan2

  • 1School of Pharmacy, Second Military Medical University, Shanghai, China; School of Pharmacy, Henan University, Kaifeng, China.

Pharmacological Research
|November 6, 2022
PubMed
Summary
This summary is machine-generated.

Ras-GAP SH3 domain binding protein 2 (G3BP2) is an RNA-binding protein involved in cell functions and disease. This review explores G3BP2

Keywords:
G3BP2NFκBRNA bindingStress granulesSubcellular locationTumor

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Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
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Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Ras-GAP SH3 domain binding proteins (G3BPs) are crucial RNA-binding proteins, with G3BP1 and G3BP2 being prominent in mammals.
  • G3BP2's structure facilitates RNA and protein binding, regulating nucleoplasmic transport and impacting cell growth, differentiation, migration, and metabolism.
  • Abnormal G3BP2 expression is linked to various pathologies, including breast, lung, and prostate cancers, cardiac hypertrophy, and atherosclerosis, highlighting its potential as a therapeutic target.

Purpose of the Study:

  • To review the structure and expression regulation of G3BP2.
  • To summarize the multifaceted functions of G3BP2 in biological processes.
  • To elucidate the role of G3BP2 in RNA stabilization, protein subcellular localization, and stress granule assembly.

Main Methods:

  • Literature review of existing research on G3BP2.
  • Analysis of studies investigating G3BP2 structure and expression.
  • Synthesis of findings on G3BP2's functional roles.

Main Results:

  • G3BP2 possesses a versatile structure enabling interactions with RNA and proteins.
  • G3BP2 plays a significant role in regulating RNA and protein metabolism and cellular localization.
  • G3BP2 is implicated in the formation of stress granules, key components of cellular stress response.

Conclusions:

  • G3BP2 is a critical protein with diverse functions in cellular processes.
  • Dysregulation of G3BP2 is associated with numerous diseases, underscoring its clinical relevance.
  • Further understanding of G3BP2 mechanisms may lead to novel therapeutic strategies.