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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

10.1K
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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Small GTPases - Ras and Rho01:24

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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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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.
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Activation and Inactivation of G Proteins01:22

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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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Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Rab GTPases and cell division.

Paulius Gibieža1, Rytis Prekeris2

  • 1a Institute of Cardiology, Lithuanian University of Health Sciences , Kaunas , Lithuania.

Small Gtpases
|May 5, 2017
PubMed
Summary
This summary is machine-generated.

Rab GTPases regulate cell division by coordinating cytoskeleton and membrane trafficking during cytokinesis. These small proteins are crucial for the final separation of daughter cells, known as abscission.

Keywords:
Rab GTPasesabscissioncell polaritycytokinesisendosomes

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Cytokinesis, the physical separation of two daughter cells, requires coordinated cytoskeleton and membrane trafficking.
  • Rab GTPases are small proteins regulating diverse cellular functions, notably membrane transport.

Purpose of the Study:

  • To review the latest findings on Rab GTPase function in cell division.
  • To highlight the role of polarized membrane transport during cytokinesis and abscission.

Main Methods:

  • Literature review of recent studies on Rab GTPases and cytokinesis.
  • Analysis of the role of membrane trafficking pathways in cell division.

Main Results:

  • Rab GTPases are key regulators of membrane transport steps essential for cytokinesis.
  • Specific Rab GTPases have been identified to control cell division progression and abscission.

Conclusions:

  • Rab GTPases and polarized membrane transport are critical for successful cytokinesis.
  • Further research into Rab GTPase functions can elucidate mechanisms of cell division and abscission.