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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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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.
Three regulatory proteins control their activity:
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The Ras Gene02:38

The Ras Gene

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The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a...
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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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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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MAPK Signaling Cascades01:07

MAPK Signaling Cascades

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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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Cell Polarization by Rho Proteins

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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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Complex interplay between RAS GTPases and RASSF effectors regulates subcellular localization of YAP.

Swati Singh1, Gabriela Bernal Astrain1, Ana Maria Hincapie2

  • 1Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC, H3T 1J4, Canada.

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|July 15, 2024
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Summary
This summary is machine-generated.

This study maps interactions between BRAF, RASSF proteins, and small GTPases, revealing new effector functions and signaling pathways. The research uncovers novel roles for RASSF proteins in cellular processes like Hippo signaling and mitochondrial dynamics.

Keywords:
Hippo PathwayMIRORAS GTPaseRASSFYAP

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • RAS GTPases are key regulators of cellular functions, translating upstream signals into downstream responses.
  • Effectors typically bind GTP-bound GTPases via specific domains like RBD/RA, but their specificity across the large RAS superfamily is not well understood.

Purpose of the Study:

  • To systematically map interactions between BRAF, RASSF effectors, and various small GTPases (RAS, RHO, ARF).
  • To explore the specificity of these interactions and uncover novel biological functions.
  • To investigate the roles of RASSF proteins in cellular signaling and organelle dynamics.

Main Methods:

  • Systematic mapping of protein-protein interactions.
  • Biochemical assays to validate GTPase-effector complexes.
  • Cellular assays to assess signaling pathway activation and organelle distribution.

Main Results:

  • 39 validated GTPase-effector complexes were identified, showing plasticity in RASSF binding.
  • BRAF exhibited specific binding to classical H/K/NRAS GTPases.
  • RASSF5-RAS interactions activated Hippo signaling and YAP sequestration.
  • RASSF8 formed phase-separated condensates with RAS and RHO GTPases.
  • RASSF3 was identified as a potential effector of mitochondrial MIRO proteins, influencing organelle distribution.

Conclusions:

  • Systematic mapping of GTPase-effector interactions reveals complex binding patterns and novel biological functions.
  • RASSF proteins play diverse roles, including regulating signaling pathways and organelle dynamics.
  • This approach can uncover previously unknown cellular processes mediated by GTPase-effector networks.