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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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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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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.
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GTPases and their Regulation02:14

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Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
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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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RAS GTPase signalling to alternative effector pathways.

Swati Singh1, Matthew J Smith1,2

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

Biochemical Society Transactions
|October 30, 2020
PubMed
Summary
This summary is machine-generated.

RAS GTPases drive cancer by signaling through effectors like RAF and PI3K. Exploring alternative RAS effectors, such as RALGEFs, RASSF5, and AFDN, may overcome drug resistance in cancer treatment.

Keywords:
AFDNGTPasesRALGEFRASRASSFeffector

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

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • RAS GTPases are crucial for cell development and are frequently mutated in human cancers.
  • RAS oncoproteins promote cancer initiation, progression, and metastasis through constitutive downstream signaling.
  • Current therapies targeting RAF and PI3K pathways are limited by acquired drug resistance.

Purpose of the Study:

  • To explore alternative RAS effector pathways beyond RAF and PI3K.
  • To investigate the biological significance of candidate alternative effectors: RALGEFs, RASSF5, and AFDN.
  • To identify potential new therapeutic targets for RAS-driven cancers.

Main Methods:

  • Review of existing literature on RAS GTPase signaling and effector interactions.
  • Analysis of the roles of RALGEFs, RASSF5, and AFDN in RAS-mediated cellular processes.
  • Discussion of the implications for cancer therapy.

Main Results:

  • RAS GTPases interact with a diverse range of alternative effectors.
  • RALGEFs, RASSF5, and AFDN are identified as key alternative effectors with unexplored roles.
  • These alternative pathways are implicated in cell adhesion, polarity, size, and cytoskeletal organization.

Conclusions:

  • Alternative RAS effector pathways represent promising targets for overcoming drug resistance in RAS-driven cancers.
  • Targeting RALGEFs, RASSF5, and AFDN could offer novel combinatorial therapeutic strategies.
  • Further research into these pathways is warranted given their role in cancer metastasis.