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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 Proteins01:14

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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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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
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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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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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Related Experiment Video

Updated: Sep 2, 2025

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
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Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

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TGFβ-induced changes in membrane curvature influence Ras oncoprotein membrane localization.

Alexandros Damalas1,2, Ivana Vonkova1,3, Marijonas Tutkus1,4,5

  • 1Department of Chemistry, University of Copenhagen, Copenhagen, Denmark.

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Transforming growth factor beta (TGFβ) induces epithelial to mesenchymal transition (EMT) by altering plasma membrane curvature, which recruits H-ras and K-ras, enhancing cancer cell invasion.

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Area of Science:

  • Cell Biology
  • Cancer Research
  • Molecular Biology

Background:

  • Cancer progression involves tumor cell morphological changes, increasing motility and invasiveness, leading to metastasis.
  • Epithelial to mesenchymal transition (EMT), triggered by transforming growth factor beta (TGFβ), is crucial for invasive potential.
  • Ras GTPases, essential for cell signaling, interact with TGFβ to drive cancer cell invasiveness.

Purpose of the Study:

  • To investigate the effect of TGFβ on the subcellular localization of H-ras and K-ras.
  • To elucidate the role of plasma membrane curvature in TGFβ-induced cancer cell invasion.

Main Methods:

  • Treatment of cancer cells with TGFβ.
  • Analysis of subcellular localization of H-ras and K-ras using microscopy.
  • Measurement of plasma membrane curvature.

Main Results:

  • TGFβ treatment increases positive plasma membrane curvature.
  • H-ras is recruited to the plasma membrane in response to increased curvature.
  • This recruitment leads to elevated H-ras activation and promotes further EMT.

Conclusions:

  • A novel positive feedback loop exists where TGFβ-induced EMT increases plasma membrane curvature, attracting Ras proteins.
  • Increased Ras activity at the plasma membrane potentiates EMT and enhances cancer cell invasiveness.
  • Targeting this feedback loop could offer new therapeutic strategies for invasive cancers.