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Related Concept Videos

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.
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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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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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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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Rab Cascades01:25

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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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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Lipid Profiles of RAS Nanoclusters Regulate RAS Function.

Yong Zhou1, John F Hancock1

  • 1Department of Integrative Biology and Pharmacology, University of Texas Health Science Center, Houston, TX 77030, USA.

Biomolecules
|October 23, 2021
PubMed
Summary
This summary is machine-generated.

RAS (Rat sarcoma) proteins are key in cancer, often gathering in plasma membrane nanoclusters. This review explores how specific lipids within these nanoclusters influence RAS signaling and cancer, and how targeting these lipid interactions may offer new therapeutic strategies.

Keywords:
RASlipid acyl chainnanoclustersphosphatidylserinephospholipidsplasma membrane

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Cancer Research

Background:

  • RAS (Rat sarcoma) small GTPases are crucial in human cancer, frequently localized to plasma membrane nanoclusters.
  • Targeting RAS enzymatic activity is challenging; understanding its localization and lipid interactions is vital.
  • RAS nanoclusters act as signaling platforms, with lipids playing a key structural and functional role.

Purpose of the Study:

  • To review current knowledge on the specific lipid composition of RAS nanoclusters.
  • To elucidate the mechanisms of selective lipid sorting within RAS nanoclusters on the plasma membrane.
  • To explore how modulating these lipid compositions impacts RAS function, oncogenesis, and potential therapeutic strategies.

Main Methods:

  • Quantitative super-resolution imaging techniques to characterize RAS/lipid interactions.
  • Molecular dynamic simulations to analyze lipid-protein interactions at the nanoscale.
  • Review of existing literature on lipidomics and RAS signaling pathways.

Main Results:

  • RAS nanoclusters exhibit selective enrichment of specific lipids, characterized by distinct headgroups and acyl chains.
  • Specific mechanisms governing the sorting of these lipids into RAS nanoclusters have been identified.
  • Perturbing the lipid composition within RAS nanoclusters demonstrably affects RAS signaling and associated pathologies.

Conclusions:

  • The lipid environment of RAS nanoclusters is critical for RAS function and oncogenic potential.
  • Targeting the selective lipid sorting and composition within RAS nanoclusters presents a promising therapeutic avenue.
  • Further research into RAS/lipid interactions can unlock novel strategies for cancer treatment.