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Related Concept Videos

Rab Proteins01:14

Rab Proteins

3.9K
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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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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Updated: Jun 16, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Capturing RAS oligomerization on a membrane.

Sangho D Yun1, Elena Scott1, Jing-Yuan Chang1

  • 1Department of Chemistry, Texas A&M University, College Station, TX 77843.

Proceedings of the National Academy of Sciences of the United States of America
|August 15, 2024
PubMed
Summary
This summary is machine-generated.

RAS GTPases form dimers on cell membranes when active, a process influenced by lipids and palmitoylation. This dimerization is key to regulating cell growth and offers a potential therapeutic target.

Keywords:
RAScancermass spectrometryperipheral membrane protein

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Biochemistry

Background:

  • RAS GTPases are crucial molecular switches regulating cell growth by associating with cell membranes.
  • RAS protein oligomerization on membranes is a recent finding, suggesting it as a therapeutic target.
  • Conflicting reports on RAS assembly size necessitate clarification of stoichiometry and regulatory factors.

Purpose of the Study:

  • To investigate the stoichiometry and influencing parameters of RAS protein oligomerization on membranes.
  • To analyze three RAS isoforms (KRAS, HRAS, NRAS) directly from membranes.
  • To understand how nucleotides, lipids, and palmitoylation affect RAS assembly and activity.

Main Methods:

  • Mass spectrometry was used to analyze RAS isoforms (KRAS, HRAS, NRAS) directly from cell membranes.
  • Intrinsic GTPase activity was monitored to observe RAS dimerization dynamics.
  • The effect of small molecule BI2852 and effector protein Son of Sevenless (SOScat) on RAS was assessed.

Main Results:

  • Inactive (GDP-bound) KRAS is monomeric on membranes, while active (GTP-bound) KRAS forms dimers.
  • The small molecule BI2852 induces KRAS dimerization; effector protein binding disrupts it.
  • RAS dimerization depends on lipid composition, and NRAS oligomerization is regulated by palmitoylation.

Conclusions:

  • RAS assembly stoichiometry on membranes is revealed, with dimers forming upon activation.
  • Nucleotide-bound state, lipid composition, and palmitoylation critically regulate RAS oligomerization.
  • Understanding these factors provides insights into RAS signaling and potential therapeutic strategies.