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Related Concept Videos

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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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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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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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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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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Updated: Feb 14, 2026

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

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Insight into the Interactions Between GhXI-K and Rab GTPases in Cotton Fiber.

Xinyu Li1,2, Bingke Hao1, Junwen Li1

  • 1State Key Laboratory of Cotton Bio-Breeding and Integrated Utilization, Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang 455099, China.

Plants (Basel, Switzerland)
|February 13, 2026
PubMed
Summary
This summary is machine-generated.

Myosin XI-K interacts with Rab GTPases in cotton fibers, utilizing both motor and tail domains. This interaction is crucial for vesicle trafficking and polarized growth in cotton fiber cells.

Keywords:
Rab GTPasescell growth proteincottonmyosin XI-Kpolarized growth

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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
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Area of Science:

  • Plant Cell Biology
  • Molecular Plant Science
  • Cotton Fiber Development

Background:

  • Myosin XI-K is a motor protein essential for cell expansion and polarized growth.
  • It drives organelle trafficking and cytoplasmic streaming in plant cells.
  • Understanding its role in cotton fiber development is key to improving crop yield.

Purpose of the Study:

  • To investigate the molecular mechanisms of myosin XI-K in cotton fiber polarized growth.
  • To elucidate the interactions between GhXI-K (cotton myosin XI-K) and Rab GTPases.
  • To identify specific interaction sites and domains involved in GhXI-K function.

Main Methods:

  • Protein docking analysis using AlphaFold3 to predict interactions.
  • Identification of interaction residues in GhXI-K and Rab GTPases.
  • Experimental validation using yeast two-hybrid and bimolecular fluorescence complementation (BiFC) assays.

Main Results:

  • AlphaFold3 predicted interactions between GhXI-K and eight Rab GTPases.
  • Identified 37 interaction residues in GhXI-K, with key sites in the globular tail domain (GTD) and motor domain.
  • Yeast two-hybrid and BiFC assays confirmed interactions, primarily involving the GTD and motor domain.

Conclusions:

  • GhXI-K interacts with Rab GTPases through its motor and tail domains.
  • These interactions suggest a synergistic mechanism for polarized vesicle trafficking.
  • The findings provide insights into the regulation of cotton fiber cell expansion and growth.