Related Experiment Video
Updated: Nov 7, 2025
04:36
Assay for Adhesion and Agar Invasion in S. cerevisiae
Published on: November 8, 2006
15.2K
The Small GTPases in Fungal Signaling Conservation and Function
Mitzuko Dautt-Castro1, Montserrat Rosendo-Vargas1, Sergio Casas-Flores1
1Laboratorio de Genómica Funcional y Comparativa, División de Biología Molecular, IPICYT, San Luis Potosí 78216, Mexico.
Cells
|April 30, 2021
Summary
This study analyzes small GTPase families in fungi, revealing their roles in growth, metabolism, and plant interactions. These proteins are crucial for various fungal biological processes.
Area of Science:
- Molecular Biology
- Mycology
- Biochemistry
Background:
- Monomeric GTPases, part of the Ras superfamily, regulate diverse biological processes.
- They are controlled by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs).
- Key families include Ras, Rho, Rab, Ran, Arf, Miro, and the newly identified Big Ras GTPases.
Purpose of the Study:
- To conduct an exhaustive analysis of small GTPase families in fungi.
- To investigate the functions and evolutionary aspects of these GTPases in fungal species.
- To review their roles in fungal biology and interactions with plants.
Main Methods:
- Phylogenetic analysis of small GTPase families across 56 fungal genomes.
- Sequence analysis to identify conserved motifs and family-specific features.
- Comparative genomics approaches.
Main Results:
- Identification and characterization of multiple small GTPase families within the studied fungal phyla.
- Elucidation of conserved structural motifs (G1-G5) and unique family characteristics.
- Functional roles linked to morphogenesis, secondary metabolism, vesicle trafficking, and virulence were highlighted.
Conclusions:
- Small GTPases are essential regulators of fundamental biological processes in fungi.
- These proteins play significant roles in fungal development, metabolism, and pathogenicity.
- Their involvement in fungus-plant interactions warrants further investigation.
Related Concept Videos
02:14GTPases and their Regulation
9.2K
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.
Large G-proteins,...
Large G-proteins,...
9.2K
02:14GTPases and their Regulation
2.5K
2.5K
01:24Small GTPases - Ras and Rho
4.6K
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:
Three regulatory proteins control their activity:
4.6K
01:22Activation and Inactivation of G Proteins
8.4K
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...
8.4K
01:14Rab Proteins
4.5K
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...
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...
4.5K
01:25Rab Cascades
3.1K
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.
3.1K