Related Experiment Video
Updated: May 21, 2026

13:51
Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Published on: November 11, 2018
A big new job for small GTPases
1Instituto de Neurociencias, CSIC/UMH, 03550-Sant Joan d'Alacant, Alicante, Spain. acarmena@umh.es
Small Gtpases
|June 1, 2012
Summary
Small guanosine triphosphatases (GTPases) like Rap1 and Ral are crucial for cell division. These Ras superfamily proteins regulate cell polarity and spindle orientation in Drosophila neuroblast division.
Area of Science:
- Cell Biology
- Molecular Biology
- Developmental Biology
Background:
- Ras superfamily small guanosine triphosphatases (GTPases) are central regulators of diverse cellular processes.
- Cellular signaling networks rely on GTPases for functions such as proliferation, differentiation, and apoptosis.
- Cortical polarity and spindle orientation are critical for asymmetric cell division.
Purpose of the Study:
- To investigate the role of Ras-like small GTPases Rap1 and Ral in asymmetric neuroblast division.
- To elucidate the mechanisms by which Rap1 and Ral regulate cortical polarity and spindle orientation.
- To determine if the role of these GTPases in cell polarization is evolutionarily conserved.
Main Methods:
- Utilized Drosophila melanogaster as a model organism for studying neuroblast division.
- Employed genetic and molecular techniques to manipulate Rap1 and Ral activity.
- Observed and quantified cortical polarity and spindle orientation during cell division.
Main Results:
- Rap1 and Ral were found to play a novel role in regulating cortical polarity.
- These GTPases are essential for proper spindle orientation during asymmetric neuroblast division.
- Evidence suggests a conserved role for Rap1 and Ral in promoting cell polarization across species.
Conclusions:
- Rap1 and Ral are key regulators of asymmetric cell division in Drosophila neuroblasts.
- The findings highlight a conserved function of Ras-like GTPases in establishing cell polarity.
- This study expands the understanding of GTPase signaling in developmental processes.
Related Concept Videos
Small GTPases - Ras and Rho
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:
GTPases and their Regulation
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, also known...
Large G-proteins, also known...
GTPases and their Regulation
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, also known...
Large G-proteins, also known...
Coat Assembly and GTPases
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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Activation and Inactivation of G Proteins
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 affinity and are together...
Rab Cascades
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.

