Related Experiment Video
Updated: May 30, 2026

10:27
Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
Published on: March 9, 2012
Rab8 GTPase as a regulator of cell shape
1Institute of Biotechnology, University of Helsinki, Finland. johan.peranen@helsinki.fi
Cytoskeleton (Hoboken, N.J.)
|August 19, 2011
Summary
Rab8 protein is crucial for forming dynamic cell structures and influences cell migration and differentiation. Its regulation impacts membrane recycling and the creation of new cell surface domains.
Area of Science:
- Cell Biology
- Molecular Biology
Background:
- Rab8 is a GTPase found in dynamic cellular structures like filopodia and primary cilia.
- Rab8 activation correlates with the formation of actin-rich structures, while inhibition impairs their development.
Purpose of the Study:
- To review the multifaceted roles of Rab8 in cellular processes.
- To elucidate Rab8's involvement in cell migration, epithelial polarization, neuron differentiation, and ciliogenesis.
Main Methods:
- This review synthesizes existing research on Rab8 function.
- Focuses on regulatory mechanisms involving guanine nucleotide exchange factors and GTPase activating proteins.
- Examines Rab8's interactions within membrane trafficking pathways.
Main Results:
- Rab8 activity is essential for the formation and maintenance of cellular protrusions and ruffles.
- Rab8 participates in a membrane recycling pathway involving Arf6, EHD1, Myo5, and Rab11.
- A hypothesis regarding Rab8's role in novel cell surface domain formation is presented.
Conclusions:
- Rab8 is a key regulator of cell shape, migration, and differentiation.
- Understanding Rab8's regulatory network is vital for comprehending fundamental cell biology.
- Further research into Rab8's role in ciliogenesis and polarization is warranted.
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...
Rab Proteins
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...
Mechanism of Lamellipodia Formation
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Negative Regulator Molecules
Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.

