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Rab Proteins

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 Cascades

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.

The Ras Gene

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...

The Ras Gene

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...

Small GTPases - Ras and Rho

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:

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Related Experiment Video

Updated: Jul 19, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

Lipidated ras and rab peptides and proteins--synthesis, structure, and function.

Luc Brunsveld¹, Jürgen Kuhlmann, Kirill Alexandrov

¹Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Str. 11, 44227 Dortmund, Germany.

Angewandte Chemie (International Ed. in English)

|October 13, 2006

Summary

Chemical biology uses chemistry to investigate biological processes. Researchers developed new synthetic methods for lipidated peptides, enabling studies of Ras-superfamily GTPases previously impossible with traditional techniques.

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Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

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Cell-Free Production of Proteoliposomes for Functional Analysis and Antibody Development Targeting Membrane Proteins

Cell-Free Production of Proteoliposomes for Functional Analysis and Antibody Development Targeting Membrane Proteins

Published on: September 22, 2020

Area of Science:

Chemical biology
Biochemistry
Synthetic chemistry

Background:

Chemical biology integrates chemistry and biology to address biological questions.
Unsolved problems in biology can be tackled by analyzing biological phenomena and their chemical structures.
New synthetic strategies are crucial for developing chemical tools to probe biological systems.

Purpose of the Study:

To develop novel synthetic methodologies for creating complex biomolecules.
To apply these methods to investigate the Ras-superfamily GTPases.
To overcome limitations of traditional chemical and biological techniques in studying these proteins.

Main Methods:

Solid-phase synthesis for lipidated peptides.
Chemoselective ligation techniques.
Application of synthesized peptides and proteins to study Ras-superfamily GTPases.

Main Results:

Successful synthesis of lipidated peptides using solid-phase synthesis.
Chemoselective ligation of synthesized peptides to Ras-superfamily proteins.
Resolution of biological questions concerning Ras-superfamily GTPases.

Conclusions:

Solid-phase synthesis is effective for creating lipidated peptides for biological studies.
The developed chemical approach provides novel insights into Ras-superfamily GTPase function.
This interdisciplinary strategy advances the study of complex biological systems.