Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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:

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...

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...

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.

MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.

bioRxiv : the preprint server for biology·2026

Same author

Negative Compressibility Transitions in Hybrid Metal Oxides.

Journal of the American Chemical Society·2025

Same author

Mechanistic Insights for Glucose-Driven Coacervation of a Supramolecular Peptide and Therapeutic Protein.

ACS applied materials & interfaces·2025

Same author

Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data.

Biophysical chemistry·2025

Same author

Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.

Nature communications·2025

Search research articles

Related Experiment Video

Updated: Jul 2, 2026

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

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

Published on: March 9, 2012

Global conformational dynamics in ras.

Casey O'Connor¹, Evgenii L Kovrigin

¹Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, Wisconsin 53226, USA.

|September 6, 2008

Summary

Ras proteins regulate cellular processes by binding GTP. This study reveals that the conformational dynamics of human H-Ras are global, impacting its entire catalytic domain and offering insights into allosteric regulation.

Area of Science:

Biochemistry
Molecular Biology
Cellular Signaling

Background:

Ras proteins, including human H-Ras, are critical regulators of cellular processes.
Ras-GTP complexes activate downstream signaling pathways.
Previous (31)P NMR studies suggested millisecond-scale conformational heterogeneity in Ras-GTP, but dynamics remain unclear.

Purpose of the Study:

To investigate the conformational dynamics of human H-Ras in complex with the GTP mimic GppNHp.
To determine the extent and nature of conformational exchange in Ras-GTP.

Main Methods:

Utilized (31)P Nuclear Magnetic Resonance ((31)P NMR) spectroscopy.
Analyzed conformational dynamics of human H-Ras complexed with GppNHp.

Main Results:

More Related Videos

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Published on: January 24, 2025

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation (BiFC-PALM)

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation (BiFC-PALM)

Published on: December 22, 2015

Related Experiment Videos

Last Updated: Jul 2, 2026

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

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

Published on: March 9, 2012

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Published on: January 24, 2025

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation (BiFC-PALM)

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation (BiFC-PALM)

Published on: December 22, 2015

Evidence presented for a global conformational exchange process in human H-Ras-GppNHp.
The conformational dynamics encompass the majority of the GTPase catalytic domain.
Conformational dynamics exhibit correlated behavior.

Conclusions:

Ras conformational dynamics are not localized but global, affecting the entire catalytic domain.
The correlated nature of these dynamics provides a framework for understanding allosteric regulation in Ras function.
This research deepens our understanding of Ras signaling mechanisms.