Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

GTPases and their Regulation02:14

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...
GTPases and their Regulation02:14

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...
Rab Cascades01:25

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.
Small GTPases - Ras and Rho01:24

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:
Activation and Inactivation of G Proteins01:22

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...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...

You might also read

Related Articles

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

Sort by
Same author

Bone marrow immunosuppressive states associate with survival after guadecitabine and atezolizumab therapy in HMA-R/R MDS.

Blood neoplasia·2026
Same author

Consensus Pituitary Atlas, a scalable resource for annotation, novel marker discovery, and analyses in mouse pituitary gland research.

Cell reports·2026
Same author

Multi-Omic, Multi-Tissue Responses to Acute Exercise in Sedentary Adults: Findings from the Molecular Transducers of Physical Activity Consortium.

bioRxiv : the preprint server for biology·2026
Same author

The long non-coding RNA landscape of endurance exercise training.

Molecular metabolism·2026
Same author

Multi-omic responses to acute exercise in abdominal subcutaneous adipose tissue of sedentary adults: findings from MoTrPAC.

bioRxiv : the preprint server for biology·2026
Same author

Molecular Transducers of Physical Activity Consortium (MoTrPAC): Initial Insights into the Dynamic Human Responses to Exercise.

bioRxiv : the preprint server for biology·2026
Same journal

Erratum for Yamamoto et al., Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from <i>Chlamydomonas</i> to Mammals.

Eukaryotic cell·2017
Same journal

Correction for Liang et al., A Novel Function for Hog1 Stress-Activated Protein Kinase in Controlling White-Opaque Switching and Mating in Candida albicans.

Eukaryotic cell·2016
Same journal

Retraction for Chavez-Dozal et al. Functional Analysis of the Exocyst Subunit Sec15 in Candida albicans.

Eukaryotic cell·2016
Same journal

Retraction for Chavez-Dozal et al., The Candida albicans Exocyst Subunit Sec6 Contributes to Cell Wall Integrity and Is a Determinant of Hyphal Branching.

Eukaryotic cell·2016
Same journal

The New Shape of EC.

Eukaryotic cell·2015
Same journal

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

Eukaryotic cell·2015
See all related articles

Related Experiment Video

Updated: Jun 7, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

GTPase-activating proteins for Cdc42.

Gregory R Smith1, Scott A Givan, Paul Cullen

  • 1Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229, USA.

Eukaryotic Cell
|November 29, 2002
PubMed
Summary
This summary is machine-generated.

Researchers identified and confirmed Rga1, Rga2, and Bem3 as GTPase-activating proteins (GAPs) for Cdc42 in yeast. These GAPs regulate distinct Cdc42 functions, impacting cellular processes like invasive growth and septin organization.

More Related Videos

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Related Experiment Videos

Last Updated: Jun 7, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cdc42, a Rho-type GTPase, is crucial for yeast cell functions including cytokinesis, pheromone response, and invasive growth.
  • GTPase-activating proteins (GAPs) inactivate Cdc42 by promoting GTP hydrolysis.
  • Prior to this study, only Bem3 was a known Cdc42 GAP, with Rga1 identified as a putative GAP.

Purpose of the Study:

  • To identify and characterize novel GTPase-activating proteins (GAPs) for Cdc42 in yeast.
  • To elucidate the specific roles of Rga1, Rga2, and Bem3 in regulating Cdc42-dependent cellular processes.
  • To investigate the functional distinctions between these GAPs in yeast.

Main Methods:

  • Genetic analysis involving gene deletions and overproduction.
  • Biochemical assays to confirm GTPase-activating protein activity.
  • Yeast two-hybrid assays to study protein interactions.

Main Results:

  • Rga1, Rga2, and Bem3 were confirmed as functional GAPs for Cdc42.
  • Deletion mutants exhibited distinct phenotypes: rga1Δ caused hyperinvasive growth, while BEM3 deletion led to severe morphological defects.
  • Rga1 and Rga2, but not Bem3, influenced the Cdc42-Ste20 interaction, suggesting a role in the invasive growth pathway.
  • Bem3, Rga1, and Rga2 were implicated in Cdc42's role in septin organization.

Conclusions:

  • The identified GAPs (Rga1, Rga2, Bem3) differentially regulate Cdc42 functions.
  • Rga1 and Rga2 appear to mediate Cdc42 signaling in haploid invasive growth via interaction with Ste20.
  • Bem3 plays a critical role in septin organization, with Rga1 and Rga2 having a lesser contribution.
  • These findings highlight the specific roles of GAPs in modulating distinct aspects of Cdc42 activity.