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

TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
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...
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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...
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

Atmospheric emissions of microplastics entrained with dust from potential source regions.

Journal of hazardous materials·2025
Same author

Atmospheric Deposition of Microplastics in South Central Appalachia in the United States.

ACS ES&T air·2025
Same author

Efficacy of prebiotic, probiotic, and synbiotics in improving growth in children under age five years in Africa: A protocol for a systematic review.

Nutrition and health·2024
Same author

Reproductive factors and mammographic density within the International Consortium of Mammographic Density: A cross-sectional study.

Breast cancer research : BCR·2024
Same author

Microplastics and nanoplastics pose risks on the Tibetan Plateau environment.

Science bulletin·2023
Same author

Somatic mutations of CADM1 in aldosterone-producing adenomas and gap junction-dependent regulation of aldosterone production.

Nature genetics·2023

Related Experiment Video

Updated: Jul 11, 2026

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates
11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates

Published on: March 31, 2012

FGF mediated Sulf1 regulation.

Wanfeng Zhao1, Steve Allen, Gurtej K Dhoot

  • 1Department of Basic Sciences, The Royal Veterinary College, University of London, Royal College Street, London NW1 OTU, UK.

FEBS Letters
|October 2, 2007
PubMed
Summary
This summary is machine-generated.

Fibroblast growth factor 4 (FGF4) regulates Sulf1 during embryonic limb development. FGF4 influences cell death and digit formation, with Sulf1 acting as a key mediator in these processes.

Related Experiment Videos

Last Updated: Jul 11, 2026

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates
11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates

Published on: March 31, 2012

Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Signaling Pathways

Background:

  • Fibroblast Growth Factor (FGF) signaling is essential for embryonic development.
  • Sulf1 is known to antagonize FGF activity.
  • The specific role of FGF4 in Sulf1 regulation during limb development requires further elucidation.

Purpose of the Study:

  • To investigate the regulatory role of FGF4 on Sulf1 expression during quail autopod (limb bud) development.
  • To understand how FGF4 affects apoptosis and digit formation in relation to Sulf1.

Main Methods:

  • Implantation of FGF4-soaked beads into quail embryonic limb buds (interdigit and digit tip).
  • Micromass cultures to assess Sulf1 regulation in vitro.
  • Administration of FGF inhibitor SU5402 to examine its effects on Sulf1 expression and digit development.

Main Results:

  • FGF4 beads differentially upregulated Sulf1 expression in both interdigital and digital tip regions.
  • FGF4 demonstrated a concentration-dependent inhibition of apoptosis in the interdigital mesoderm.
  • The FGF inhibitor SU5402 suppressed Sulf1 expression in the interdigit but induced ectopic Sulf1 expression and inhibited phalange formation at the digital tip.

Conclusions:

  • FGF4 plays a significant role in regulating Sulf1 expression during embryonic limb development.
  • Sulf1 is implicated in mediating FGF4's effects on interdigital apoptosis and digit formation.
  • The precise localization of FGF signaling and Sulf1 activity is critical for normal phalange development.