Jove
Visualize
Contact Us

Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

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...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

You might also read

Related Articles

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

Sort by
Same author

Atomic-level architecture and assembly mechanism of high-order structures of RIPK1 fibril revealed by integrated structural biology.

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

Correlating Protein Dynamics and Catalytic Activity of a Model Hydrogenase Using Paramagnetic and Biological Nuclear Magnetic Resonance Spectroscopy.

Journal of the American Chemical Society·2026
Same author

A Perspective on Quantum Computing Applications in Quantum Chemistry Using 25-100 Logical Qubits.

Journal of chemical theory and computation·2025
Same author

Diverse Bone Matrix and Mineral Alterations in Osteoporosis with Different Causes: A Solid-State NMR Study.

ACS biomaterials science & engineering·2025
Same author

A molecular view of peptoid-induced acceleration of calcite growth.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Understanding the role of negative charge in the scaffold of an artificial enzyme for CO<sub>2</sub> hydrogenation on catalysis.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2024
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 Experiment Video

Updated: May 13, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.

Jun-xia Lu1, Yimin Sharon Xu, Wendy J Shaw

  • 1Pacific Northwest National Laboratory, Richland, WA 99354, USA.

Biochemistry
|March 13, 2013
PubMed
Summary
This summary is machine-generated.

This study reveals how amelogenin (LRAP) interacts with hydroxyapatite (HAP) under changing pH and ionic strength conditions during enamel development. Phosphorylation significantly alters LRAP’s structure and interaction with HAP, suggesting a regulatory role.

More Related Videos

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Related Experiment Videos

Last Updated: May 13, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Area of Science:

  • Biomineralization
  • Protein-mineral interactions
  • Enamel formation

Background:

  • Enamel crystallite development is influenced by dynamic conditions like pH and ionic strength.
  • Amelogenin (LRAP) plays a crucial role in regulating hydroxyapatite (HAP) formation.
  • Understanding LRAP-HAP interactions is key to comprehending enamel structure and development.

Purpose of the Study:

  • To investigate the impact of pH and ionic strength on the interaction between amelogenin (LRAP) and hydroxyapatite (HAP).
  • To examine how phosphorylation affects the structure, orientation, and dynamics of LRAP's N-terminus interacting with HAP.
  • To elucidate the molecular mechanisms governing LRAP's role in enamel biomineralization.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) techniques, including REDOR dipolar recoupling and chemical shift analysis.
  • Investigation of three specific N-terminal regions of LRAP (L15-V19, V19-L23, K24-S28).
  • Comparative analysis of phosphorylated (LRAP(+P)) and unphosphorylated (LRAP(-P)) forms of LRAP under varying solution conditions.

Main Results:

  • LRAP regions studied exhibited restricted motion, with some increased mobility noted for L15(+P) and K24(-P).
  • The N-terminus of phosphorylated LRAP (LRAP(+P)) demonstrated remarkable stability in structure and orientation across different pH and ionic strengths.
  • Phosphorylation induced significant structural changes, including a shift from random coil to helical structure in K24-S28 and an extended conformation in V19-L23 at high ionic strength.

Conclusions:

  • The N-terminus of phosphorylated LRAP is highly stable, suggesting robust interactions during enamel development.
  • Changes in ionic strength and dephosphorylation may act as critical switches modulating LRAP's function.
  • These findings provide insights into the dynamic regulation of mineral development in tooth enamel.