Hedgehog lipid modifications are required for Hedgehog stabilization in the extracellular matrix
Related Experiment Video
Updated: Aug 13, 2026

Quantitative PCR-based Assay to Measure Sonic Hedgehog Signaling in Cellular Model of Ciliogenesis
Published on: January 31, 2025
Ainhoa Callejo1, Carlos Torroja, Luis Quijada
1Centro de Biología Molecular Severo Ochoa, CSIC, Universidad Autónoma de Madrid, Cantoblanco, Spain.
Abstract:
The Hedgehog (Hh) family of morphogenetic proteins has important instructional roles in metazoan development. Despite Hh being modified by Ct-cholesterol and Nt-palmitate adducts, Hh migrates far from its site of synthesis and programs cellular outcomes, depending on its local concentrations. We show that in the receiving cells of the Drosophila wing imaginal disc, lipid-unmodified Hh spreads across many more cell diameters than the wild type and this spreading leads to the activation of low but not high threshold responses. Unlipidated Hh forms become internalized through the apical plasma membrane, while wild-type Hh enters through the basolateral cell surface - in all cases via a dynamin-dependent mechanism. Full activation of the Hh pathway and the spread of Hh throughout the extracellular matrix depend on the ability of lipid-modified Hh to interact with heparan sulfate proteoglycans (HSPG). However, neither Hh-lipid modifications nor HSPG function are required to activate the targets that respond to low levels of Hh. All these data show that the interaction of lipid-modified Hh with HSPG is important both for precise Hh spreading through the epithelium surface and for correct Hh reception.
More Related Videos
12:04A High-throughput Cell Microarray Platform for Correlative Analysis of Cell Differentiation and Traction Forces
Published on: March 1, 2017
07:49Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
Published on: January 22, 2019
Related Concept Videos
Hedgehog Signaling Pathway
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Mechanism of Lamellipodia Formation
Regulation of Angiogenesis and Blood Supply
Asymmetric Lipid Bilayer
Anchoring Junctions