Year: 2015
Type: article
Abstract: In the past two decades, the Hedgehog (HH) family of secreted proteins has been demonstrated to play an essential role in both animal development and various human diseases [1]. Sonic Hedgehog (SHH) is the most extensively studied HH protein biochemically. Fully processed SHH (SHH-Np) was previously reported to be post-translationally modified by cholesterol at its carboxyl terminus and palmitic acid at its amino terminus. This dual lipid modification was shown to dictate the biological functions of SHH, including its potency, intracellular trafficking and ability to move far from its site of synthesis. However, our recent work suggests a novel addition to this well-established model, by identifying a family of lipid speciated SHH proteins that are modified at their amino termini not only by palmitic acid, but by a
Source: Oncotarget
Authors: Jun Long, Emily Winterbottom, David J. Robbins
Institution: University of Miami
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
OpenAlex ID: W2169558223