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Lipids as Anchors

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...

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Updated: Dec 3, 2025

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Lipid headgroups alter huntingtin aggregation on membranes.

Maryssa Beasley¹, Sharon Groover¹, Stephen J Valentine¹

¹The C. Eugene Bennett Department of Chemistry, West Virginia University, 217 Clark Hall, Morgantown, WV 26506, United States.

Biochimica Et Biophysica Acta. Biomembranes

|November 1, 2020

Summary

Lipid headgroup properties significantly influence Huntington's disease protein aggregation and membrane interactions. Anionic lipids promote fibrillization, while zwitterionic lipids enhance membrane activity and protein:lipid complex formation.

Keywords:

Amyloid Atomic force microscopy Electrospray ionization-mass spectrometry Huntington's disease Lipid membranes Polyglutamine

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Huntington's disease (HD) is a fatal neurodegenerative disorder.
HD pathogenesis involves the aggregation of huntingtin protein (htt) with expanded polyglutamine (polyQ) regions.
The N-terminal 17 amino acids (Nt17) of htt are crucial for membrane binding and initiating aggregation.

Purpose of the Study:

To investigate how lipid headgroup properties affect htt-exon1 aggregation.
To determine the impact of lipid headgroups on htt membrane activity and protein:lipid complex formation.

Main Methods:

Exposing htt-exon1 (46Q) to lipid vesicles with zwitterionic (POPC, POPE) or anionic (POPG, POPS) headgroups.
Analyzing htt aggregation, fibrillization, membrane activity, and protein:lipid complex formation.

Main Results:

Anionic lipids enhanced htt fibrillization at low lipid:protein ratios, altering aggregate morphology.
Zwitterionic lipids required higher lipid:protein ratios for significant aggregation impact but increased htt-exon1 membrane activity.
Lipid headgroups mediated Nt17 complex formation, with zwitterionic lipids favoring association with multimeric Nt17.

Conclusions:

Lipid headgroup charge critically influences htt aggregation pathways and membrane interactions in HD.
Understanding these htt/membrane interactions is key to deciphering HD pathogenesis and developing therapeutic strategies.