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Huntingtin associates with acidic phospholipids at the plasma membrane


Huntingtin associates with acidic phospholipids at the plasma membrane



Journal of Biological Chemistry 280(43): 36464-36473



ISSN/ISBN: 0021-9258

PMID: 16085648

DOI: 10.1074/jbc.m503672200

We have identified a domain in the N terminus of huntingtin that binds to membranes. A three-dimensional homology model of the structure of the binding domain predicts helical HEAT repeats, which emanate a positive electrostatic potential, consistent with a charge-based mechanism for membrane association. An amphipathic helix capable of inserting into pure lipid bilayers may serve to anchor huntingtin to the membrane. In cells, N-terminal huntingtin fragments targeted to regions of plasma membrane enriched in phosphatidylinositol 4,5-bisphosphate, receptor bound-transferrin, and endogenous huntingtin. N-terminal huntingtin fragments with an expanded polyglutamine tract aberrantly localized to intracellular regions instead of plasma membrane. Our data support a new model in which huntingtin directly binds membranes through electrostatic interactions with acidic phospholipids.

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Accession: 013137540

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