Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1.

Hook1 is a member of a family of microtubule-binding proteins. Studies on the Drosophila homolog of Hook1 have suggested a role in the maturation and trafficking of internalized proteins to the late endosome. A weak interaction between Hook1 and the lysosomal/late endosomal protein, CLN3, was recently reported. Mutations in CLN3 ...
result in the neurological disorder Batten disease. Here we show a novel interaction between Hook1 and Ankyrin G, an adaptor protein that binds the spectrin-actin cytoskeleton and targets proteins to the peripheral membrane. Although we demonstrate co-localization of Hook1 and Ankyrin G, Hook1 also localizes to additional regions of the cell devoid of Ankyrin G where it likely interacts with other proteins. There is no disruption of the Hook1-Ankyrin G interaction or localization in tissue derived from a Cln3-knockout mouse despite a nearly threefold increase in the expression of Hook1. However, mutation of CLN3 could lead to alterations in the functioning and positioning of organelles and membrane proteins through this Hook1-Ankyrin G interaction.
Mesh Terms:
Animals, Ankyrins, Humans, Membrane Glycoproteins, Mice, Mice, Knockout, Microtubule-Associated Proteins, Molecular Chaperones, Mutation, Neuronal Ceroid-Lipofuscinoses, Optic Nerve, RNA, Messenger, Two-Hybrid System Techniques
Biochem. Biophys. Res. Commun.
Date: May. 20, 2005
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