| First Author | Weimer JM | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 330 |
| Issue | 4 | Pages | 1176-81 |
| PubMed ID | 15823567 | Mgi Jnum | J:97449 |
| Mgi Id | MGI:3575466 | Doi | 10.1016/j.bbrc.2005.03.103 |
| Citation | Weimer JM, et al. (2005) Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1. Biochem Biophys Res Commun 330(4):1176-81 |
| abstractText | 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. |
