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Article

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

Biochemical and biophysical research communications - 20 May 2005

Weimer Jill M, Chattopadhyay Subrata, Custer Andrew W, Pearce David A

Abstract excerpt

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...

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Source

Identifiers

PMID: 15823567
DOI: 10.1016/j.bbrc.2005.03.103

Genes

CLN3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1.PMID 15823567Read ↗

Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathwaySemantic proximity Read ↗

Loss of the lysosomal protein CLN3 modifies the lipid content of the nuclear envelope leading to DNA damage and activation of YAP1 pro-apoptotic signalingSemantic proximity Read ↗

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Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathwaysSemantic proximity Read ↗

Genetic analysis of hook, a gene required for endocytic trafficking in drosophila.Semantic proximity Read ↗

Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons.Semantic proximity Read ↗

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