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The SH3, HOOK and guanylate kinase‐like domains of hDLG are important for its cytoplasmic localization by Kazuyoshi Kohu; Fumiaki Ogawa; Tetsu Akiyama is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract **Background:** hDLG, the human homologue of the __Drosophila__ tumour suppressor __dlg__, functions as a scaffolding protein that facilitates the transmission of diverse downstream signals. hDLG possesses multiple protein‐binding domains, including three PDZ domains, an SH3 domain, a HOOK domain and a guanylate kinase‐like (GK) domain. **Results:** We studied the significance of the PDZ, SH3, HOOK and GK domains in the cytoplasmic localization of hDLG. We found that mutation of the SH3 or GK domain, but not the PDZ domain, resulted in a re‐localization of hDLG to the nucleus. Furthermore, hDLG was found to possess a potential nuclear localization signal in the HOOK domain. **Conclusion:** These results suggest that the SH3, HOOK and GK domains of hDLG are important for its cytoplasmic localization.

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Author

Kazuyoshi Kohu; Fumiaki Ogawa; Tetsu Akiyama

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 1356-9597)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)