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The SH3, HOOK and guanylate kinase‐like domains of hDLG are important for its cytoplasmic localization
Author(s) -
Kohu Kazuyoshi,
Ogawa Fumiaki,
Akiyama Tetsu
Publication year - 2002
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2002.00555.x
Subject(s) - pdz domain , guanylate kinase , biology , sh3 domain , microbiology and biotechnology , signal transducing adaptor protein , scaffold protein , cytoplasm , nuclear localization sequence , subcellular localization , kinase , phosphorylation , signal transduction , membrane protein , genetics , proto oncogene tyrosine protein kinase src , membrane
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.