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Cited by 368

The DOI matches its Crossref record.

Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1.

Open access
Lue, R A, Marfatia, S M, Branton, D, Chishti, A H·1994·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.91.21.9818
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Abstract

The Drosophila discs large tumor suppressor protein, dlg, has been shown to regulate the growth of imaginal discs during embryogenesis [Woods, D. F. & Bryant, P. J. (1991) Cell 66, 451-464]. We cloned and sequenced the complete cDNA for a human B-lymphocyte 100-kDa protein that shares 60% amino acid identity with dlg. This human homologue of Drosophila discs large (hdlg) contains a C-terminal domain homologous to the known guanylate kinases, a src homology 3 region motif, and three dlg homology repeats. Two nonhomologous domains that can contain in-frame insertions result in at least four alternatively spliced isoforms of hdlg. Several hdlg RNA transcripts are widely distributed in human and murine tissues, and the protein is localized to regions of cell-cell contact. Protein 4.1, the defining member of a family that includes talin and merlin/schwannomin, has the same cellular localization as hdlg, and two sites within hdlg associate in vitro with the 30-kDa N-terminal domain of protein 4.1.

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Metadata

Authors
Lue, R. A., Marfatia, S. M., Branton, D., & Chishti, A. H.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
1994-10-11
Volume
91
Issue
21
Pages
9818-9822
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.91.21.9818
OpenAlex
W2060061784
Cited by
368
References
0
FWCI
8.75
Type
journal article
Language
en
Open access
green

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