Journal home
Advance online publication
Current issue
Archive
Press releases
Supplements and Focuses
Image gallery
Guide to authors
Online submissionOnline submission
Permissions
For referees
Free online issue
Contact the journal
Subscribe
Advertising
work@npg
naturereprints
About this site
For librarians
 
NPG Resources
Nature
Nature Reviews Molecular Cell Biology
UCSD-Nature Signaling Gateway
The Cell Migration Gateway
Nature Reports Stem Cells
Nature Reports Avian Flu
NPG Subject areas
Biotechnology
Cancer
Chemistry
Clinical Medicine
Dentistry
Development
Drug Discovery
Earth Sciences
Evolution & Ecology
Genetics
Immunology
Materials Science
Medical Research
Microbiology
Molecular Cell Biology
Neuroscience
Pharmacology
Physics
Browse all publications
Letter
Nature Cell Biology  5, 987 - 993 (2003)
Published online: 19 October 2003; | doi:10.1038/ncb1055

Discs-Large and Strabismus are functionally linked to plasma membrane formation

Ok-Kyung Lee1, Kristopher K. Frese2, Jennifer S. James1, Darshana Chadda1, Zhi-Hong Chen1, Ronald T. Javier2 & Kyung-Ok Cho1

1  Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

2  Department of Molecular Virology and Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

Correspondence should be addressed to Kyung-Ok Cho kcho@bcm.tmc.edu
During early embryogenesis in Drosophila melanogaster, extensive vesicle transport occurs to build cell boundaries for 6,000 nuclei. Here we show that this important process depends on a functional complex formed between the tumour suppressor and adaptor protein Discs-Large (Dlg)1 and the integral membrane protein Strabismus (Stbm)/Van Gogh (Vang)2, 3. In support of this idea, embryos with mutations in either dlg or stbm displayed severe defects in plasma membrane formation. Conversely, overexpression of Dlg and Stbm synergistically induced excessive plasma membrane formation. In addition, ectopic co-expression of Stbm (which associated with post-Golgi vesicles) and the mammalian Dlg homologue SAP97/hDlg4, 5 promoted translocation of SAP97 from the cytoplasm to both post-Golgi vesicles and the plasma membrane. This effect was dependent on the interaction between Stbm and SAP97. These findings suggest that the Dlg−Stbm complex recruits membrane-associated proteins and lipids from internal membranes to sites of new plasma membrane formation.


MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated

RESEARCH
Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein
Oncogene Original Article (06 Feb 2003)

 Top
Abstract
Previous | Next
Table of contents
Full textFull text
Download PDFDownload PDF
Send to a friendSend to a friend
Save this linkSave this link

Open Innovation Challenges

  • Corrosion Inhibitor

    • Deadline: Aug 19 2009
    • Reward: $10,000 USD

    The Seeker is looking for inhibitors of corrosion. This Challenge requires only a written descripti...

  • Efficient Chromosome Doubling: Plant Cell Division

    • Deadline: Jul 15 2009
    • Reward: $20,000 USD

    The Seeker is looking for an efficient chromosome doubling method in plants and in particular, metho...

Figures & Tables
Supplementary info
Export citation
natureproducts

Search buyers guide:

 
ADVERTISEMENT
 
Nature Cell Biology
ISSN: 1465-7392
EISSN: 1476-4679
Journal home | Advance online publication | Current issue | Archive | Press releases | For authors | Online submission | For referees | Free online issue | About the journal | Contact the journal | Subscribe | Advertising | work@npg | Reprints and permissions | About this site | For librarians
Nature Publishing Group, publisher of Nature, and other science journals and reference works©2003 Nature Publishing Group | Privacy policy