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doi: 10.1242/10.1242/dev.00481
subunits and their role in C. elegans development
1 Department of Pathology, Robert Wood Johnson Medical School, Piscataway, NJ
08854, USA
2 Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New
York, NY 104661, USA
3 Department of Biology, Johns Hopkins University, Baltimore, MD 21218,
USA
4 Medical Biotechnology Center, University of Maryland Biotechnology Institute,
725 West Lombard Street, Baltimore, MD 21201, USA
5 Max-Planck-Institut Für Medizinische Forchung, Heidelberg, 69120
Germany
6 Department of Biology, Sinsheimer Laboratories, University of California,
Santa Cruz, CA 95064, USA
* These authors contributed equally to the paper
Author for correspondence (e-mail:
william.wadsworth{at}umdnj.edu)
Accepted 14 April 2003
Laminins are heterotrimeric (
/ß/
) glycoproteins that
form a major polymer within basement membranes. Different , ß and
subunits can assemble into various laminin isoforms that have
different, but often overlapping, distributions and functions. In this study,
we examine the contributions of the laminin subunits to the
development of C. elegans. There are two , one ß and one
laminin subunit, suggesting two laminin isoforms that differ by their
subunit assemble in C. elegans. We find that near the end of
gastrulation and before other basement membrane components are detected, the
subunits are secreted between primary tissue layers and become
distributed in different patterns to the surfaces of cells. Mutations in
either subunit gene cause missing or disrupted extracellular matrix
where the protein normally localizes. Cell-cell adhesions are abnormal: in
some cases essential cell-cell adhesions are lacking, while in other cases,
cells inappropriately adhere to and invade neighboring tissues. Using electron
microscopy, we observe adhesion complexes at improper cell surfaces and
disoriented cytoskeletal filaments. Cells throughout the animal show defective
differentiation, proliferation or migration, suggesting a general disruption
of cell-cell signaling. The results suggest a receptor-mediated process
localizes each secreted laminin to exposed cell surfaces and that laminin is
crucial for organizing extracellular matrix, receptor and intracellular
proteins at those surfaces. We propose this supramolecular architecture
regulates adhesions and signaling between adjacent tissues.
Key words: Laminin, Basement membranes, Extracellular matrix, C. elegans, Cell adhesion, Cell polarity, Cell migration, Differentiation, Cell-cell signaling
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