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Vol. 11, Issue 11, 3911-3923, November 2000

Nidogen Is Nonessential and Not Required for Normal Type IV Collagen Localization in Caenorhabditis elegans

Seong Hoon Kang, and James M. Kramer*

Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611

Nidogen (entactin) can form a ternary complex with type IV collagen and laminin and is thought to play a critical role in basement membrane assembly. We show that the Caenorhabditis elegans nidogen homologue nid-1 generates three isoforms that differ in numbers of rod domain endothelial growth factor repeats and are differentially expressed during development. NID-1 appears at the start of embryonic morphogenesis associated with muscle cells and subsequently accumulates on pharyngeal, intestinal, and gonad primordia. In larvae and adults NID-1 is detected in most basement membranes but accumulates most strongly around the nerve ring and developing gonad. NID-1 is concentrated under dense bodies, at the edges of muscle quadrants, and on the sublateral nerves that run under muscles. Two deletions in nid-1 were isolated: cg119 is a molecular null, whereas cg118 produces truncated NID-1 missing the G2 collagen IV binding domain. Neither deletion causes overt abnormal phenotypes, except for mildly reduced fecundity. Truncated cg118 NID-1 shows wild-type localization, demonstrating that the G2 domain is not necessary for nidogen assembly. Both nid-1 mutants assemble type IV collagen in a completely wild-type pattern, demonstrating that nidogen is not essential for type IV collagen assembly into basement membranes.

* Corresponding author. E-mail address: jkramer{at}nwu.edu.

Molecular Biology of the Cell
Vol. 11, 3911-3923, November 2000
Copyright © 2000 by The American Society for Cell Biology


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