Development, Vol 115, Issue 1 267-276, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

Dynamic expression of the cell adhesion molecule fasciclin I during embryonic development in Drosophila

L McAllister, CS Goodman and K Zinn
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.

A number of different cell surface glycoproteins expressed in the central nervous system (CNS) have been identified in insects and shown to mediate cell adhesion in tissue culture systems. The fasciclin I protein is expressed on a subset of CNS axon pathways in both grasshopper and Drosophila. It consists of four homologous 150-amino acid domains which are unrelated to other sequences in the current databases, and is tethered to the cell surface by a glycosyl-phosphatidylinositol linkage. In this paper we examine in detail the expression of fasciclin I mRNA and protein during Drosophila embryonic development. We find that fasciclin I is expressed in several distinct patterns at different stages of development. In blastoderm embryos it is briefly localized in a graded pattern. During the germ band extended period its expression evolves through two distinct phases. Fasciclin I mRNA and protein are initially localized in a 14-stripe pattern which corresponds to segmentally repeated patches of neuroepithelial cells and neuroblasts. Expression then becomes confined to CNS and peripheral sensory (PNS) neurons. Fasciclin I is expressed on all PNS neurons, and this expression is stably maintained for several hours. In the CNS, fasciclin I is initially expressed on all commissural axons, but then becomes restricted to specific axon bundles. The early commissural expression pattern is not observed in grasshopper embryos, but the later bundle-specific pattern is very similar to that seen in grasshopper. The existence of an initial phase of expression on all commissural bundles helps to explain the loss-of-commissures phenotype of embryos lacking expression of both fasciclin I and of the D-abl tyrosine kinase. Fasciclin I is also expressed in several nonneural tissues in the embryo.

This article has been cited by other articles:

				S. Zhu, M. F. Barbe, N. Amin, S. Rani, S. N. Popoff, F. F. Safadi, and J. Litvin Immunolocalization of Periostin-like Factor and Periostin During Embryogenesis J. Histochem. Cytochem., April 1, 2008; 56(4): 329 - 345. [Abstract] [Full Text] [PDF]

				K. L. Johnson, B. J. Jones, A. Bacic, and C. J. Schultz The Fasciclin-Like Arabinogalactan Proteins of Arabidopsis. A Multigene Family of Putative Cell Adhesion Molecules Plant Physiology, December 1, 2003; 133(4): 1911 - 1925. [Abstract] [Full Text]

				P. Paulsrud and P. Lindblad Fasciclin Domain Proteins Are Present in Nostoc Symbionts of Lichens Appl. Envir. Microbiol., April 1, 2002; 68(4): 2036 - 2039. [Abstract] [Full Text] [PDF]

				L. Meadows, D Gell, K Broadie, A. Gould, and R. White The cell adhesion molecule, connectin, and the development of the Drosophila neuromuscular system J. Cell Sci., January 1, 1994; 107(1): 321 - 328. [Abstract] [PDF]