QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

doi: 10.1242/10.1242/dev.00604

This Article Figures Only Full Text Full Text (PDF) Supplemental Data Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Goodman, S. J. Articles by Stern, M. J. Search for Related Content PubMed PubMed Citation Articles by Goodman, S. J. Articles by Stern, M. J. Social Bookmarking                         What's this?

Alternative splicing affecting a novel domain in the C. elegans EGL-15 FGF receptor confers functional specificity

S. Jay Goodman¹, Catherine S. Branda^2,*, Matthew K. Robinson^2,, Rebecca D. Burdine^1, and Michael J. Stern^2,

¹ Department of Cell Biology, Yale University School of Medicine, I-354 SHM PO Box 208005, New Haven, CT 06520-8005, USA
² Department of Genetics, Yale University School of Medicine, I-354 SHM PO Box 208005, New Haven, CT 06520-8005, USA

Author for correspondence (e-mail: michael.stern{at}yale.edu)

Accepted 12 May 2003

Fibroblast growth factor (FGF) receptors trigger a wide variety of cellular responses as diverse as cell migration, cell proliferation and cell differentiation. However, the molecular basis of the specificity of these responses is not well understood. The C. elegans FGF receptor EGL-15 similarly mediates a number of different responses, including transducing a chemoattractive signal and mediating an essential function. Analysis of the migration-specific alleles of egl-15 has identified a novel EGL-15 isoform that provides a molecular explanation for the different phenotypic effects of lesions at this locus. Alternative splicing yields two EGL-15 proteins containing different forms of a domain located within the extracellular region of the receptors immediately after the first IG domain. Neither of these two domain forms is found in any other FGF receptor. We have tested the roles of these EGL-15 receptor isoforms and their two FGF ligands for their signaling specificity. Our analyses demonstrate different physiological functions for the two receptor variants. EGL-15(5A) is required for the response to the FGF chemoattractant that guides the migrating sex myoblasts to their final positions. By contrast, EGL-15(5B) is both necessary and sufficient to elicit the essential function mediated by this receptor.

Key words: FGF receptor, EGL-15, Alternative splicing, Chemoattraction, Achondroplasia, Sex myoblast

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				K. L. Schmidt, N. Marcus-Gueret, A. Adeleye, J. Webber, D. Baillie, and E. G. Stringham The cell migration molecule UNC-53/NAV2 is linked to the ARP2/3 complex by ABI-1 Development, February 15, 2009; 136(4): 563 - 574. [Abstract] [Full Text] [PDF]

				Y.-T. Huang, F.-C. Chen, C.-J. Chen, H.-L. Chen, and T.-J. Chuang Identification and analysis of ancestral hominoid transcriptome inferred from cross-species transcript and processed pseudogene comparisons Genome Res., July 1, 2008; 18(7): 1163 - 1170. [Abstract] [Full Text] [PDF]

				H. Kuroyanagi, G. Ohno, S. Mitani, and M. Hagiwara The Fox-1 Family and SUP-12 Coordinately Regulate Tissue-Specific Alternative Splicing In Vivo Mol. Cell. Biol., December 15, 2007; 27(24): 8612 - 8621. [Abstract] [Full Text] [PDF]

				H. D. Sun, M. Malabunga, J. R. Tonra, R. DiRenzo, F. E. Carrick, H. Zheng, H.-R. Berthoud, O. P. McGuinness, J. Shen, P. Bohlen, et al. Monoclonal antibody antagonists of hypothalamic FGFR1 cause potent but reversible hypophagia and weight loss in rodents and monkeys Am J Physiol Endocrinol Metab, March 1, 2007; 292(3): E964 - E976. [Abstract] [Full Text] [PDF]

				S. J. Dixon, M. Alexander, R. Fernandes, N. Ricker, and P. J. Roy FGF negatively regulates muscle membrane extension in Caenorhabditis elegans Development, April 1, 2006; 133(7): 1263 - 1275. [Abstract] [Full Text] [PDF]

				T. C. Fleming, F. W. Wolf, and G. Garriga Sensitized genetic backgrounds reveal a role for C. elegans FGF EGL-17 as a repellent for migrating CAN neurons Development, November 1, 2005; 132(21): 4857 - 4867. [Abstract] [Full Text] [PDF]

				T. D. Dinkova, B. D. Keiper, N. L. Korneeva, E. J. Aamodt, and R. E. Rhoads Translation of a Small Subset of Caenorhabditis elegans mRNAs Is Dependent on a Specific Eukaryotic Translation Initiation Factor 4E Isoform Mol. Cell. Biol., January 1, 2005; 25(1): 100 - 113. [Abstract] [Full Text] [PDF]

				I. E. Sasson and M. J. Stern FGF and PI3 kinase signaling pathways antagonistically modulate sex muscle differentiation in C. elegans Development, November 1, 2004; 131(21): 5381 - 5392. [Abstract] [Full Text] [PDF]

				C. Popovici, F. Conchonaud, D. Birnbaum, and R. Roubin Functional Phylogeny Relates LET-756 to Fibroblast Growth Factor 9 J. Biol. Chem., September 17, 2004; 279(38): 40146 - 40152. [Abstract] [Full Text] [PDF]