Different isoforms of the C. elegans FGF receptor are required for attraction and repulsion of the migrating sex myoblasts

    Authors

    T. W. Lo; C. S. Branda; P. Huang; I. E. Sasson; S. J. Goodman;M. J. Stern

    Comments

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    Abbreviated Journal Title

    Dev. Biol.

    Keywords

    alternative splicing; chemoattraction; EGL-15; FGF receptor; sex; myoblast; CAENORHABDITIS-ELEGANS; CELL-MIGRATION; AXON GUIDANCE; IN-VIVO; SIGNALING PATHWAY; SEMAPHORIN 3A; GENE; EXPRESSION; HERMAPHRODITES; ASSOCIATION; Developmental Biology

    Abstract

    The Caenorhabditis elegans FGF receptor, EGL-15, is alternatively-spliced to yield two major isoforms that differ in their extracellular domains. The EGL-15(5A) isoform is necessary for the gonadal chemoattraction of the migrating sex myoblasts (SMs), while the EGL-15(5B) isoform is required for viability. Here we show that 5A is predominantly expressed in the M lineage, which gives rise to the migrating SMs and their sex muscle descendants, while 5B is predominantly expressed in the hypodermis. Tissue-specific expression, however, explains only part of the functional differences between these two receptor isoforms. 5A can carry out the reciprocal essential function of 513 when expressed in the hypodermis, but 513 is incapable of carrying out SM chemoattraction. Our data, therefore, indicate that the structural differences in these two isoforms contribute to their functional differences. Two lines of evidence indicate that the 5B isoform also plays a role in SM migration, implicating it in the repulsion that is observed when the chemoattraction is compromised. Thus, structural differences in the extracellular domains of these two isoforms can specify either attraction to or repulsion from the gonad. (C) 2008 Elsevier Inc. All rights reserved.

    Journal Title

    Developmental Biology

    Volume

    318

    Issue/Number

    2

    Publication Date

    1-1-2008

    Document Type

    Article

    Language

    English

    First Page

    268

    Last Page

    275

    WOS Identifier

    WOS:000256651500006

    ISSN

    0012-1606

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