Coscarelli EM [class:all]
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381 results (0.018 seconds)
- interaction: Interaction involving inx-6
- paper:
Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids
[
Midwest Worm Meeting,
1998] During morphogenesis, the <EM>C. elegans</EM> embryo elongates four-fold from a ball of cells into a long, thin worm. This elongation is dependent on circumferentially oriented actin bundles which form in the embryonic epidermal cells and are thought to generate the contractile force required for elongation. SMA-1 is a cytoskeletal protein which is homologous to <EM>Drosophila</EM> Beta-H-spectrin and is required for normal elongation: in <EM>sma-1</EM> mutants, the rate of elongation is decreased resulting in larvae that are shorter than wild-type at hatching. In many of the <EM>sma-1</EM> mutants it is been found that the organization of the epidermal actin bundles is altered (V. Praitis, personal communication). The <EM>sma-1</EM> alleles isolated in our lab vary in their effect on the rate of elongation suggesting that, in addition to its likely structural function, SMA-1 plays a role in regulation of elongation. To understand these functions of SMA-1, we have begun to isolate suppressors of <EM>sma-1</EM> mutants. We have designed a simple genetic screen that takes advantage of the inability of <EM>sma-1</EM> larvae to chemotax to food and have used this screen to isolate both dominant and recessive suppressors. We are currently examining the suppressed phenotypes and mapping the mutations. Characterization of our <EM>sma-1</EM> suppressors will begin to answer questions regarding the role of the cytoskeleton during morphogenesis and the function of SMA-1 in the regulation of elongation. In addition, we hope to understand the relationship between SMA-1's role in body elongation and its role in morphogenesis of the pharynx and excretory cell canal.
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