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dc.contributor.authorHueston, Jennifer L.
dc.contributor.authorHerren, Gina Purinton
dc.contributor.authorCueva, Juan G.
dc.contributor.authorBuechner, Matthew
dc.contributor.authorLundquist, Erik A.
dc.contributor.authorGoodman, Miriam B.
dc.contributor.authorSuprenant, Kathy A.
dc.date.accessioned2014-01-24T21:10:14Z
dc.date.available2014-01-24T21:10:14Z
dc.date.issued2008-11-17
dc.identifier.citationHueston, Jennifer L, Gina Purinton Herren, Juan G Cueva, Matthew Buechner, Erik A Lundquist, Miriam B Goodman, and Kathy A Suprenant. 2008. “The C. Elegans EMAP-like Protein, ELP-1 Is Required for Touch Sensation and Associates with Microtubules and Adhesion Complexes.” BMC Developmental Biology 8:110. http://dx.doi.org/10.1186/1471-213X-8-110.
dc.identifier.urihttp://hdl.handle.net/1808/12839
dc.description.abstractBackground: The founding member of the EMAP-like protein family is the Echinoderm Microtubule-Associated Protein (EMAP), so-named for its abundance in sea urchin, starfish, and sand dollar eggs. The EMAP-like protein family has five members in mammals (EML1 through EML5) and only one in both Drosophila (ELP-1) and C. elegans (ELP-1). Biochemical studies of sea urchin EMAP and vertebrate EMLs implicate these proteins in the regulation of microtubule stability. So far, however, the physiological function of this protein family remains unknown.

Results: We examined the expression pattern of C. elegans ELP-1 by means of transgenic gene expression in living embryos and adults, and by immunolocalization with an ELP-1-specific antibody in fixed tissues. In embryos, ELP-1 is expressed in the hypodermis. In larvae and adults, ELP-1 is expressed in the body wall, spermatheca and vulval muscles, intestine, and hypodermal seam cells. In muscle, ELP-1 is associated with adhesion complexes near the cell surface and is bound to a criss-crossing network of microtubules in the cytoplasm. ELP-1 is also expressed in a subset of mechanoreceptor neurons, including the ray neurons in the male tail, microtubule-rich touch receptor neurons, and the six ciliated IL1 neurons. This restricted localization in the nervous system implies that ELP-1 plays a role in mechanotransmission. Consistent with this idea, decreasing ELP-1 expression decreases sensitivity to gentle touch applied to the body wall.

Conclusion: These data imply that ELP-1 may play an important role during the transmission of forces and signals between the body surface and both muscle cells and touch receptor neurons.
dc.publisherBioMed Central
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights.urihttp://creativecommons.org/licenses/by/2.0
dc.titleThe C. elegans EMAP-like protein, ELP-1 is required for touch sensation and associates with microtubules and adhesion complexes
dc.typeArticle
kusw.kuauthorHueston, Jennifer L.
kusw.kuauthorHerren, Gina Purinton
kusw.kuauthorBuechner, Matthew
kusw.kuauthorLundquist, Erik A.
kusw.kuauthorSuprenant, Kathy A.
kusw.kudepartmentMolecular Biosciences
kusw.oastatusfullparticipation
dc.identifier.doi10.1186/1471-213X-8-110
dc.identifier.orcidhttps://orcid.org/0000-0002-2103-9399
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as: This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.