HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 47, 35989-35996, November 24, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/47/35989    most recent M606086200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map 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 Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Carroll, B. T. Articles by Morgan, P. G. Search for Related Content PubMed PubMed Citation Articles by Carroll, B. T. Articles by Morgan, P. G. Social Bookmarking                      What's this?

Sulfated Signal from ASJ Sensory Neurons Modulates Stomatin-dependent Coordination in Caenorhabditis elegans^*

Bryan T. Carroll¹², George R. Dubyak, Margaret M. Sedensky^¶1, and Phil G. Morgan^¶13

From the Department of Genetics and the Department of Physiology and Biophysics, Case School of Medicine and the ^¶Departments of Anesthesiology and Genetics, University Hospitals and Case School of Medicine, Cleveland, Ohio 44106

The neuronal stomatin-like proteins UNC-1 and UNC-24 play important roles in the nervous system of Caenorhabditis elegans. These neuronal stomatin-like proteins are putative chaperone proteins that can modify volatile anesthetic sensitivity and disrupt coordinated locomotion. A suppressor of unc-1 and unc-24, named ssu-1(fc73) (for suppressor of stomatin uncoordination), suppresses three phenotypes of neuronal stomatin-like protein deficiency as follows: volatile anesthetic sensitivity, uncoordinated locomotion, and a constitutive alternative developmental phenotype known as dauer. Here we provide the first phenotypic characterization of ssu-1, predicted to be the only C. elegans cytosolic alcohol sulfotransferase, a family of enzymes that catalyze a sulfate linkage with the alcohol group of small molecules for the purposes of detoxification or modification of signaling. In vitro enzyme analysis of bacterially expressed SSU-1 demonstrates sulfotransferase activity and thus confirms the function predicted by protein sequence similarities. Whereas unc-1 is expressed in the majority of neurons of C. elegans, expression of SSU-1 protein in only the two ASJ amphid interneurons is sufficient to restore the wild type phenotype. This work demonstrates that SSU-1 is a functional sulfotransferase that likely modifies endocrine signaling in C. elegans. The expression of SSU-1 in the ASJ neurons refines the understanding of the function of these cells and supports their classification as endocrine tissue. The relationship of unc-1, unc-24, and ssu-1 is the first association of neuronal stomatin-like proteins sharing regulatory roles with a sulfotransferase enzyme.

Received for publication, June 26, 2006 , and in revised form, September 1, 2006.

^* This work was supported in part by the Department of Anesthesiology of University Hospitals of Cleveland. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a movie.

¹ Supported in part by National Institutes of Health Grant GM-45402.

² Supported in part by National Institutes of Health Grant T32 GM07250 and the Case Medical Scientist Training Program.

³ To whom correspondence should be addressed: Dept. of Anesthesiology, 11100 Euclid Ave., University Hospitals and Case School of Medicine, Cleveland, OH 44106-5007. Tel.: 216-844-7340; Fax: 216-844-3781; E-mail: philip.morgan{at}uhhs.com.

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