CATP-6, a C. elegans ortholog of ATP13A2 PARK9, positively regulates GEM-1, an SLC16A transporter
| Autor: | Pamela J. Tieu, Eric J. Lambie, Barbara Conradt, Nadja Lebedeva, Diane L. Church |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Monocarboxylic Acid Transporters
Genotype endocrine system diseases ATPase Molecular Sequence Data Regulator Sequence Homology lcsh:Medicine Suppression Genetic TRPM Animals Magnesium Amino Acid Sequence Caenorhabditis elegans Caenorhabditis elegans Proteins Gonads lcsh:Science Adenosine Triphosphatases Genetics Multidisciplinary biology lcsh:R Gene Expression Regulation Developmental Transporter biology.organism_classification Transport protein Cell biology Proton-Translocating ATPases Membrane protein biology.protein lcsh:Q Intracellular Research Article |
| Zdroj: | PLoS ONE, Vol 8, Iss 10, p e77202 (2013) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | In previous work, we found that gain-of-function mutations that hyperactivate GEM-1 (an SLC16A transporter protein) can bypass the requirement for GON-2 (a TRPM channel protein) during the initiation of gonadogenesis in C. elegans. Consequently, we proposed that GEM-1 might function as part of a Mg(2+) uptake pathway that functions in parallel to GON-2. In this study, we report that CATP-6, a C. elegans ortholog of the P5B ATPase, ATP13A2 (PARK9), is necessary for gem-1 gain-of-function mutations to suppress the effects of gon-2 inactivation. One possible explanation for this observation is that GEM-1 serves to activate CATP-6, which then functions as a Mg(2+) transporter. However, we found that overexpression of GEM-1 can alleviate the requirement for CATP-6 activity, suggesting that CATP-6 probably acts as a non-essential upstream positive regulator of GEM-1. Our results are consistent with the notion that P5B ATPases govern intracellular levels of Mg(2+) and/or Mn(2+) by regulating the trafficking of transporters and other proteins associated with the plasma membrane. |
| Databáze: | OpenAIRE |
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