Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling.
Bone morphogenetic protein (BMP) pathways control an array of developmental and homeostatic events, and must themselves be exquisitely controlled. Here, we identify Caenorhabditis elegans SMA-10 as a positive extracellular regulator of BMP-like receptor signaling. SMA-10 acts genetically in a BMP-li...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2010-05-01
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| Series: | PLoS Genetics |
| Online Access: | http://europepmc.org/articles/PMC2873917?pdf=render |
| _version_ | 1819107729015308288 |
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| author | Tina L Gumienny Lesley Macneil Cole M Zimmerman Huang Wang Lena Chin Jeffrey L Wrana Richard W Padgett |
| author_facet | Tina L Gumienny Lesley Macneil Cole M Zimmerman Huang Wang Lena Chin Jeffrey L Wrana Richard W Padgett |
| author_sort | Tina L Gumienny |
| collection | DOAJ |
| description | Bone morphogenetic protein (BMP) pathways control an array of developmental and homeostatic events, and must themselves be exquisitely controlled. Here, we identify Caenorhabditis elegans SMA-10 as a positive extracellular regulator of BMP-like receptor signaling. SMA-10 acts genetically in a BMP-like (Sma/Mab) pathway between the ligand DBL-1 and its receptors SMA-6 and DAF-4. We cloned sma-10 and show that it has fifteen leucine-rich repeats and three immunoglobulin-like domains, hallmarks of an LRIG subfamily of transmembrane proteins. SMA-10 is required in the hypodermis, where the core Sma/Mab signaling components function. We demonstrate functional conservation of LRIGs by rescuing sma-10(lf) animals with the Drosophila ortholog lambik, showing that SMA-10 physically binds the DBL-1 receptors SMA-6 and DAF-4 and enhances signaling in vitro. This interaction is evolutionarily conserved, evidenced by LRIG1 binding to vertebrate receptors. We propose a new role for LRIG family members: the positive regulation of BMP signaling by binding both Type I and Type II receptors. |
| first_indexed | 2024-12-22T02:58:39Z |
| format | Article |
| id | doaj.art-25f62f5a67c94157ad37422dfa78a436 |
| institution | Directory Open Access Journal |
| issn | 1553-7390 1553-7404 |
| language | English |
| last_indexed | 2024-12-22T02:58:39Z |
| publishDate | 2010-05-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Genetics |
| spelling | doaj.art-25f62f5a67c94157ad37422dfa78a4362022-12-21T18:41:12ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042010-05-0165e100096310.1371/journal.pgen.1000963Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling.Tina L GumiennyLesley MacneilCole M ZimmermanHuang WangLena ChinJeffrey L WranaRichard W PadgettBone morphogenetic protein (BMP) pathways control an array of developmental and homeostatic events, and must themselves be exquisitely controlled. Here, we identify Caenorhabditis elegans SMA-10 as a positive extracellular regulator of BMP-like receptor signaling. SMA-10 acts genetically in a BMP-like (Sma/Mab) pathway between the ligand DBL-1 and its receptors SMA-6 and DAF-4. We cloned sma-10 and show that it has fifteen leucine-rich repeats and three immunoglobulin-like domains, hallmarks of an LRIG subfamily of transmembrane proteins. SMA-10 is required in the hypodermis, where the core Sma/Mab signaling components function. We demonstrate functional conservation of LRIGs by rescuing sma-10(lf) animals with the Drosophila ortholog lambik, showing that SMA-10 physically binds the DBL-1 receptors SMA-6 and DAF-4 and enhances signaling in vitro. This interaction is evolutionarily conserved, evidenced by LRIG1 binding to vertebrate receptors. We propose a new role for LRIG family members: the positive regulation of BMP signaling by binding both Type I and Type II receptors.http://europepmc.org/articles/PMC2873917?pdf=render |
| spellingShingle | Tina L Gumienny Lesley Macneil Cole M Zimmerman Huang Wang Lena Chin Jeffrey L Wrana Richard W Padgett Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. PLoS Genetics |
| title | Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. |
| title_full | Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. |
| title_fullStr | Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. |
| title_full_unstemmed | Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. |
| title_short | Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling. |
| title_sort | caenorhabditis elegans sma 10 lrig is a conserved transmembrane protein that enhances bone morphogenetic protein signaling |
| url | http://europepmc.org/articles/PMC2873917?pdf=render |
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