Unknown

Dataset Information

0

EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the MADD-4 guidance cue in Caenorhabditis elegans.


ABSTRACT: We recently discovered a secreted and diffusible midline cue called MADD-4 (an ADAMTSL) that guides migrations along the dorsoventral axis of the nematode Caenorhabditis elegans. We showed that the transmembrane receptor, UNC-40 (DCC), whose canonical ligand is the UNC-6 (netrin) guidance cue, is required for extension towards MADD-4. Here, we demonstrate that MADD-4 interacts with an EVA-1/UNC-40 co-receptor complex to attract cell extensions. EVA-1 is a conserved transmembrane protein with predicted galactose-binding lectin domains. EVA-1 functions in the same pathway as MADD-4, physically interacts with both MADD-4 and UNC-40, and enhances UNC-40's sensitivity to the MADD-4 cue. This enhancement is especially important in the presence of UNC-6. In EVA-1's absence, UNC-6 interferes with UNC-40's responsiveness to MADD-4; in UNC-6's absence, UNC-40's responsiveness to MADD-4 is less dependent on EVA-1. By enabling UNC-40 to respond to MADD-4 in the presence of UNC-6, EVA-1 may increase the precision by which UNC-40-directed processes can reach their MADD-4-expressing targets within a field of the UNC-6 guidance cue.

SUBMITTER: Chan KK 

PROVIDER: S-EPMC4133157 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the MADD-4 guidance cue in Caenorhabditis elegans.

Chan Kevin Ka Ming KK   Seetharaman Ashwin A   Bagg Rachel R   Selman Guillermo G   Zhang Yuqian Y   Kim Joowan J   Roy Peter J PJ  

PLoS genetics 20140814 8


We recently discovered a secreted and diffusible midline cue called MADD-4 (an ADAMTSL) that guides migrations along the dorsoventral axis of the nematode Caenorhabditis elegans. We showed that the transmembrane receptor, UNC-40 (DCC), whose canonical ligand is the UNC-6 (netrin) guidance cue, is required for extension towards MADD-4. Here, we demonstrate that MADD-4 interacts with an EVA-1/UNC-40 co-receptor complex to attract cell extensions. EVA-1 is a conserved transmembrane protein with pre  ...[more]

Similar Datasets

| S-EPMC3908881 | biostudies-literature
| S-EPMC4849719 | biostudies-literature
| S-EPMC2974572 | biostudies-literature
| S-EPMC2762468 | biostudies-literature
| S-EPMC2120500 | biostudies-other
| S-EPMC3188576 | biostudies-literature
| S-EPMC2613081 | biostudies-literature
| S-EPMC2175264 | biostudies-literature
| S-EPMC2441656 | biostudies-literature
| S-EPMC4325984 | biostudies-literature