Loss of function in rpms-1 does not enhance phenotypes of rpm-1 mutants
The E3 ubiquitin ligase RPM-1 consists of 3,766 amino acids, with a RING finger domain at the C-terminus that functions to target the DLK-1 kinase for degradation for synapse development and axon termination. for aka F07B7.12 resides 35 kb away from on chromosome V, and is a near-perfect 12 kb dupli...
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Veröffentlicht in: | microPublication biology 2024, Vol.2024 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The
E3 ubiquitin ligase RPM-1 consists of 3,766 amino acids, with a RING finger domain at the C-terminus that functions to target the DLK-1 kinase for degradation for synapse development and axon termination.
for
aka F07B7.12
resides 35 kb away from
on chromosome V, and is a near-perfect 12 kb duplication of
including the entire promoter region and coding sequences. RPMS-1 consists of 1,964 amino acids and is identical to the N-terminal half of RPM-1 , except the last 40 amino acids. Previous studies showed that transgenic overexpression of the duplicated region of
did not rescue synapse defects of
loss of function mutants. Here, using CRISPR editing, we generated a double knockout of
and
. We find that axon and synapse defects in
double mutants resemble those in
single mutants. Expression levels of endogenously tagged DLK-1 protein are increased to a comparable degree in
and
mutants, compared to the control. These data, along with previous transgene expression analysis, support the idea that
does not have a major role in RPM-1-mediated cellular processes. |
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ISSN: | 2578-9430 2578-9430 |
DOI: | 10.17912/micropub.biology.001396 |