Investigation of Conserved Amino Acids in the EGL-15 5A Domain Required for Sex Myoblast Migration in C. elegans

Fibroblast Growth Factor Receptors (FGFRs) play a role in diverse developmental pathways that mediate cell proliferation, cell migration, and cell survival. We use <i>C. elegans</i> as a model to better understand FGFR signaling specificity. <i>C. elegans</i> has a single FGFR, EGL-15 . EGL-15 contains an alternatively spliced exon 5 that results in two isoforms, EGL-15(5A) and EGL-15(5B), that differ in their extracellular domains. The EGL-15(5A) isoform is required for the chemoattraction of a pair of migrating sex myoblasts, whose correct positioning is required for egg laying. Deletion of the 5A domain results in an egg-laying defective (Egl) organism. We identified six highly conserved amino acids within the 5A domain and found that two amino acids, S145 and L148 are specifically required for sex myoblast migration in <i>C. elegans</i> .

Authors

Institutions

Publication Details

Journal
PubMed
Published
2024-09-30
DOI
https://doi.org/10.17912/micropub.biology.001374
Primary Topic
Epigenetics and DNA Methylation
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Investigation of Conserved Amino Acids in the EGL-15 5A Domain Required for Sex Myoblast Migration in C. elegans

Isabel Suárez, Dallas R. Fonseca, Michael Stern, Te‐Wen Lo et al.
PubMed
Epigenetics and DNA Methylation
article

Investigation of Conserved Amino Acids in the EGL-15 5A Domain Required for Sex Myoblast Migration in C. elegans

Isabel Suárez, Dallas R. Fonseca, Michael Stern, Te‐Wen Lo, Birsen Gürkaynak
article en

Abstract

Fibroblast Growth Factor Receptors (FGFRs) play a role in diverse developmental pathways that mediate cell proliferation, cell migration, and cell survival. We use <i>C. elegans</i> as a model to better understand FGFR signaling specificity. <i>C. elegans</i> has a single FGFR, EGL-15 . EGL-15 contains an alternatively spliced exon 5 that results in two isoforms, EGL-15(5A) and EGL-15(5B), that differ in their extracellular domains. The EGL-15(5A) isoform is required for the chemoattraction of a pair of migrating sex myoblasts, whose correct positioning is required for egg laying. Deletion of the 5A domain results in an egg-laying defective (Egl) organism. We identified six highly conserved amino acids within the 5A domain and found that two amino acids, S145 and L148 are specifically required for sex myoblast migration in <i>C. elegans</i> .

PubMedVol. 2024
New England Biolabs (United States) (US), Northeastern Illinois University (US), Ithaca College (US)
National Institutes of Health
Openalex Percentile: Top 83%
Epigenetics and DNA Methylation
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.