Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila

Frans Tax, Jon J. Yeargers, James H. Thomas

Research output: Contribution to journalArticle

205 Citations (Scopus)

Abstract

THE lin-12 and glp-1 genes of Caenorhabditis elegans encode members of the Notch family of transmembrane proteins. Genetic studies indicate that the lin-12 and glp-1 proteins act as receptors in specific developmental cell interactions and that their functions are partially redundant. lin-12 glp-1 double mutants display certain embryonic defects not found in either single mutant. The phenotype of this double mutant is called Lag, and recessive mutations in either of the genes lag-1 or lag-2 can also result in the Lag phenotype, indicating that these two genes may participate in the same cell interactions that require lin-12 or glp-1. We report here that lag-2 encodes a predicted transmembrane protein of 402 amino acids. The predicted extracellular region of lag-2 is similar to amino-terminal regions of Delta and Serrate, two Drosophila proteins that are thought to function as ligands for Notch. The region of similarity includes sequences related to epidermal growth factor (EGF) repeats. We have isolated lag-2(sa37), a dominant allele that shows specific genetic interactions with lin-12. The sa37 mutation causes a Gly→Asp change in a conserved residue of an EGF motif. Because of its overall structure, its sequence similarity to Delta and Serrate, and its genetic interactions, we suggest that lag-2 encodes an intercellular signal for the lin-12 and glp-1 receptors.

Original languageEnglish (US)
Pages (from-to)150-154
Number of pages5
JournalNature
Volume368
Issue number6467
DOIs
StatePublished - Mar 10 1994
Externally publishedYes

Fingerprint

Drosophila
Epidermal Growth Factor
Cell Communication
Genes
Phenotype
Mutation
Proteins
Caenorhabditis elegans
Alleles
Ligands
Amino Acids
Drosophila Ser protein

ASJC Scopus subject areas

  • General

Cite this

Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila. / Tax, Frans; Yeargers, Jon J.; Thomas, James H.

In: Nature, Vol. 368, No. 6467, 10.03.1994, p. 150-154.

Research output: Contribution to journalArticle

Tax, Frans ; Yeargers, Jon J. ; Thomas, James H. / Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila. In: Nature. 1994 ; Vol. 368, No. 6467. pp. 150-154.
@article{8a31baf7fb84469f869436793dd4108d,
title = "Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila",
abstract = "THE lin-12 and glp-1 genes of Caenorhabditis elegans encode members of the Notch family of transmembrane proteins. Genetic studies indicate that the lin-12 and glp-1 proteins act as receptors in specific developmental cell interactions and that their functions are partially redundant. lin-12 glp-1 double mutants display certain embryonic defects not found in either single mutant. The phenotype of this double mutant is called Lag, and recessive mutations in either of the genes lag-1 or lag-2 can also result in the Lag phenotype, indicating that these two genes may participate in the same cell interactions that require lin-12 or glp-1. We report here that lag-2 encodes a predicted transmembrane protein of 402 amino acids. The predicted extracellular region of lag-2 is similar to amino-terminal regions of Delta and Serrate, two Drosophila proteins that are thought to function as ligands for Notch. The region of similarity includes sequences related to epidermal growth factor (EGF) repeats. We have isolated lag-2(sa37), a dominant allele that shows specific genetic interactions with lin-12. The sa37 mutation causes a Gly→Asp change in a conserved residue of an EGF motif. Because of its overall structure, its sequence similarity to Delta and Serrate, and its genetic interactions, we suggest that lag-2 encodes an intercellular signal for the lin-12 and glp-1 receptors.",
author = "Frans Tax and Yeargers, {Jon J.} and Thomas, {James H.}",
year = "1994",
month = "3",
day = "10",
doi = "10.1038/368150a0",
language = "English (US)",
volume = "368",
pages = "150--154",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6467",

}

TY - JOUR

T1 - Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila

AU - Tax, Frans

AU - Yeargers, Jon J.

AU - Thomas, James H.

PY - 1994/3/10

Y1 - 1994/3/10

N2 - THE lin-12 and glp-1 genes of Caenorhabditis elegans encode members of the Notch family of transmembrane proteins. Genetic studies indicate that the lin-12 and glp-1 proteins act as receptors in specific developmental cell interactions and that their functions are partially redundant. lin-12 glp-1 double mutants display certain embryonic defects not found in either single mutant. The phenotype of this double mutant is called Lag, and recessive mutations in either of the genes lag-1 or lag-2 can also result in the Lag phenotype, indicating that these two genes may participate in the same cell interactions that require lin-12 or glp-1. We report here that lag-2 encodes a predicted transmembrane protein of 402 amino acids. The predicted extracellular region of lag-2 is similar to amino-terminal regions of Delta and Serrate, two Drosophila proteins that are thought to function as ligands for Notch. The region of similarity includes sequences related to epidermal growth factor (EGF) repeats. We have isolated lag-2(sa37), a dominant allele that shows specific genetic interactions with lin-12. The sa37 mutation causes a Gly→Asp change in a conserved residue of an EGF motif. Because of its overall structure, its sequence similarity to Delta and Serrate, and its genetic interactions, we suggest that lag-2 encodes an intercellular signal for the lin-12 and glp-1 receptors.

AB - THE lin-12 and glp-1 genes of Caenorhabditis elegans encode members of the Notch family of transmembrane proteins. Genetic studies indicate that the lin-12 and glp-1 proteins act as receptors in specific developmental cell interactions and that their functions are partially redundant. lin-12 glp-1 double mutants display certain embryonic defects not found in either single mutant. The phenotype of this double mutant is called Lag, and recessive mutations in either of the genes lag-1 or lag-2 can also result in the Lag phenotype, indicating that these two genes may participate in the same cell interactions that require lin-12 or glp-1. We report here that lag-2 encodes a predicted transmembrane protein of 402 amino acids. The predicted extracellular region of lag-2 is similar to amino-terminal regions of Delta and Serrate, two Drosophila proteins that are thought to function as ligands for Notch. The region of similarity includes sequences related to epidermal growth factor (EGF) repeats. We have isolated lag-2(sa37), a dominant allele that shows specific genetic interactions with lin-12. The sa37 mutation causes a Gly→Asp change in a conserved residue of an EGF motif. Because of its overall structure, its sequence similarity to Delta and Serrate, and its genetic interactions, we suggest that lag-2 encodes an intercellular signal for the lin-12 and glp-1 receptors.

UR - http://www.scopus.com/inward/record.url?scp=0028203495&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028203495&partnerID=8YFLogxK

U2 - 10.1038/368150a0

DO - 10.1038/368150a0

M3 - Article

C2 - 8139658

AN - SCOPUS:0028203495

VL - 368

SP - 150

EP - 154

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6467

ER -