PUBLICATION
The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals
- Authors
- Baïsse, B., Spertini, C., Galisson, F., Smirnova, T., Spertini, O.
- ID
- ZDB-PUB-190716-4
- Date
- 2019
- Source
- Journal of Leukocyte Biology 106(6): 1271-1283 (Journal)
- Registered Authors
- Keywords
- adhesion, evolution, sequence
- MeSH Terms
-
- Humans
- Cricetulus
- Amino Acid Sequence
- Binding Sites
- Protein Binding
- Animals
- Fishes/genetics*
- Mammals/genetics*
- Membrane Glycoproteins/chemistry
- Membrane Glycoproteins/genetics*
- Membrane Glycoproteins/metabolism
- Mutation
- CHO Cells
- Conserved Sequence
- Biological Evolution*
- Protein Interaction Domains and Motifs
- Amino Acid Motifs
- Base Sequence
- PubMed
- 31302947 Full text @ J. Leukoc. Biol.
Citation
Baïsse, B., Spertini, C., Galisson, F., Smirnova, T., Spertini, O. (2019) The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals. Journal of Leukocyte Biology. 106(6):1271-1283.
Abstract
PSGL-1 is a mucin-like glycoprotein that supports, in mammals, leukocyte rolling on selectins. However, we have limited knowledge whether its function is conserved in non-mammals and how its structure adapted during evolution. To identify conserved amino acid sequences required for selectin binding, we performed multiple alignments of PSGL-1 sequences from 18 mammals, 4 birds, 3 reptiles, 1 amphibian, and 15 fishes. The amino-terminal T[D/E]PP[D/E] motif, which identifies in mammals a core-2 O-glycosylated threonine required for selectin-binding, is partially conserved in some fishes (e.g., T. rubripes) and birds (e.g., G. gallus), however, most non-mammals do not display it. The sulfated tyrosine residues of human PSGL-1, which bind L- and P-selectin, are not observed in non-mammals, suggesting that they are dispensable for selectin-binding or that other amino acids play their role. A mucin-like domain is present in all species. Interestingly, the alignment of cytoplasmic sequences of non-mammals reveals the conservation of ezrin/radixin/moesin binding site and two new motifs (M1 and M2). To examine the conservation of PSGL-1 function, we cloned PSGL-1 cDNA sequences of zebrafish and fugu, and established their cross-reactivity with human selectins under flow conditions. Importantly, deleting the well-conserved M1 motif strongly decreased PSGL-1 expression at leukocyte surface and induced retention of the precursor molecule in the endoplasmic reticulum, indicating that M1 motif provides a signal required to export PSGL-1 precursors to the Golgi complex. These data show for the first time the conservation of PSGL-1 function from fishes to mammals and reveal the function of a new motif.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping