The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals.
Details
Serval ID
serval:BIB_747AB0288635
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals.
Journal
Journal of leukocyte biology
ISSN
1938-3673 (Electronic)
ISSN-L
0741-5400
Publication state
Published
Issued date
12/2019
Peer-reviewed
Oui
Volume
106
Number
6
Pages
1271-1283
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
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.
Keywords
Amino Acid Motifs, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Biological Evolution, CHO Cells, Conserved Sequence, Cricetulus, Fishes/genetics, Humans, Mammals/genetics, Membrane Glycoproteins/chemistry, Membrane Glycoproteins/genetics, Membrane Glycoproteins/metabolism, Mutation, Protein Binding, Protein Interaction Domains and Motifs, adhesion, evolution, sequence
Pubmed
Web of science
Create date
22/07/2019 17:42
Last modification date
20/06/2020 6:18