Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148
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Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148. / Whiteford, James R; Xian, Xiaojie; Chaussade, Claire; Vanhaesebroeck, Bart; Nourshargh, Sussan; Couchman, John R.
In: Molecular Biology of the Cell, Vol. 22, No. 19, 2011, p. 3609-24.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148
AU - Whiteford, James R
AU - Xian, Xiaojie
AU - Chaussade, Claire
AU - Vanhaesebroeck, Bart
AU - Nourshargh, Sussan
AU - Couchman, John R
PY - 2011
Y1 - 2011
N2 - Syndecan-2 is a heparan sulfate proteoglycan that has a cell adhesion regulatory domain contained within its extracellular core protein. Cell adhesion to the syndecan-2 extracellular domain (S2ED) is ß1 integrin dependent; however, syndecan-2 is not an integrin ligand. Here the protein tyrosine phosphatase receptor CD148 is shown to be a key intermediary in cell adhesion to S2ED, with downstream ß1 integrin-mediated adhesion and cytoskeletal organization. We show that S2ED is a novel ligand for CD148 and identify the region proximal to the transmembrane domain of syndecan-2 as the site of interaction with CD148. A mechanism for the transduction of the signal from CD148 to ß1 integrins is elucidated requiring Src kinase and potential implication of the C2ß isoform of phosphatidylinositol 3 kinase. Our data uncover a novel pathway for ß1 integrin-mediated adhesion of importance in cellular processes such as angiogenesis and inflammation.
AB - Syndecan-2 is a heparan sulfate proteoglycan that has a cell adhesion regulatory domain contained within its extracellular core protein. Cell adhesion to the syndecan-2 extracellular domain (S2ED) is ß1 integrin dependent; however, syndecan-2 is not an integrin ligand. Here the protein tyrosine phosphatase receptor CD148 is shown to be a key intermediary in cell adhesion to S2ED, with downstream ß1 integrin-mediated adhesion and cytoskeletal organization. We show that S2ED is a novel ligand for CD148 and identify the region proximal to the transmembrane domain of syndecan-2 as the site of interaction with CD148. A mechanism for the transduction of the signal from CD148 to ß1 integrins is elucidated requiring Src kinase and potential implication of the C2ß isoform of phosphatidylinositol 3 kinase. Our data uncover a novel pathway for ß1 integrin-mediated adhesion of importance in cellular processes such as angiogenesis and inflammation.
KW - Animals
KW - Antigens, CD29
KW - Cell Adhesion
KW - Cell Line
KW - Cytoskeleton
KW - Fibroblasts
KW - Gene Expression Regulation
KW - Humans
KW - Inflammation
KW - Jurkat Cells
KW - Ligands
KW - Lung
KW - Mice
KW - Neovascularization, Physiologic
KW - Phosphatidylinositol 3-Kinase
KW - Protein Interaction Domains and Motifs
KW - RNA, Small Interfering
KW - Rats
KW - Receptor-Like Protein Tyrosine Phosphatases, Class 3
KW - Signal Transduction
KW - Syndecan-2
KW - src-Family Kinases
U2 - 10.1091/mbc.E11-02-0099
DO - 10.1091/mbc.E11-02-0099
M3 - Journal article
C2 - 21813734
VL - 22
SP - 3609
EP - 3624
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 19
ER -
ID: 38429768