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Involvement of the YIGSR sequence of laminin in protein tyrosine phosphorylation
Author(s) -
Bushkin-Harav I,
Littauer U.Z
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00180-x
Subject(s) - tyrosine , phosphorylation , laminin , peptide , molecular mass , chemistry , microbiology and biotechnology , tyrosine phosphorylation , biochemistry , biology , cell , enzyme
We have examined the mechanism of signaling by the 67 kDa YIGSR binding protein of laminin and its properties in neuroblastoma cells. Ligand displacement analysis showed that the interaction with the C(YIGSR) 3 ‐NH 2 peptide amide is of intermediate affinity (1.5×10 −7 M). Cross‐linking experiments with sulfo‐MBS detected an additional protein with a molecular mass of 116 kDa that binds the YIGSR sequence. Incubation of neuroblastoma cells with C(YIGSR) 3 ‐NH 2 peptide amide or antibody directed against the 67 kDa laminin binding protein induces tyrosine phosphorylation of proteins with a molecular mass ranging from 115 to 130 kDa and another heterogeneous protein group of 32 kDa.