PMID: 9539159Apr 16, 1998Paper

Involvement of the YIGSR sequence of laminin in protein tyrosine phosphorylation

FEBS Letters
I Bushkin-Harav, U Z Littauer

Abstract

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-NH2 peptide amide is of intermediate affinity (1.5 x 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-NH2 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.

References

Oct 1, 1992·Current Opinion in Cell Biology·Y Yamada, H K Kleinman
Jul 5, 1991·Science·S DavisG D Yancopoulos
Jan 1, 1991·The Journal of Clinical Investigation·E Ruoslahti
Jan 1, 1990·The Journal of Cell Biology·B ClémentY Yamada
Oct 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·U M WewerR Albrechtsen
Oct 1, 1989·Current Opinion in Cell Biology·H K Kleinman, B S Weeks
Apr 1, 1989·European Journal of Biochemistry·R Timpl
Jul 31, 1989·Biochemical and Biophysical Research Communications·G C SephelH K Kleinman
Sep 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·H K YowL B Chen
Jan 1, 1988·Annual Review of Biochemistry·M A Ferguson, A F Williams
Jan 1, 1982·Methods in Enzymology·R Timpl
Jan 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·V P TerranovaL A Liotta
Apr 14, 1995·Science·E A Clark, J S Brugge
Jun 2, 1995·The Journal of Biological Chemistry·I Bushkin-HaravU Z Littauer
Apr 1, 1994·Molecular Biology of the Cell·M A Schwartz, D E Ingber

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Citations

Apr 18, 2008·Developmental Neurobiology·Elyanne M RatcliffeMichael D Gershon
Dec 25, 2012·Cell Adhesion & Migration·Yamato KikkawaJennifer E Koblinski
Oct 31, 2000·Microscopy Research and Technique·S Ghosh, M S Stack
Nov 19, 2010·Regenerative Medicine·Swati Pradhan, Mary C Farach-Carson
Jul 24, 2002·News in Physiological Sciences : an International Journal of Physiology Produced Jointly by the International Union of Physiological Sciences and the American Physiological Society·Torsten Gloe, Ulrich Pohl
May 14, 2005·Cancer Letters·Vered Givant-HorwitzReuven Reich
Nov 3, 2005·Biochemical and Biophysical Research Communications·Kwanghee KimBarbara J Ballermann

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