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Src regulated by C-terminal phosphorylation is monomeric

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Src regulated by C-terminal phosphorylation is monomeric

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Williams, J. C. Wierenga, R. K. Courtneidge, S. A. Neubauer, G. Weijland, A. Superti-furga, G.
Description	Author Affiliation: Weijland A ( European Molecular Biology Laboratory, Heidelberg, Germany.);
Abstract	The activity of the c-Src protein tyrosine kinase is regulated by phosphorylation of a tyrosine residue (Tyr-527) in the C-terminal tail of the molecule. Phosphorylation of Tyr-527 promotes association of the tail with the SH2 domain and a concomitant reduction of the enzymatic activity of Src. We asked the question whether regulation by C-terminal phosphorylation was accompanied by a change in the quaternary structure of the enzyme or if it occurred within a monomeric form of Src. For this purpose we purified to homogeneity a chicken Src form lacking the unique domain from Schizosaccharomyces pombe cells. The cells were engineered to express Src along with Csk, a protein kinase able to phosphorylate Tyr-527 efficiently. Mass spectrometric analysis showed that purified Src was homogeneously phosphorylated at Tyr-527. The enzyme was in the regulated form, because it could be activated by a phosphorylated peptide able to bind the SH2 domain with high affinity. Using gel filtration chromatography, dynamic light scattering, and ultracentrifugation, we found that the regulated form of Src was a monomer. We have obtained crystals diffracting to 2.4 A with space group P2(1)2(1)2(1) and one molecule per asymmetric unit, in agreement with the monomeric state. These results indicate that the structural rearrangements of regulated Src are of an intramolecular nature.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Proto-Oncogene Proteins Pp60(c-src) Chemistry Amino Acid Sequence Enzyme Activation Mass Spectrometry Molecular Sequence Data Phosphorylation Metabolism Schizosaccharomyces Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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