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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Simons, P. C. Articles by Elias, L. Search for Related Content PubMed PubMed Citation Articles by Simons, P. C. Articles by Elias, L. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  The 47-kD fragment of talin is a substrate for protein kinase P PC Simons and L Elias University of New Mexico Cancer Center, Albuquerque 87131-5636. This laboratory has been characterizing protein serine/threonine kinase reactions of hematopoietic tissues, whose most distinguishing characteristics in vitro are stimulation with vesicular phosphatidyl glycerol, and the ability to function using Mn2+ as the sole divalent cation. The major protein substrates are a 73-kD protein and a protein migrating near ovalbumin on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The 47-kD protein was partially purified from cells harvested by leukapheresis from a patient with acute myelogenous leukemia, using ammonium sulfate precipitation and ion exchange chromatography. This partially purified ion-exchange fraction contained an endogenous kinase activity with characteristics similar to those we previously described of protein kinase P (protein kinase, phospholipid- stimulable: PK-P), but not typical of any form of protein kinase C (PK- C). With longer phosphorylation, the 47-kD band showed increasingly lower mobility demonstrable both by Coomassie blue staining and autoradiography, suggesting both that it was multiply phosphorylated, and that the excisable band was pure. The protein was thus eluted from preparative gel slices and digested with endoproteinase lys C. Sequence data from the fragments identified the protein as the 47-kD calpain fragment of talin, a protein found in focal adhesion plaques and some cell-cell contacts. PK-C phosphorylated the 47-kD protein, as has been reported previously, and phosphopeptide mapping disclosed a similar pattern of phosphorylation using either PK-C or the endogenous activity. The 47-kD protein labeled with the endogenous kinase contained predominantly phosphoserine, with some phosphothreonine and a trace of phosphotyrosine. Intact, purified talin was also phosphorylated by PK-P in a phospholipid-stimulable manner, but at 1/20 the rate of the 47-kD fragment. Volume 82, Issue 11, pp. 3343-3349, 12/01/1993 Copyright © 1993 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. Hayashi, Y. Koshihara, H. Ishibashi, S. Yamamoto, S. Tsubuki, T. C. Saido, S. Kawashima, and M. Inomata Involvement of Calpain in Osteoclastic Bone Resorption J. Biochem., March 1, 2005; 137(3): 331 - 338. [Abstract] [Full Text] [PDF] S. F. Pietromonaco, P. C. Simons, A. Altman, and L. Elias Protein Kinase C-theta Phosphorylation of Moesin in the Actin-binding Sequence J. Biol. Chem., March 27, 1998; 273(13): 7594 - 7603. [Abstract] [Full Text] [PDF] C Albiges-Rizo, P Frachet, and M. Block Down regulation of talin alters cell adhesion and the processing of the alpha 5 beta 1 integrin J. Cell Sci., January 10, 1995; 108(10): 3317 - 3329. [Abstract] [PDF]

	Copyright © 1993 by American Society of Hematology         Online ISSN: 1528-0020