A 42-kD Tyrosine Kinase Substrate Linked to Chromaffin Cell Secretion Exhibits an Associated MAP Kinase Activity and Is Highly Related to a 42-kD Mitogen-Stimulated Protein in Fibroblasts

The localization of the protein tyrosine kinase pp60 c-src to the plasma membrane and to the membrane of secretory vesicles in neurally derived bovine chromaffin cells has suggested that tyrosine phosphorylations may be associated with the process of secretion. In the present study we have identifie...

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Bibliographic Details
Published in:	The Journal of cell biology Vol. 110; no. 3; pp. 731 - 742
Main Authors:	Ely, Constance M., Oddie, Karen M., Litz, Julie S., Rossomando, Anthony J., Kanner, Steven B., Sturgill, Thomas W., Parsons, Sarah J.
Format:	Journal Article
Language:	English
Published:	New York, NY Rockefeller University Press 01-03-1990 The Rockefeller University Press
Subjects:	Adipocytes Adrenal Gland Neoplasms Adrenal Medulla - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Cell growth Cell Line Cell lines Cells Cells, Cultured Chromaffin cells Cultured cells Cyanogen Bromide Fibroblasts Fundamental and applied biological sciences. Psychology Gels Miscellaneous Molecular Weight Norepinephrine - metabolism Peptide Mapping Pheochromocytoma Phosphoproteins - isolation & purification Phosphorylation Phosphotyrosine plasma membranes Protein-Tyrosine Kinases - metabolism Proteins Proteins - metabolism Secretion Substrate Specificity Tyrosine - analogs & derivatives Tyrosine - analysis Tyrosine Phosphorylation Bovine Gel electrophoresis Enzyme Identification Chromaffin cell Cytosol Ion exchange chromatography Proteins Vertebrata Mammalia Enzymatic activity Protein kinase Artiodactyla Microtubule Localization Ungulata
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Summary:	The localization of the protein tyrosine kinase pp60 c-src to the plasma membrane and to the membrane of secretory vesicles in neurally derived bovine chromaffin cells has suggested that tyrosine phosphorylations may be associated with the process of secretion. In the present study we have identified two cytosolic proteins of ∼42 and 45 kD that become phosphorylated on tyrosine in response to secretagogue treatment. Phosphorylation of these proteins reached a maximum (3 min after stimulation) before maximum catecholamine release was observed (5-10 min after stimulation). Both secretion and tyrosine phosphorylation of p42 and p45 required extracellular Ca2+. Tyrosine-phosphorylated proteins of similar M r have previously been identified in 3T3-L1 adipocytes stimulated with insulin (MAP kinase; Ray, L. B., and T. W. Sturgill. 1987. Proc. Natl. Acad. Sci. USA. 84:1502-1506) and in avian and rodent fibroblasts stimulated with a variety of mitogenic agents (Cooper, J. A., D. F. Bowen-Pope, E. Raines, R. Ross, and T. Hunter. 1982. Cell. 31:263-273; Nakamura, K. D., R. Martinez, and M. J. Weber. 1983. Mol. Cell. Biol. 3:380-390). Comparisons of the secretion-associated 42-kD protein of chromaffin cells with the 42-kD protein of Swiss 3T3 fibroblasts and 3T3-L1 adipocytes provide evidence that these three proteins are highly related. This evidence includes comigration during one-dimensional SDS-PAGE, cochromatography using ion exchange and hydrophobic matrices, similar isoelectric points, identical cyanogen-bromide peptide maps, and cochromatography of MAP kinase activity with the tyrosine-phosphorylated form of pp42. This protein(s), which appears to be activated in a variety of cell types, may serve a common function, perhaps in signal transduction involving a cascade of kinases.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0021-9525 1540-8140
DOI:	10.1083/jcb.110.3.731