Differential Regulation of Oncogenic and Cellular p185 by Serine/Threonine Kinases
- 1 December 1989
- journal article
- research article
- Published by Mary Ann Liebert Inc in DNA
- Vol. 8 (10) , 723-732
- https://doi.org/10.1089/dna.1989.8.723
Abstract
185c-neu is a member of a family of growth factor receptors with tyrosine kinase activity. A point mutation in the transmembrane region leads to activation of the enzymatic domain. We demonstrate that TPA (phorbol-12-myristate- 13-acetate) stimulates the phosphorylation of p185c-neu on serine and threonine residues coincident with the inhibition of its intrinsic tyrosine kinase and the proliferation of cells that express it. The tyrosine kinase activity as well as the phosphorylation pattern of serine and threonine residues of oncogenic p 185 (p185neu) and the growth of p185neu-expressing cells are not influenced by TPA. These observations indicate that the functional activity of p185c-neu can be regulated through protein kinase C (PKC) but the transmembrane point mutation present in p185neu renders it refractory to serine/threonine kinase regulation.This publication has 47 references indexed in Scilit:
- Epidermal growth factor (EGF) promotes phosphorylation at threonine-654 of the EGF receptor: possible role of protein kinase C in homologous regulation of the EGF receptor.The Journal of cell biology, 1986
- Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanismsCell, 1986
- The neu oncogene encodes an epidermal growth factor receptor-related proteinNature, 1986
- Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteinsCell, 1985
- Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogeneNature, 1984
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cellsNature, 1984
- Disappearance of Ca2+-sensitive, phospholipid-dependent protein kinase activity in phorbol ester-treated 3T3 cellsBiochemical and Biophysical Research Communications, 1984
- Identification of a calcium- and phospholipid-dependent phorbol ester binding activity in the soluble fraction of mouse tissuesBiochemical and Biophysical Research Communications, 1983
- Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptorsNature, 1979