Interaction of protein 4.1 with the red cell membrane: effects of phosphorylation by protein kinase C.
Phosphorylation with endogenous protein kinase C causes the membrane skeletal protein, band 4.1, to lose its capacity to attach to one of two classes of high-affinity binding sites on the red cell membrane. These sites are the ones eliminated by proteolysis in situ of glycophorin C; the surviving type of site is located in a C-terminal peptide of the glycophorin C, retained on the membrane after proteolysis, which is also the site of attachment of p55. A synthetic peptide, comprising the 28 C-terminal residues of glycophorin C, also binds protein 4.1. Phosphorylation of the intact cells, stimulated by phorbol ester, approximately halves the retention of glycophorin C in the membrane cytoskeletons prepared from these cells and reduces the affinity of extracellular glycophorin C epitopes for their antibody.
Pinder
J C
JC
Medical Research Council Muscle and Cell Motility Unit, King's College, London, United Kingdom.
Gardner
B
B
Gratzer
W B
WB
D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006021:Glycophorins / Q000378:metabolism; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism*; D009479:Neuropeptides; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D006021:Glycophorins; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D011493:Protein Kinase C