Role of actin binding protein phosphorylation in platelet cytoskeleton assembly.
Actin binding protein from human blood platelets is shown to exist in the resting platelet as a phosphorylated protein and contains two residues of phosphate per 260,000 kd. Removal of one-half of these residues with E. coli alkaline phosphatase results in the loss of its ability to crosslink F-actin into a low speed sedimentable complex (its cytoskeleton) and to bind to an F-actin affinity column. Thus, phosphorylation-dephosphorylation of ABP may be an important regulatory mechanism by which the platelet regulates its shape via its cytoskeletal structure.
D000199:Actins / Q000097:blood* / Q000302:isolation & purification; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D001792:Blood Platelets / Q000378:metabolism*; D002352:Carrier Proteins / Q000097:blood*; D004926:Escherichia coli / Q000201:enzymology; D018260:Gelsolin; D006801:Humans; D008840:Microfilament Proteins; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits
D000199:Actins; D002352:Carrier Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; C016953:brevin; D000469:Alkaline Phosphatase