| First Author | Blackshear PJ | Year | 1992 |
| Journal | J Biol Chem | Volume | 267 |
| Issue | 19 | Pages | 13540-6 |
| PubMed ID | 1618855 | Mgi Jnum | J:1361 |
| Mgi Id | MGI:49888 | Doi | 10.1016/s0021-9258(18)42245-4 |
| Citation | Blackshear PJ, et al. (1992) Characteristics of the F52 protein, a MARCKS homologue. J Biol Chem 267(19):13540-6 |
| abstractText | A recently cloned mouse cDNA designated F52 encodes a putative protein with striking sequence similarity to the MARCKS protein, a major cellular substrate for protein kinase C (PKC). Major regions of sequence similarity include the amino-terminal myristoylation consensus sequence and the central calmodulin-binding/PKC phosphorylation site domain. The F52 protein was expressed in Escherichia coli with apparent M(r) 50,000; it was a substrate for PKC and comigrated on two-dimensional electrophoresis with a myristoylated protein whose phosphorylation was stimulated by phorbol 12-myristate 13-acetate in mouse neuroblastoma cells. The F52 protein also was myristoylated in E. coli by co-expression with N-myristoyltransferase. A 24-amino acid peptide derived from the protein's phosphorylation site domain was a good substrate for PKC; like the cognate MARCKS peptide, it was phosphorylated with high affinity (S0.5 = 173 nM) and positive cooperativity (KH = 5.4). The F52 peptide also bound calmodulin with high affinity (Kd = less than 3 nM); this binding could be disrupted by phosphorylation of the peptide with PKC, with a half-time of 8 min. The F52 protein is clearly a member of the MARCKS family as defined by primary sequence; in addition, the two proteins share several key attributes that may be functionally important. |
