The MARCKS family of cellular protein kinase C substrates

• Published in: The Journal of biological chemistry 1993-01, Vol.268 (3), p.1501-1504
• Main Author: BLACKSHEAR, P. J
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Humans; Intracellular Signaling Peptides and Proteins; MARCKS protein; Membrane Proteins; Molecular Sequence Data; Myristoylated Alanine-Rich C Kinase Substrate; protein kinase C; Protein Kinase C - metabolism; Proteins; Proteins - chemistry; Proteins - genetics; Proteins - metabolism; reviews; structure-activity relationships; substrates
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(18)53878-3

Stimulation of membrane polyphosphoinositol turnover is one of the most commonly employed signal transduction systems in normal physiology. The two second messengers generated by this reaction include inositol 1,4,5-trisphosphate, which can transiently elevate intracellular calcium levels, and diacylglycerols, which can activate most isoforms of protein kinase C (PKC). This review will focus on one class of PKC substrates of which the prototype is the myristoylated, alanine-rich C kinase substrate or MARCKS protein. This protein, also referred to as 87 kDa, 80 K, phosphomyristin, etc. has been employed for at least a decade as an indicator or marker for PKC activation in intact cells; early studies of this type have been reviewed previously. This review will concentrate on data that have accrued since the elucidation of the primary sequence of the protein, particularly potential structure:function relationships.