The MARCKS family of cellular protein kinase C substrates

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 diacy...

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Bibliographic Details
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
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)53878-3