(Q28289277)

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Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells

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Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells (English)

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author name string

S L Swierczynski

1

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P J Blackshear

2

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language of work or name

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publication date

20 September 1996

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Journal of Biological Chemistry

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271

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38

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23424-30

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Turnover of Inositol Phospholipids and Signal Transduction

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Studies and perspectives of protein kinase C.

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The MARCKS brothers: a family of protein kinase C substrates

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MARCKS deficiency in mice leads to abnormal brain development and perinatal death

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Stimulus-dependent myristoylation of a major substrate for protein kinase C

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A major myristylated substrate of protein kinase C and protein kinase C itself are differentially regulated during murine B- and T-lymphocyte development and activation

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Molecular cloning, sequence, and expression of a cDNA encoding the chicken myristoylated alanine-rich C kinase substrate (MARCKS).

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Molecular cloning, characterization, and expression of a cDNA encoding the "80- to 87-kDa" myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C.

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The biology and enzymology of eukaryotic protein acylation

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Chromosomal mapping of the human (MACS) and mouse (Macs) genes encoding the MARCKS protein

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Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing

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Regulation of peptide-calmodulin complexes by protein kinase C in vivo

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MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin

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Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin

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21 January 2018

Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions

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Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E-115 neuroblastoma cells.

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Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia

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Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane

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Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals

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Epitope tagging and protein surveillance

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DNA sequencing with chain-terminating inhibitors

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Altered growth regulation and enhanced tumorigenicity of NIH 3T3 fibroblasts transfected with protein kinase C-I cDNA.

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Mutant p53 tumor suppressor alleles release ras-induced cell cycle growth arrest

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Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation

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Specific association of the proto-oncogene product pp60c-src with an intracellular organelle, the PC12 synaptic vesicle

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The ADP/ATP carrier is the 32-kilodalton receptor for an NH2-terminally myristylated src peptide but not for pp60src polypeptide

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The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions

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Molecular cloning and characterization of a novel human diacylglycerol kinase zeta

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Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit

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Identification of a 32K plasma membrane protein that binds to the myristylated amino-terminal sequence of p60v-src

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21 January 2018

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10.1074/JBC.271.38.23424

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