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1. Full Text Suppression of chemotaxis by SSeCKS via scaffolding of phosphoinositol phosphates and the recruitment of the Cdc42 GEF, frabin, to the leading edge
by Ko, Hyun-Kyung and Guo, Li-Wu and Su, Bing and Gao, Lingqiu and Gelman, Irwin H
PLoS ONE, ISSN 1932-6203, 10/2014, Volume 9, Issue 10, pp. e111534 - e111534
Chemotaxis is controlled by interactions between receptors, Rho-family GTPases, phosphatidylinositol 3-kinases, and cytoskeleton remodeling proteins. We... 
MEMBRANE INTERACTIONS | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | ACTIN-CYTOSKELETON | PROSTATE-CANCER | CELL INVASION | ONCOGENIC TRANSFORMATION | PLASMA-MEMBRANE | C-KINASE SUBSTRATE | CYTOSKELETAL ARCHITECTURE | Phosphatidylinositol Phosphates - metabolism | Humans | Molecular Sequence Data | cdc42 GTP-Binding Protein - metabolism | A Kinase Anchor Proteins - chemistry | Cell Cycle Proteins - chemistry | Guanine Nucleotide Exchange Factors - metabolism | src-Family Kinases - metabolism | Female | Microfilament Proteins - metabolism | A Kinase Anchor Proteins - metabolism | Fibroblasts - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Signal Transduction | Mice, Inbred C57BL | Cell Cycle Proteins - metabolism | Chemotaxis | Mice, Knockout | Phenotype | Animals | Pseudopodia - metabolism | Embryo, Mammalian - cytology | Models, Biological | Cell Line, Tumor | Phosphates | Membrane lipids | Blood lipids | G proteins | Muscle proteins | Cdc42 protein | Enrichment | GTP | Correlation | Protein kinase C | Motility | AKT protein | Phospholipids | Metastasis | Phosphatidylinositol 4,5-diphosphate | Kinases | Guanine | Cell adhesion & migration | Recruitment | Fibers | Metastases | Proteins | Morphogenesis | Receptors | Actin | Fibroblasts | Genetics | Inhibition | Trends | Guanine nucleotide exchange factor | Active control | Growth factors | Binding | Alanine | Phosphatidylinositol 3,4,5-triphosphate | Pseudopodia | Rac1 protein | Embryo fibroblasts | Embryos | Substrates | 1-Phosphatidylinositol 3-kinase | Scaffolding | Cytoskeleton | MARCKS protein | Cancer | Tips | Index Medicus
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2. Full Text Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-22: Direct involvement of protein myristoylation in calmodulin-target protein interaction
by Takasaki, Akihiko and Hayashi, Nobuhiro and Matsubara, Mamoru and Yamauchi, Emiko and Taniguchi, Hisaaki
Journal of Biological Chemistry, ISSN 0021-9258, 04/1999, Volume 274, Issue 17, pp. 11848 - 11853
Various proteins in the signal transduction pathways as well as those of viral origin have been shown to be myristoylated, Although the modification is often... 
RECOVERIN | CATALYTIC SUBUNIT | BOVINE BRAIN | MARCKS | COMPLEX | PEPTIDES | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | MYRISTYLATION | N-MYRISTOYLATION | Cytoskeletal Proteins | Recombinant Proteins - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Phosphorylation | Calmodulin - metabolism | Humans | Models, Molecular | Molecular Sequence Data | Rats | Recombinant Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | Brain - metabolism | Nerve Tissue Proteins - metabolism | Sequence Homology, Amino Acid | Myristic Acid - metabolism | Animals | Protein Kinase C - metabolism | Protein Conformation | Calmodulin - chemistry | Binding Sites
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3. Full Text Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling Pathway
by Ziemba, Brian P and Burke, John E and Masson, Glenn and Williams, Roger L and Falke, Joseph J
Biophysical Journal, ISSN 0006-3495, 04/2016, Volume 110, Issue 8, pp. 1811 - 1825
In chemotaxing ameboid cells, a complex leading-edge signaling circuit forms on the cytoplasmic leaflet of the plasma membrane and directs both actin and... 
PROTEIN-KINASE-C | BIOPHYSICS | PHOSPHOINOSITIDE-DEPENDENT KINASE | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | LEADING-EDGE | SUBSTRATE MARCKS | ELECTROSTATIC SEQUESTRATION | PHOSPHOLIPASE C-BETA ACTIVITY | ACTIVATION MECHANISM | CALMODULIN-BINDING | MEMBRANE-PROTEINS | Protein Kinase C-alpha - metabolism | Signal Transduction | Calcium - metabolism | Myristoylated Alanine-Rich C Kinase Substrate | Humans | Models, Molecular | Peptide Fragments - pharmacology | Intracellular Signaling Peptides and Proteins - metabolism | Phosphatidylinositol 3-Kinases - metabolism | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Membrane Proteins - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Protein Conformation | Cell Membrane - metabolism | Membrane Proteins - metabolism | Lipid Bilayers - metabolism | Peptides | Microbiology | Analysis | Molecular biology | Muscle proteins | Binding proteins | Protein kinases | Protein binding | Membranes
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4. Full Text Upregulation of MARCKS in kidney cancer and its potential as a therapeutic target
by Chen, C.-H and Fong, L.W.R and Yu, E and Wu, R and Trott, J.F and Weiss, R.H
Oncogene, ISSN 0950-9232, 06/2017, Volume 36, Issue 25, pp. 3588 - 3598
Targeted therapeutics, such as those abrogating hypoxia inducible factor (HIF)/vascular endothelial growth factor signaling, are initially effective against... 
Up-Regulation | Kidney Neoplasms - genetics | TOR Serine-Threonine Kinases - metabolism | Myristoylated Alanine-Rich C Kinase Substrate | Humans | Middle Aged | Gene Expression Regulation, Neoplastic | Cell Survival - genetics | Male | Kidney Neoplasms - metabolism | Proto-Oncogene Proteins c-akt - genetics | TOR Serine-Threonine Kinases - genetics | Adult | Female | Carcinoma, Renal Cell - drug therapy | Proto-Oncogene Proteins c-akt - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Cell Survival - drug effects | Carcinoma, Renal Cell - pathology | Membrane Proteins - genetics | Intracellular Signaling Peptides and Proteins - biosynthesis | Xenograft Model Antitumor Assays | Carcinoma, Renal Cell - metabolism | Membrane Proteins - biosynthesis | Animals | Mice, Nude | Cell Line, Tumor | Kidney Neoplasms - pathology | Aged | Mice | Phenylurea Compounds - pharmacology | Pyridines - pharmacology | Kidney Neoplasms - drug therapy | Molecular targeted therapy | Care and treatment | Transcription factors | Kidney cancer | Innovations | Development and progression | Genetic aspects | Health aspects | Phosphotransferases | TOR protein | Cell proliferation | Phosphorylation | Protein kinase C | Transcription | Leukocyte migration | AKT protein | Genomes | Drug resistance | Kinases | Cancer therapies | Angiogenesis | Allografts | Nephrectomy | Xenografts | Vascular endothelial growth factor | Alanine | Cell survival | Survival | Protein kinase | Cell lines | Hypoxia | MARCKS protein | Cell migration | Clear cell-type renal cell carcinoma | Kidney transplantation
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5. Full Text Taurolithocholate‐induced MRP2 retrieval involves MARCKS phosphorylation by protein kinase Cϵ in HUH‐NTCP Cells
by Schonhoff, Christopher M and Webster, Cynthia R. L and Anwer, M. Sawkat
Hepatology, ISSN 0270-9139, 07/2013, Volume 58, Issue 1, pp. 284 - 292
Taurolithocholate (TLC) acutely inhibits the biliary excretion of multidrug‐resistant associated protein 2 (Mrp2) substrates by inducing Mrp2 retrieval from... 
CONJUGATE EXPORT PUMP | NA+/TAUROCHOLATE COTRANSPORT | DEPENDENT TRANSLOCATION | ESTRADIOL 17-BETA-D-GLUCURONIDE-INDUCED CHOLESTASIS | SIGNALING PATHWAY | RAT HEPATOCYTE COUPLETS | INTESTINAL EPITHELIA | SUBSTRATE MARCKS | PKC-EPSILON | GASTROENTEROLOGY & HEPATOLOGY | CANALICULAR MEMBRANES | Protein Kinase C-delta - physiology | Animals | Myristoylated Alanine-Rich C Kinase Substrate | Humans | Multidrug Resistance-Associated Proteins - drug effects | Cell Line, Tumor | Rats | Male | Intracellular Signaling Peptides and Proteins - metabolism | Membrane Proteins - metabolism | Multidrug Resistance-Associated Proteins - metabolism | Taurolithocholic Acid - metabolism | DN-PKCε | cAMP | PMA | HuH-NTCP cells | Phosphorylation deficient MARCKS
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6. Full Text Hts, the Drosophila homologue of adducin, physically interacts with the transmembrane receptor golden goal to guide photoreceptor axons
by Ohler, Stephan and Hakeda‐Suzuki, Satoko and Suzuki, Takashi
Developmental Dynamics, ISSN 1058-8388, 01/2011, Volume 240, Issue 1, pp. 135 - 148
Neurons steer their axons towards their proper targets during development. Molecularly, a number of guidance receptors have been identified. The transmembrane... 
growth cone cytoskeleton | photoreceptor axon guidance | Drosophila visual system | Growth cone cytoskeleton | Photoreceptor axon guidance | PROTEIN-KINASE-C | ANATOMY & MORPHOLOGY | DEVELOPMENTAL BIOLOGY | GUIDANCE | LI-TAI-SHAO | ERYTHROCYTE ADDUCIN | ALPHA-SPECTRIN | GROWTH CONE MOTILITY | MARCKS-RELATED DOMAIN | OOGENESIS | BRAIN SPECTRIN | SPECTRIN-ACTIN COMPLEXES | Axons - physiology | Drosophila Proteins - metabolism | Cell Movement - genetics | Drosophila - physiology | Sequence Homology | Drosophila Proteins - physiology | Membrane Proteins - physiology | Protein Multimerization - genetics | Membrane Proteins - metabolism | Receptors, Cell Surface - physiology | Eye Proteins - genetics | Drosophila - genetics | Calmodulin-Binding Proteins - genetics | Animals, Genetically Modified | Membrane Proteins - genetics | Cells, Cultured | Axons - metabolism | Calmodulin-Binding Proteins - physiology | Receptors, Cell Surface - metabolism | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | Protein Structure, Tertiary - genetics | Drosophila Proteins - chemistry | Animals | Eye Proteins - metabolism | Pseudopodia - metabolism | Models, Biological | Photoreceptor Cells - metabolism | Pseudopodia - genetics | Eye Proteins - physiology | Drosophila - metabolism | Drosophila Proteins - genetics | Pseudopodia - physiology | Photoreceptor Cells - physiology | Protein Binding - physiology | Protein Structure, Tertiary - physiology | Receptors, Cell Surface - genetics
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7. Full Text Fibroblast Migration Is Regulated by Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Protein
by Ott, Laura E and Sung, Eui Jae and Melvin, Adam T and Sheats, Mary K and Haugh, Jason M and Adler, Kenneth B and Jones, Samuel L
PLoS ONE, ISSN 1932-6203, 06/2013, Volume 8, Issue 6, p. e66512
Myristoylated alanine-rich C-kinase substrate (MARCKS) is a ubiquitously expressed substrate of protein kinase C (PKC) that is involved in reorganization of... 
IN-VITRO | MYOBLAST MIGRATION | INTEGRIN ACTIVATION | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | FILAMENT CROSS-LINKING | SUBCELLULAR-DISTRIBUTION | SIGNALING PATHWAY | MULTIDISCIPLINARY SCIENCES | NEUTROPHIL CHEMOTAXIS | CELL-PROLIFERATION | GROWTH-FACTOR | Phosphorylation | Myristoylated Alanine-Rich C Kinase Substrate | Intracellular Signaling Peptides and Proteins - metabolism | Chemotaxis - drug effects | Fibronectins - metabolism | Collagen - metabolism | Animals | Chemotaxis - physiology | Membrane Proteins - physiology | Fibroblasts - cytology | Membrane Proteins - metabolism | Mice | Intracellular Signaling Peptides and Proteins - physiology | Proto-Oncogene Proteins c-akt - metabolism | Proto-Oncogene Proteins c-sis - pharmacology | 3T3 Cells | Amino acids | Platelet-derived growth factor | Peptides | Muscle proteins | Protein kinases | Cell proliferation | Veterinary colleges | Protein kinase C | AKT protein | Kinases | Myristoylation | Cell adhesion & migration | Proteins | Actin | Rodents | Fibroblasts | Attenuation | Inhibition | Function analysis | Alanine | Genetic structure | Chemotaxis | Platelet-derived growth factor BB | Substrates | 1-Phosphatidylinositol 3-kinase | Wounding | Signaling | Cytoskeleton | MARCKS protein | Cell migration | Structure-function relationships
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8. Full Text MARCKS phosphorylation by PKC strongly impairs cell polarity in the chick neural plate
by Aparicio, Gonzalo and Arruti, Cristina and Zolessi, Flavio R
genesis, ISSN 1526-954X, 04/2018, Volume 56, Issue 4, pp. e23104 - n/a
Summary Neurulation involves a complex coordination of cellular movements that are in great part based on the modulation of the actin cytoskeleton. MARCKS, an... 
actin filaments | neural tube | neuroepithelium | cell extrusion | chick embryo | neurulation | PROTEIN-KINASE-C | ZEBRAFISH | SUBSTRATE PROTEIN | NEUROEPITHELIAL CELLS | DEVELOPMENTAL BIOLOGY | TUBE CLOSURE | SHAPE | EMBRYO | GENETICS & HEREDITY | MICE | BINDING | Phosphorylation | Actin Cytoskeleton - metabolism | Protein Kinase C - physiology | Signal Transduction | Actins - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Neurulation - genetics | Neural Plate - metabolism | Chick Embryo | Neurulation - physiology | Chickens - metabolism | Animals | Carrier Proteins - metabolism | Myristoylated Alanine-Rich C Kinase Substrate - physiology | Protein Kinase C - metabolism | Cell Polarity - physiology | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Myristoylated Alanine-Rich C Kinase Substrate - metabolism | Binding proteins | Muscle proteins | Actin | Protein binding | Frogs | Protein kinase C | Gastrulation | Actomyosin | Activation | Embryos | Substrates | Defects | Neural tube | Polarity | Cytoskeleton | Extrusion | Neural plate | MARCKS protein | Coordination compounds | Cytoplasm
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9. Full Text B-cell deficiency and severe autoimmunity caused by deficiency of protein kinase C δ
by Salzer, Elisabeth and Salzer, Elisabeth and Santos-Valente, Elisangela and Santos-Valente, Elisangela and Klaver, Stefanie and Klaver, Stefanie and Ban, Sol A and Ban, Sol A and Emminger, Wolfgang and Emminger, Wolfgang and Prengemann, Nina Kathrin and Prengemann, Nina Kathrin and Garncarz, Wojciech and Garncarz, Wojciech and Müllauer, Leonhard and Müllauer, Leonhard and Kain, Renate and Kain, Renate and Boztug, Heidrun and Boztug, Heidrun and Heitger, Andreas and Heitger, Andreas and Arbeiter, Klaus and Arbeiter, Klaus and Eitelberger, Franz and Eitelberger, Franz and Seidel, Markus G and Seidel, Markus G and Holter, Wolfgang and Holter, Wolfgang and Pollak, Arnold and Pollak, Arnold and Pickl, Winfried F and Pickl, Winfried F and Förster-Waldl, Elisabeth and Förster-Waldl, Elisabeth and Boztug, Kaan and Boztug, Kaan
Blood, ISSN 0006-4971, 2013, Volume 121, Issue 16, pp. 3112 - 3116
Primary B-cell disorders comprise a heterogeneous group of inherited immunodeficiencies, often associated with autoimmunity causing significant morbidity. The... 
MARCKS | GENE | DISEASE | PLCG2 | CTLA4 | POLYMORPHISM | HEMATOLOGY | IMMUNODEFICIENCY | Autoimmunity | Immunologic Deficiency Syndromes - pathology | Immunologic Deficiency Syndromes - therapy | Humans | Immunophenotyping | Male | Protein Kinase C-delta - immunology | Immunoglobulin M - immunology | B-Lymphocytes - immunology | Immunoglobulin G - immunology | Pedigree | Immunologic Deficiency Syndromes - genetics | Adult | Female | Polymorphism, Single Nucleotide | B-Lymphocytes - pathology | Mutation | Immunologic Deficiency Syndromes - immunology | Protein Isoforms - immunology | Child | Protein Kinase C-delta - genetics | B-Lymphocytes - metabolism | Antigens, CD19 - immunology | Protein Isoforms - genetics | Immunobiology
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10. Full Text Construction and analysis of the protein-protein interaction networks based on gene expression profiles of Parkinson's Disease
by Rakshit, Hindol and Rakshit, Hindol and Rathi, Nitin and Rathi, Nitin and Roy, Debjani and Roy, Debjani
PLoS ONE, ISSN 1932-6203, 08/2014, Volume 9, Issue 8, p. e103047
Background: Parkinson's Disease (PD) is one of the most prevailing neurodegenerative diseases. Improving diagnoses and treatments of this disease is essential,... 
PLATFORM | GENOMIC DATA | DATABASE | PHOSPHORYLATION | ANNOTATION | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | COMPLEXES | REPRESENTATION | RESOURCE | TOOL | Substantia Nigra - pathology | Humans | Transcriptome | Gene Expression Profiling | Parkinson Disease - genetics | Substantia Nigra - metabolism | Protein Interaction Mapping | Protein Interaction Maps | Brain - metabolism | Proteins - genetics | Proteins - metabolism | Proteomics | Brain - pathology | Parkinson Disease - metabolism | Brain | Networks | Science education | Cerebral cortex | Parkinson's disease | Modules | Substantia nigra | Genes | Parkinsons disease | Schizophrenia | Bipolar disorder | Genomes | Kinases | Data bases | Proteins | Cortex (frontal) | Research methodology | Bioindicators | Movement disorders | Dopamine | Neurodegenerative diseases | Therapeutic applications | Medical treatment | Cortex | Gene expression | Nodes | Neurological diseases | b-Arrestin | Neurotransmitters | Protein arrays | Brain research | DNA microarrays | Acids | Neural networks | Biomarkers | MARCKS protein | Mutation | Alzheimers disease | Protein interaction
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