MARCKS

MARCKS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1IWQ
Identifiers
Aliases	MARCKS, 80K-L, MACS, PKCSL, PRKCSL, myristoylated alanine rich protein kinase C substrate
External IDs	OMIM: 177061; MGI: 96907; HomoloGene: 135584; GeneCards: MARCKS; OMA:MARCKS - orthologs
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6q21 Start 113,857,345 bp[1] End 113,863,475 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 B1|10 19.49 cM Start 37,009,371 bp[2] End 37,014,916 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence buccal mucosa cell mucosa of colon mucosa of sigmoid colon internal globus pallidus trigeminal ganglion bronchial epithelial cell mucosa of paranasal sinus superior vestibular nucleus Top expressed in Rostral migratory stream medial ganglionic eminence dermis Gonadal ridge abdominal wall vas deferens fossa external carotid artery human fetus left lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calmodulin binding actin binding protein kinase C binding identical protein binding actin filament binding Cellular component cytoplasm germinal vesicle centrosome membrane focal adhesion cell cortex actin cytoskeleton extracellular exosome cytoskeleton plasma membrane actin filament bundle Biological process regulation of insulin secretion actin filament bundle assembly protein homooligomerization actin crosslink formation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4082 17118 Ensembl ENSG00000277443 ENSMUSG00000069662 UniProt P29966 P26645 RefSeq (mRNA) NM_002356 NM_008538 RefSeq (protein) NP_002347 NP_032564 Location (UCSC) Chr 6: 113.86 – 113.86 Mb Chr 10: 37.01 – 37.01 Mb PubMed search [3] [4]
Wikidata
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Myristoylated alanine-rich C-kinase substrate is a protein that in humans is encoded by the MARCKS gene.^[5][6][7] It plays important roles in cell shape, cell motility, secretion, transmembrane transport, regulation of the cell cycle, and neural development.^[8] Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin. It is also the name of a protein family, of which MARCKS is the most studied member. They are intrinsically disordered proteins, with an acidic pH, with high proportions of alanine, glycine, proline, and glutamic acid. They are membrane-bound through a lipid anchor at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca²⁺/calmodulin and protein kinase C. In their unphosphorylated form, they bind to actin filaments, causing them to crosslink, and sequester acidic membrane phospholipids such as PIP2.

The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.^[7] MARCKS has been shown to regulate the Toll-like receptor pathway in macrophages^[9]

Interactions

MARCKS has been shown to interact with TOB1^[10] and with NMT2.^[11]

References

Further reading