Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
CD116/GM-CSFR has been preferentially associated with M4, M5 subtype of AML but is not specific. The cluster of differentiation (cluster of designation) (often abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules present on white blood cells initially but found in almost any kind of cell of the body, providing targets for immunophenotyping of cells. Physiologically, CD molecules can act in numerous ways, often acting as receptors or ligands (the molecule that activates a receptor) important to the cell. A signal cascade is usually initiated, altering the behavior of the cell (see cell signaling). Some CD proteins do not play a role in cell signaling, but have other functions, such as cell adhesion. CD116/GM-CSFR is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. The encoded protein is a member of the cytokine family of receptors. CD116/GM-CSFR is found in the pseudoautosomal region (PAR) of the X and Y chromosomes.
Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit α (CSF2RA) is a single-pass type I membrane protein which belongs to the type I cytokine receptor family of Type 5 subfamily. The CSF2RA gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes with some of the isoforms being membrane-bound and others being soluble. CSF2RA is a low affinity receptor for granulocyte-macrophage colony-stimulating factor. CSF2RA transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells. Defects in CSF2RA are the cause of pulmonary surfactant metabolism dysfunction type 4 (SMDP4).
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tail. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.
Kappa-Casein (CSN3) is a secreted protein that belongs to the Kappa-Casein family. CSN3 exists in heteromultimers that are composed of alpha-s 1casein and kappa casein linked by disulfide bonds. CSN3 is involved in a number of important physiological processes. In the gut, CSN3 protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of digestion, prevention of neonate hypersensitivity to ingested proteins, and inhibition of gastric pathogens. Kappa-casein also stabilizes micelle formation, preventing casein precipitation in milk.
Casein kinase I isoform alpha, also known as CKI-alpha, CK1 and CSNK1A1, is a cytoplasm protein which belongs to theprotein kinase superfamily, CK1 Ser/Thr protein kinase family and casein kinase I subfamily. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. High expression of CSNK2A1, or concomitantly high expression of CSNK2A1, are independent prognostic factors of poor survival in NSCLC patients. CSNK2A1 are useful prognosis markers in non-small cell lung cancer (NSCLC) patients after complete resection, independent of lymph node metastasis status. CSNK1A1 can phosphorylate a large number of proteins. It participates in Wnt signaling. It phosphorylates CTNNB1 at 'Ser-45'. CSNK1A1 may play a role in segregating chromosomes during mitosis.
Casein kinase I isoform gamma-1, also known as CSNK1G1, is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family and casein kinase I subfamily. Thecasein kinase I family of protein kinases are serine / threonine-selective enzymes that function as regulators ofsignal transductionpathways in most eukaryotic cell types. Casein has been used as a substrate since the earliest days of research on protein phosphorylation. Casein kinase activity associated with the endoplasmic reticulum of mammary glands was first characterized in 1974 and its activity was shown to not depend on cyclic AMP. The CKI family of monomeric serine–threonine protein kinases is found in eukaryotic organisms from yeast to human. Mammals have seven family members: alpha, beta 1, gamma 1, gamma 2, gamma 3, delta, and epsilon. The family members have the highest homology in their kinase domains (53%–98% identical) and differ from most other protein kinases by the presence of the sequence S-I-N instead of A-P-E in kinase domain VIII. The CKI family members appear to have similar substrate specificity and substrate selection is thought to be regulated via subcellular localization and docking sites in specific substrates.
Casein kinase I gamma 2 isoform (CSNK1G2); a member of the large casein kinase I (CKI) subfamily; protein kinase superfamily. It may affect the development of brain; and associate with vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. The CKI family includes several other isoforms (alpha; beta; gamma; and delta). Dishevelled (Dsh); another positive component of the Wnt pathway; becomes phosphorylated in response to Wnt signals. All the CKI isoforms; with the exception of gamma; increase the phosphorylation of Dsh in vivo. Casein kinase 1 gamma (CK1gamma; or CSNK1G) is associated with the cell membrane and binds to LRP. CK1gamma was found to be needed for Wnt signaling through Wnt receptor LRP. CSNK1G2 inhibits Smad3-mediated TGF-beta responses including induction of target genes and cell growth arrest; and this inhibition is dependent on CSNK1G2 kinase activity. The overexpression of CSNK1G2 in human cancers; may act as an oncoprotein during tumorigenesis. In addition; as an MTA1s-binding protein; CSNK1G2 could further potentiate the estrogen receptor (ER) corepressive function of MTA1s.
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