Caveolin-1 (CAV1),a multifunctional protein,is the main constituent molecule of caveolae and represents a scaffolding molecule for several signaling molecules including epidermal growth factor receptor . Several studies have implicated that a reduced expression of CAV1 was found in cancers including head and neck carcinoma . However,other studies recognize CAV1 as a tumor promoter because CAV1 is overexpressed in various kinds of cancers,especially in oral cancer . Recent study also show that CAV1 is involved in astric Cancer .
The scaffolding protein encoded by this gene is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 mitogen-activated kinase cascade. Caveolin 1 and caveolin 2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. Mutations in this gene have been associated with Berardinelli-Seip congenital lipodystrophy. Alternatively spliced transcripts encode alpha and beta isoforms of caveolin 1.
The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids. Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease. Caveolins interact with multiple signaling molecules, such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS. It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins, such as GRB7. Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway.
Cytotoxic Tlymphocyte 4(CTLA-4,CD152), is a type I transmembrane T cell inhibitory molecule that is a member of the Ig superfamily.CD28 and CTLA-4, together with their ligands, B7-1 and B7-2, constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. CTLA4 transmits an inhibitory signal to T cells, whereas CD28 transmits a stimulatory signal. Intracellular CTLA4 is also found in regulatory T Cells and may play an important role in their functions. Tcell activation through the Tcell receptor and CD28 leads to increased expression of CTLA4.
Interleukin-1 beta (IL1B) belongs to the IL-1 family. Interleukin 1 (IL-1) is a family of polypeptide cytokines consisting of two agonists, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2) encoded by two distinct genes and perform identical biological functions. IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response. It is identified as endogenous pyrogens, and is reported to stimulate the release of prostaglandin and collagenase from synovial cells.
CREB-binding protein (CREBBP/CBP), encoded by the human CREBBP gene, is a transcriptional co-activator. CREBBP functions through interactions with transcription factors, mediated by one or more domains: the nuclear receptor interaction domain (RID), the KIX domain (CREB and MYB interaction domain), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3), and the interferon response binding domain. The KIX, TAZ1, and TAZ2 domains of CREBBP bind tightly to the 9aaTADs, the nine amino acid transactivation domains within the tumor suppressor protein p53, thereby influencing its transcriptional activity.
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