CCND2,also known as G1/S-specific cyclin-D2,is a member of the highly conserved cyclin family. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Cyclins function as regulators of CDK kinases. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition. CCND2 is involved in a number of fundamental biological processes such as phosphorylating and inhibiting members of the retinoblastoma (RB) protein family including RB1 and regulating the cell-cycle during G1/S transition. It is also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G1 phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Component of the ternary complex, cyclin D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Peptidyl-prolyl cis-trans isomerase A is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family; which catalyzes the cis-trans isomerization of proline imidic peptide bonds. Cyclophilin A regulate many biological processes; including intracellular signaling; transcription; inflammation; and apoptosis. Cyclophilin is also incorporated into many viruses; including HIV1; where it has been speculated to be involved in functions such as viral assembly and infectivity. The immunosuppressive activity of cyclosporins has been correlated with their ability to form complexes with cyclophilins that inhibit calcineurin phosphatase activity and prevent incorporation of cyclophilin into viral particles. The cyclosporin/cyclophilin complex selectively binds and inactivates calcineurin; making it a useful inhibitor for studying calcineurin activity.
Peptidyl-prolyl cis-trans isomerase A; also known as PPIase A; Rotamase A; Cyclophilin A; Cyclosporin A-binding protein; PPIA and CYPA; is a cytoplasm protein which belongs to thecyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins (CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity; suggesting that they influence the conformation of proteins in cells. PPIA / Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIA / Cyclophilin A is secreted by vascular smooth muscle cells in response to inflammatory stimuli; and could thus contribute to atherosclerosis. It is not essential for mammalian cell viability. PPIA / Cyclophilin A can interact with several HIV proteins; including p55 gag; Vpr; and capsid protein; and has been shown to be necessary for the formation of infectious HIV virions.
Cyclophilin B (SCYLP, CyPB and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in the ER. When secreted, Cyclophilin B mediates chemotaxis and T cell adhesion to fibronectin. This is likely due to its prolyl cis/trans isomerase activity. Intracellularly, Cyclophilin B appears to serve as a molecular chaperone for molecules destined for secretion. It does so via stabilization, and facilitating the activity of additional chaperones.
Cyclophilin C is an enzyme (EC 5.2.1.8) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but prolines unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.
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