Protein cytoplasmic

Kemler, R. (1993). From cadherins to catenins Cytoplasmic protein mreracrions and reglnrion of cell adhesion. Trends Genet. 9(9), 317-321. 

Cadherins (Calcium-dependent adhesion proteins) are transmembrane proteins, which consist of an extracellular domain composed of cadherin-repeats, a transmembrane domain, and a cytoplasmic domain that interacts with catenins and/or other cytoplasmic proteins. 

Besides cytoplasmic protein kinases, membrane receptors can exert protein kinase activity. These so-called receptor tyrosine kinases (RTK) contain a ligandbinding extracellular domain, a transmembrane motif, and an intracellular catalytic domain with specificity for tyrosine residues. Upon ligand binding and subsequent receptor oligomerization, the tyrosine residues of the intracellular domain become phosphory-lated by the intrinsic tyrosine kinase activity of the receptor [3, 4]. The phosphotyrosine residues ftmction as docking sites for other proteins that will transmit the signal received by the RTK. 

Hyperphosphorylation of ERAK-1 by itself and ERAK-4 causes ERAK-1 to dissociate from the membrane-bound complex. Tumour necrosis factor (TNF) receptor-associated factor-6 ( TRAF-6), a cytoplasmic protein, is activated by ERAK-1 and with TAB-2, another cytoplasmic protein, activates transforming growth factor-P (TFG-P)-activating kinase (TAK-1). During this process both TRAF-6 and TAK-1 become ubiquitinated. TAK-1 then promotes activation of the IkB kinases, or the IKK family, EKKa and EKK 3 (found in a complex with NFicB-essential modulator [NEMO]), which phosphorylate the IkB family, notably IkB-u. IkB-u is an inhibitor of NFkB as it sequesters NFkB in an... 

Ah receptor (Aryl hydrocarbon receptor) A receptor located on a cytoplasmic protein to which planar componnds snch as PAHs, coplanar PCBs, and PCDDs bind. Binding initiates the indnction of cytochrome P4501A1/2. 

Ferritin, an iron-binding protein, prevents ionized iron (Fe ) from reaching toxic levels within cells. Elemental iron stimulates ferritin synthesis by causing the release of a cytoplasmic protein that binds to a specific region in the 5 nontranslated region of ferritin mRNA. Disruption of this protein-mRNA interaction activates ferritin mRNA and results in its translation. This mechanism provides for rapid control of the synthesis of a protein that sequesters Fe +, a potentially toxic molecule. 

This cytoplasmic protein is phosphorylated by an IKK complex which is activated by cytokines, reactive oxygen species, and mitogens. Phosphorylated IkB can be ubiquitinylated and degraded, thus releasing its hold on NF-kB. Glucocorticoids affect many steps in this process, as described in the text. 

The last class, represented by E. coli 11 , consists of a membrane domain involving two distinct peptides, one very hydrophobic, and one somewhat less hydrophobic. The domains A and B are not covalently attached to the membrane domains but are separate cytoplasmic proteins [25,107], Other representatives of this class include B. subtilis [26] and K. pneumoniae II " [8],... 

Cyclosporine and tacrolimus belong to a class of immunosuppressants called the calcineurin inhibitors. These agents are considered by many to be the cornerstone of medical immunosuppression. The calcineurin inhibitors work by complexingwith cytoplasmic proteins (cyclosporine with cyclophylin and tacrolimus with FK binding protein 12). These complexes then inhibit calcineurin phosphatase, which results in reduced IL-2 gene transcription. The final outcome is a decrease in IL-2 synthesis and a subsequent reduction in T cell activation.7 11 20 21... 

Terashima Y, Onai N, Murai M, et al. Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis. Nat Immunol 2005 6(8) 827-835. 

Figure 3. MAP kinase regulatory pathway. The MAP kinase signaling pathway begins with activation of the receptor tyrosine kinase (RTK) by exogenous signals, such as growth factors and insulin. The signal is then transmitted into the cell via activation of the Raf serine/threonine kinase either directly by the RTK or through the GTP-binding protein, Ras. The signal is then transmitted to the nucleus and to other cytoplasmic proteins via MAPKK and MAPK.

In this section we summarise the manner in which i -metals. Fig. 6, and where possible specifically the platinum complexes of concern here, interact with biological molecules. Some radio-tracer studies have been carried out on the distribution of platinum complexes in whole bacteria grown in media inocculated with the metal ion. The results are summarised in Table 11. It is noteworthy that the bacteriocidal complex [PtClg]2- was taken up almost entirely by the cytoplasmic protein whereas the filamentous forming neutral species, [Pt(NHs)2Cl4], was... 

CBP is predicted by PSORT analysis to be a cytoplasmic protein (Horton et al. 2007) and to contain a steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain of 200 amino acids at its C-terminus (Figure 24.2a). 

The phospholipids thus obtained are transported by lipid-carrier cytoplasmic proteins to the membranes (cellular or intracellular) to replace the used or impaired phospholipid molecules. 

Romero-Romero, T., Anaya, A.L. and Cruz-Ortega, R. (2002). Screening for effects of phytochemical variability on cytoplasmic protein synthesis pattern of crop plants. Journal of Chemical Ecology 28 617-629. 

Several cytoplasmic proteins capable of inducing T-cell growth (i.e. several cellular protooncogenes, including C-fos and C-myc). 

The intact GM-CSF receptor is a heterodimer, consisting of a low-affinity a-chain and a P-chain, which also forms part of the IL-3 and IL-5 receptors. (The P-chain alone does not bind GM-CSF.) The a-chain is an 80 kDa glycoprotein and exhibits only a short intracellular domain. The larger P-chain (130 kDa) displays a significant intracellular domain. Signal transduction involves the (tyrosine) phosphorylation of a number of cytoplasmic proteins (Figure 10.2). 

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