Protein kinase association with viral

When ODAR attaches to the osteoblast surface-bound ODF, the receptor/ligand complex activates a membrane-associated tyrosine-protein kinase to induce synthesis of the ruffled membrane. A tyrosine residue on C1IC-5 (Sect. 10.1.4) is phosphorylated by an activated protein kinase, called c-src, the normal cytosolic homologue of a viral tyrosine kinase which causes a sarcoma (transforms fibroblasts into cancer cells). The phosphorylated C1IC-5 interacts with phospholipids, a chloride channel protein (C1C-7) and two transporter proteins, the ATPase proton transporter, and the proton-dependent phosphate transporter. Mutations that suppress c-src or prevent expression or functioning of C1C-7 or C1IC-5 in mice or humans prevent osteoclast development and cause overly dense, brittle bones (osteopetrosis). 

In addition, some Authors suggested that the antiretroviral efficacy of hypericin is associated with the inhibition of protein-kinase C-mediated phosphorylation, occurring during the viral infection of the cells [10]. 

HIV is a retrovirus in which the virus uses the body s cellular machinery to transform RNA to DNA. The number of helper T cells is dramatically reduced thereby lowering the body s immune response. GP-120 is essential to the virus binding to the cell surface receptor for entry into the cell. 14-3-3-0 is specifically implicated in the G2 checkpoint for cell cycle arrest for the HIV-1 VPR (viral protein R) accessory protein, which is associated with cell death since VPR is necessary for viral infection of helper T cells (Bolton et al. 2008). 14-3-3-0 can bind to several cyclin-dependent kinases that regulate the cell cycle leading to overall neurodegeneration in this immune disorder. Lipid peroxidation of the 14-3-3 family of proteins may cause reduced interaction with protein kinases, which can result in reduced signal transduction by which protein synthesis, cell cycle regulation, and DNA repair may be affected. 

Besides the cytokine receptors that lack intrinsic kinase activity but have associated JAK kinases, STAT proteins can be activated by a variety of G-protein coupled receptors and growth factor receptors with intrinsic tyrosine kinase activity (for example EGF, PDGF, CSF-1, and angiotensin receptor). Increasing evidence suggests a critical role for STAT family members in oncogenesis and aberrant cell proliferation. Constitutively activated STATs have been found in many transformed cell lines and a wide variety of human tumor entities. Numerous non-receptor tyrosine kinases and viral oncoproteins, such as v-Src, v-Abl, v-Sis, and v-Eyk, have been identified to induce DNA-binding activity of STAT proteins. 

There is much more to this functional complexity than we have been able to discuss in this review. For instance, we have not touched on the complex intranuclear network mediated by the nuclear lamins, which is critically important for human health as reflected in the numerous disease phenotypes that are emerging due to mutation in lamins and their associated protein partners. We have also not discussed the association of IFs with molecules involved in bacterial and viral pathogenesis, such as the Ebstein-Barr virus latent infection membrane protein (LMP) (Liebowitz et al., 1987) or viral kinases such as the herpes simplex virus US3 kinase (Murata et at, 2002) that may be important in remodeling IFs during infection. It is clear, however, from the many critical cellular functions we have discussed in this review, that the IF structural and signaling scaffold is involved in wide-ranging functions that are important for fundamental... 

---