Interferon-induced 17 KD protein (ISG15), a 15-KD protein of unique primary amino acid sequence, functions intracellularly as a ubiquitin homolog and a cytokine that induces production of IFN-gamma and aμgments NK / lymphokine-activated killer cell proliferation and function. ISG15 is secreted from monocytes and lymphocytes. ISG15 is a ubiquitin-like molecule that is strongly upregulated by type I interferons as a primary response to diverse microbial and cellular stress stimuli. Alterations in the ISG15 signaling pathway have also been found in several human tumor entities. In addition to being stimulated by type I interferon, expression of ISG15 is greatly induced by viral or bacterial infection throμgh the Janus kinase/signal transducer and activator of transcription (Jak / STAT) signaling pathway. After induction, ISG15 is secreted by monocytes, B-and T-lymphocytes, and fibroblasts. We demonstrate the novel way in which the function of the ISG15 protein is inhibited by influenza B virus, which strongly induces the ISG15 protein: a specific region of the influenza B virus NS1 protein, which includes part of its effector domain, blocks the covalent linkage of ISG15 to its target proteins both in vitro and in infected cells.
E3 ubiquitin-protein ligase Itchy homolog, also known as Atrophin-1-interacting protein 4, NFE2-associated polypeptide 1, NAPP1 and ITCH, is a cell membrane protein which contains oneC2 domain, oneHECT (E6AP-type E3 ubiquitin-protein ligase) domain and contains fourWW domains. ITCH acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. ITCH is involved in the control of inflammatory signaling pathways. It is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. ITCH promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteosomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Defects in ITCH are the cause of syndromic multisystem autoimmune disease (SMAD) which is characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut.
Integrin α-5 belongs to the Integrin α chain family and contains 7 FG-GAP repeats. Integrin α-5 joins with Integrin-β1 to form a fibronectin and laminin receptor which recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection; the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. It is expressed on fibroblasts; endothelial cells; peripheral T cells and platelets. Integrin α-5 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains. In addition to adhesion; ITGA5 participates in cell-surface mediated signalling.
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