Functional characterization of APOBEC-1 complementation factor phosphorylation sites
نویسندگان
چکیده
منابع مشابه
Metabolic regulation of ApoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor
Apolipoprotein B (apoB) mRNA editing is a nuclear event that minimally requires the RNA substrate, APOBEC-1 and APOBEC-1 Complementation Factor (ACF). The co-localization of these macro-molecules within the nucleus and the modulation of hepatic apoB mRNA editing activity have been described following a variety of metabolic perturbations, but the mechanism that regulates editosome assembly is un...
متن کاملTargeted deletion of the murine apobec-1 complementation factor (acf) gene results in embryonic lethality.
apobec-1 complementation factor (ACF) is an hnRNP family member which functions as the obligate RNA binding subunit of the core enzyme mediating C-to-U editing of the nuclear apolipoprotein B (apoB) transcript. ACF binds to both apoB RNA and apobec-1, the catalytic cytidine deaminase, which then results in site-specific posttranscriptional editing of apoB mRNA. Targeted deletion of apobec1 elim...
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The phosphorylation of thyroid transcription factor-1 (TTF-1), is homeodomain-containing transcription factor that is required for thyroid-specific expression of the thyroglobulin and thyroperoxidase gene promoters, has been studied. Phosphorylation occurs on a maximum of seven serine residues that are distributed in three tryptic peptides. Mutant derivatives of TTF-1, with alanine sites, have ...
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Insulin-like growth factor 1 (IGF-1) is a polypeptide hormone produced mainly by the liver in response to the endocrine growth hormone (GH) stimulus. This protein is involved in a wide range of cellular functions, including cellular differentiation, transformation, apoptosis suppression, migration and cell-cycle progression and other metabolic processes. In the current study, human heart cDNA w...
متن کاملIdentification and Functional Characterization of Novel Phosphorylation Sites in TAK1-Binding Protein (TAB) 1
TAB1 was defined as a regulatory subunit of the protein kinase TAK1, which functions upstream in the pathways activated by interleukin (IL)-1, tumor necrosis factor (TNF), toll-like receptors (TLRs) and stressors. However, TAB1 also functions in the p38 MAPK pathway downstream of TAK1. We identified amino acids (aa) 452/453 and 456/457 of TAB1 as novel sites phosphorylated by TAK1 as well as by...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2007
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2006.11.019