Polyomavirus T antigens: molecular chaperones for multiprotein complexes.
نویسندگان
چکیده
منابع مشابه
پروتئین شوک حرارتی؛ کاندید واکسن سرطان
Background: Tumor cells express antigens that can be recognized by immune system as foreign particles. Heat shock proteins (HSPs) are molecular chaperones that bind to tumor antigens and mediate their uptake into antigen presenting cells. Methods: This articles is a review article and its data has been collected and categorized from the articles in the field of cancer immunotherapy. All the ar...
متن کاملGenetic analysis of the polyomavirus DnaJ domain.
Polyomavirus T antigens share a common N-terminal sequence that comprises a DnaJ domain. DnaJ domains activate DnaK molecular chaperones. The functions of J domains have primarily been tested by mutation of their conserved HPD residues. Here, we report detailed mutagenesis of the polyomavirus J domain in both large T (63 mutants) and middle T (51 mutants) backgrounds. As expected, some J mutant...
متن کاملThe DnaJ domain of polyomavirus large T antigen is required to regulate Rb family tumor suppressor function.
Tumor suppressors of the retinoblastoma susceptibility gene family regulate cell growth and differentiation. Polyomavirus large T antigens (large T) bind Rb family members and block their function. Mutations of large T sequences conserved with the DnaJ family affect large T binding to a cellular DnaK, heat shock protein 70. The same mutations abolish large T activation of E2F-containing promote...
متن کاملChaperones and Glioma Immunotherapy
Molecular chaperones, also known as heat-shock proteins or HSPs, are a functionally conserved class of proteins whose primary function is to keep cellular proteins in their native conformation, under both physiological and stress conditions. In most cases these chaperones do not participate in the final mature structures that their ‘clients’ form. Apart from folding, chaperones play vital roles...
متن کاملA subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.
We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72; GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is associated with unassembled, incompletely folded immunoglobulin ...
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ورودعنوان ژورنال:
- Journal of virology
دوره 72 7 شماره
صفحات -
تاریخ انتشار 1998