{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:50463"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:50463","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Identifizierung und Kartierung von nukleären Import- und Exportsignalmotiven innerhalb des Y-box-bindenden Proteins-1 (YB-1)","abstract":"Y-box Protein-1 (YB-1) is a multifunctional protein, which binds to DNA and RNA thereby influencing transcription and transplation. YB-1 consists of three domains: the N-terminal glycine-rich sequence, the cold shock domain (CSD) and the C-terminal domain. The latter contains alternating acidic and basic amino acids and takes part in a number of protein-protein interactions. Shuttel between the cell nucleus and cytoplasm is essential for YB-1 functionality. In immortalized and proliferationg cells YB-1 is localised in cytoplasm. After stimulation with cytotoxic agents, under hyperthermia or ultraviolet light YB-1 translocates to the nucleus. Accumulation of YB-1 in nuclei of malignant cells is associated with a bad prognosis and higher rate of metastasis in patients with various tumors. In the course of the anti-Thy1.1 nephritis, an animal model of inflammatory renal disease, YB-1 accumulates in cytoplasm of mesangial cells. This accumulation correlates with the mesangial cell proliferation and activation between the days four of the anti-Thy1.1 nephritis. Following day nine up till restitution of nehritis a gradual nuclear re-localisation of YB-1 is observed. In this work, the subcellular localisation of YB-1 domains was examined. To localize the nuclear import and export sequences of YB-1 protein, various YB-1 deletion constructs and stimulations were used in different cell lines. Mutation studies showed that both Nuclear Localisation Sequences (NLS) of the bipartite NLS 276-292 are required for nuclear localisation. On the other hand, the length of the sequence between both NLS components or the tyrosine residues had no effect on nuclear YB-1 localisation. Sorokin et al.showed that YB-1 is cleaved at the amino acid position 220 by the 20S proteasome (Sorokin et al. 2005). We showed that this C-terminal cleavage product P 220-317: (i) is translocated to cell nucleus most likely via the bipartite NLS 276-292; (ii) stimulates the MMP-2 promotor in nucleus, as was shown for full-length YB-1; (iii) exerts autoinhibitory effects on full-length YB-1 protein. These data suggest that YB-1 cleavage results in novel protein functions. Furthermore, we showed that YB-1 contains a Cytoplasmic Retention Site (CRS) in the region between the amino acids 52-101. No Nuclear Export Sequence (NES) could be identified. Next we examined the YB-1 localisation after different stimuli. Only in the tumor HeLa cells and only the full-length YB-1 localized to the nucleus after stimulation with thrombin, deferroxamin, aldosterone and angiotensin II.","abstract_html":"Y-box Protein-1 (YB-1) is a multifunctional protein, which binds to DNA and RNA thereby influencing transcription and transplation. YB-1 consists of three domains: the N-terminal glycine-rich sequence, the cold shock domain (CSD) and the C-terminal domain. The latter contains alternating acidic and basic amino acids and takes part in a number of protein-protein interactions. Shuttel between the cell nucleus and cytoplasm is essential for YB-1 functionality. In immortalized and proliferationg cells YB-1 is localised in cytoplasm. After stimulation with cytotoxic agents, under hyperthermia or ultraviolet light YB-1 translocates to the nucleus. Accumulation of YB-1 in nuclei of malignant cells is associated with a bad prognosis and higher rate of metastasis in patients with various tumors. In the course of the anti-Thy1.1 nephritis, an animal model of inflammatory renal disease, YB-1 accumulates in cytoplasm of mesangial cells. This accumulation correlates with the mesangial cell proliferation and activation between the days four of the anti-Thy1.1 nephritis. Following day nine up till restitution of nehritis a gradual nuclear re-localisation of YB-1 is observed. In this work, the subcellular localisation of YB-1 domains was examined. To localize the nuclear import and export sequences of YB-1 protein, various YB-1 deletion constructs and stimulations were used in different cell lines. Mutation studies showed that both Nuclear Localisation Sequences (NLS) of the bipartite NLS 276-292 are required for nuclear localisation. On the other hand, the length of the sequence between both NLS components or the tyrosine residues had no effect on nuclear YB-1 localisation. Sorokin et al.showed that YB-1 is cleaved at the amino acid position 220 by the 20S proteasome (Sorokin et al. 2005). We showed that this C-terminal cleavage product P 220-317: (i) is translocated to cell nucleus most likely via the bipartite NLS 276-292; (ii) stimulates the MMP-2 promotor in nucleus, as was shown for full-length YB-1; (iii) exerts autoinhibitory effects on full-length YB-1 protein. These data suggest that YB-1 cleavage results in novel protein functions. Furthermore, we showed that YB-1 contains a Cytoplasmic Retention Site (CRS) in the region between the amino acids 52-101. No Nuclear Export Sequence (NES) could be identified. Next we examined the YB-1 localisation after different stimuli. Only in the tumor HeLa cells and only the full-length YB-1 localized to the nucleus after stimulation with thrombin, deferroxamin, aldosterone and angiotensin II.","abstract_has_math":false,"creators":["Kuhl, Vanessa Alice"],"institution":"Publikationsserver der RWTH Aachen University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Mertens, Peter René"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2008,"date_issued":"2008","date_published":"2008","updated_at":"2026-07-30T19:40:25Z","subjects":["info:eu-repo/classification/ddc/610","Transkription <Genetik>","Zellkern","Cytoplasma","Transkriptionsfaktor","Intrazellulärer Transport","Medizin","YB-1","Deletionskonstrukt","NLS","NES","deletion construct"],"languages":["ger"],"rights":["info:eu-repo/semantics/openAccess"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-113009%22"],"render_values":[{"text":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-113009%22","href":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-113009%22","code":true}]}]},"links":{"outbound_url":"https://publications.rwth-aachen.de/record/50463","outbound_label":"Repository record","outbound_source":"dc:identifier"},"source_record":{"url":"https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A50463","prefix":"oai_dc"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Mertens, Peter René"]},{"key":"dc:creator","label":"Author","values":["Kuhl, Vanessa Alice"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:coverage","label":"Dc Coverage","values":["DE"]},{"key":"dc:date","label":"Dc Date","values":["2008"]},{"key":"dc:publisher","label":"Institution","values":["Publikationsserver der RWTH Aachen University"]},{"key":"dc:relation","label":"Dc Relation","values":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-25880"]},{"key":"dc:type","label":"Dc Type","values":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["info:eu-repo/classification/ddc/610","Transkription <Genetik>","Zellkern","Cytoplasma","Transkriptionsfaktor","Intrazellulärer Transport","Medizin","YB-1","Deletionskonstrukt","NLS","NES","deletion construct"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["ger"]},{"key":"dc:rights","label":"Dc Rights","values":["info:eu-repo/semantics/openAccess"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/record/50463","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-113009%22"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Y-box Protein-1 (YB-1) is a multifunctional protein, which binds to DNA and RNA thereby influencing transcription and transplation. YB-1 consists of three domains: the N-terminal glycine-rich sequence, the cold shock domain (CSD) and the C-terminal domain. The latter contains alternating acidic and basic amino acids and takes part in a number of protein-protein interactions. Shuttel between the cell nucleus and cytoplasm is essential for YB-1 functionality. In immortalized and proliferationg cells YB-1 is localised in cytoplasm. After stimulation with cytotoxic agents, under hyperthermia or ultraviolet light YB-1 translocates to the nucleus. Accumulation of YB-1 in nuclei of malignant cells is associated with a bad prognosis and higher rate of metastasis in patients with various tumors. In the course of the anti-Thy1.1 nephritis, an animal model of inflammatory renal disease, YB-1 accumulates in cytoplasm of mesangial cells. This accumulation correlates with the mesangial cell proliferation and activation between the days four of the anti-Thy1.1 nephritis. Following day nine up till restitution of nehritis a gradual nuclear re-localisation of YB-1 is observed. In this work, the subcellular localisation of YB-1 domains was examined. To localize the nuclear import and export sequences of YB-1 protein, various YB-1 deletion constructs and stimulations were used in different cell lines. Mutation studies showed that both Nuclear Localisation Sequences (NLS) of the bipartite NLS 276-292 are required for nuclear localisation. On the other hand, the length of the sequence between both NLS components or the tyrosine residues had no effect on nuclear YB-1 localisation. Sorokin et al.showed that YB-1 is cleaved at the amino acid position 220 by the 20S proteasome (Sorokin et al. 2005). We showed that this C-terminal cleavage product P 220-317: (i) is translocated to cell nucleus most likely via the bipartite NLS 276-292; (ii) stimulates the MMP-2 promotor in nucleus, as was shown for full-length YB-1; (iii) exerts autoinhibitory effects on full-length YB-1 protein. These data suggest that YB-1 cleavage results in novel protein functions. Furthermore, we showed that YB-1 contains a Cytoplasmic Retention Site (CRS) in the region between the amino acids 52-101. No Nuclear Export Sequence (NES) could be identified. Next we examined the YB-1 localisation after different stimuli. Only in the tumor HeLa cells and only the full-length YB-1 localized to the nucleus after stimulation with thrombin, deferroxamin, aldosterone and angiotensin II."]},{"key":"dc:source","label":"Dc Source","values":["Aachen : Publikationsserver der RWTH Aachen University 106 S. : Ill., graph. Darst. (2008). = Aachen, Techn. Hochsch., Diss., 2008"]},{"key":"dc:title","label":"Title","values":["Identifizierung und Kartierung von nukleären Import- und Exportsignalmotiven innerhalb des Y-box-bindenden Proteins-1 (YB-1)"]}]}],"canonical_facts":{"dc:contributor":["Mertens, Peter René"],"dc:coverage":["DE"],"dc:creator":["Kuhl, Vanessa Alice"],"dc:date":["2008"],"dc:description":["Y-box Protein-1 (YB-1) is a multifunctional protein, which binds to DNA and RNA thereby influencing transcription and transplation. YB-1 consists of three domains: the N-terminal glycine-rich sequence, the cold shock domain (CSD) and the C-terminal domain. The latter contains alternating acidic and basic amino acids and takes part in a number of protein-protein interactions. Shuttel between the cell nucleus and cytoplasm is essential for YB-1 functionality. In immortalized and proliferationg cells YB-1 is localised in cytoplasm. After stimulation with cytotoxic agents, under hyperthermia or ultraviolet light YB-1 translocates to the nucleus. Accumulation of YB-1 in nuclei of malignant cells is associated with a bad prognosis and higher rate of metastasis in patients with various tumors. In the course of the anti-Thy1.1 nephritis, an animal model of inflammatory renal disease, YB-1 accumulates in cytoplasm of mesangial cells. This accumulation correlates with the mesangial cell proliferation and activation between the days four of the anti-Thy1.1 nephritis. Following day nine up till restitution of nehritis a gradual nuclear re-localisation of YB-1 is observed. In this work, the subcellular localisation of YB-1 domains was examined. To localize the nuclear import and export sequences of YB-1 protein, various YB-1 deletion constructs and stimulations were used in different cell lines. Mutation studies showed that both Nuclear Localisation Sequences (NLS) of the bipartite NLS 276-292 are required for nuclear localisation. On the other hand, the length of the sequence between both NLS components or the tyrosine residues had no effect on nuclear YB-1 localisation. Sorokin et al.showed that YB-1 is cleaved at the amino acid position 220 by the 20S proteasome (Sorokin et al. 2005). We showed that this C-terminal cleavage product P 220-317: (i) is translocated to cell nucleus most likely via the bipartite NLS 276-292; (ii) stimulates the MMP-2 promotor in nucleus, as was shown for full-length YB-1; (iii) exerts autoinhibitory effects on full-length YB-1 protein. These data suggest that YB-1 cleavage results in novel protein functions. Furthermore, we showed that YB-1 contains a Cytoplasmic Retention Site (CRS) in the region between the amino acids 52-101. No Nuclear Export Sequence (NES) could be identified. Next we examined the YB-1 localisation after different stimuli. Only in the tumor HeLa cells and only the full-length YB-1 localized to the nucleus after stimulation with thrombin, deferroxamin, aldosterone and angiotensin II."],"dc:identifier":["https://publications.rwth-aachen.de/record/50463","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-113009%22"],"dc:language":["ger"],"dc:publisher":["Publikationsserver der RWTH Aachen University"],"dc:relation":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-25880"],"dc:rights":["info:eu-repo/semantics/openAccess"],"dc:source":["Aachen : Publikationsserver der RWTH Aachen University 106 S. : Ill., graph. Darst. (2008). = Aachen, Techn. 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