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The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer
B‐cell novel protein‐1 (BCNP1) or Family member of 129C (FAM129C) was identified as a B‐cell‐specific plasma‐membrane protein. Bioinformatics analysis predicted that BCNP1 might be heavily phosphorylated. The BCNP1 protein contains a pleckstrin homology (PH) domain, two proline‐rich (PR) regions and...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5323820/ https://www.ncbi.nlm.nih.gov/pubmed/27680505 http://dx.doi.org/10.1111/jcmm.12989 |
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author | Patel, Sapan J. Trivedi, Gaurang L. Darie, Costel C. Clarkson, Bayard D. |
author_facet | Patel, Sapan J. Trivedi, Gaurang L. Darie, Costel C. Clarkson, Bayard D. |
author_sort | Patel, Sapan J. |
collection | PubMed |
description | B‐cell novel protein‐1 (BCNP1) or Family member of 129C (FAM129C) was identified as a B‐cell‐specific plasma‐membrane protein. Bioinformatics analysis predicted that BCNP1 might be heavily phosphorylated. The BCNP1 protein contains a pleckstrin homology (PH) domain, two proline‐rich (PR) regions and a Leucine Zipper (LZ) domain suggesting that it may be involved in protein‐protein interactions. Using The Cancer Genome Atlas (TCGA) data sets, we investigated the correlation of alteration of the BCNP1 copy‐number changes and mutations in several cancer types. We also investigated the function of BCNP1 in cellular signalling pathways. We found that BCNP1 is highly altered in some types of cancers and that BCNP1 copy‐number changes and mutations co‐occur with other molecular alteration events for TP53 (tumour protein P53), PIK3CA (Phosphatidylinositol‐4,5‐Bisphosphate 3‐Kinase, Catalytic Subunit Alpha), MAPK1 (mitogen‐activated protein kinase‐1; ERK: extracellular signal regulated kinase), KRAS (Kirsten rat sarcoma viral oncogene homolog) and AKT2 (V‐Akt Murine Thymoma Viral Oncogene Homolog 2). We also found that PI3K (Phoshoinositide 3‐kinase) inhibition and p38 MAPK (p38 mitogen‐activated protein kinase) activation leads to reduction in phosphorylation of BCNP1 at serine residues, suggesting that BCNP1 phosphorylation is PI3K and p38MAPK dependent and that it might be involved in cancer. Its degradation depends on a proteasome‐mediated pathway. |
format | Online Article Text |
id | pubmed-5323820 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-53238202017-03-02 The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer Patel, Sapan J. Trivedi, Gaurang L. Darie, Costel C. Clarkson, Bayard D. J Cell Mol Med Original Articles B‐cell novel protein‐1 (BCNP1) or Family member of 129C (FAM129C) was identified as a B‐cell‐specific plasma‐membrane protein. Bioinformatics analysis predicted that BCNP1 might be heavily phosphorylated. The BCNP1 protein contains a pleckstrin homology (PH) domain, two proline‐rich (PR) regions and a Leucine Zipper (LZ) domain suggesting that it may be involved in protein‐protein interactions. Using The Cancer Genome Atlas (TCGA) data sets, we investigated the correlation of alteration of the BCNP1 copy‐number changes and mutations in several cancer types. We also investigated the function of BCNP1 in cellular signalling pathways. We found that BCNP1 is highly altered in some types of cancers and that BCNP1 copy‐number changes and mutations co‐occur with other molecular alteration events for TP53 (tumour protein P53), PIK3CA (Phosphatidylinositol‐4,5‐Bisphosphate 3‐Kinase, Catalytic Subunit Alpha), MAPK1 (mitogen‐activated protein kinase‐1; ERK: extracellular signal regulated kinase), KRAS (Kirsten rat sarcoma viral oncogene homolog) and AKT2 (V‐Akt Murine Thymoma Viral Oncogene Homolog 2). We also found that PI3K (Phoshoinositide 3‐kinase) inhibition and p38 MAPK (p38 mitogen‐activated protein kinase) activation leads to reduction in phosphorylation of BCNP1 at serine residues, suggesting that BCNP1 phosphorylation is PI3K and p38MAPK dependent and that it might be involved in cancer. Its degradation depends on a proteasome‐mediated pathway. John Wiley and Sons Inc. 2016-09-29 2017-03 /pmc/articles/PMC5323820/ /pubmed/27680505 http://dx.doi.org/10.1111/jcmm.12989 Text en © 2016 The Authors. Journal of Cellular and Molecular Medicine published by John Wiley & Sons Ltd and Foundation for Cellular and Molecular Medicine. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Patel, Sapan J. Trivedi, Gaurang L. Darie, Costel C. Clarkson, Bayard D. The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title | The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title_full | The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title_fullStr | The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title_full_unstemmed | The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title_short | The possible roles of B‐cell novel protein‐1 (BCNP1) in cellular signalling pathways and in cancer |
title_sort | possible roles of b‐cell novel protein‐1 (bcnp1) in cellular signalling pathways and in cancer |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5323820/ https://www.ncbi.nlm.nih.gov/pubmed/27680505 http://dx.doi.org/10.1111/jcmm.12989 |
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