Open AccessThe possible roles of B‐cell novel protein‐1 ( BCNP 1) in cellular signalling pathways and in cancer
Author(s) -
Patel Sapan J.,
Trivedi Gaurang L.,
Darie Costel C.,
Clarkson Bayard D.
Publication year - 2017
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.12989
Subject(s) - pleckstrin homology domain , biology , protein kinase b , protein kinase a , c raf , kinase , microbiology and biotechnology , mapk/erk pathway , signal transduction , cancer research , mitogen activated protein kinase kinase
Abstract B‐cell novel protein‐1 ( BCNP 1) or Family member of 129C ( FAM 129C) was identified as a B‐cell‐specific plasma‐membrane protein. Bioinformatics analysis predicted that BCNP 1 might be heavily phosphorylated. The BCNP 1 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 BCNP 1 copy‐number changes and mutations in several cancer types. We also investigated the function of BCNP 1 in cellular signalling pathways. We found that BCNP 1 is highly altered in some types of cancers and that BCNP 1 copy‐number changes and mutations co‐occur with other molecular alteration events for TP 53 (tumour protein P53), PIK 3 CA (Phosphatidylinositol‐4,5‐Bisphosphate 3‐Kinase, Catalytic Subunit Alpha), MAPK 1 (mitogen‐activated protein kinase‐1; ERK : extracellular signal regulated kinase), KRAS (Kirsten rat sarcoma viral oncogene homolog) and AKT 2 (V‐Akt Murine Thymoma Viral Oncogene Homolog 2). We also found that PI 3K (Phoshoinositide 3‐kinase) inhibition and p38 MAPK (p38 mitogen‐activated protein kinase) activation leads to reduction in phosphorylation of BCNP 1 at serine residues, suggesting that BCNP 1 phosphorylation is PI 3K and p38 MAPK dependent and that it might be involved in cancer. Its degradation depends on a proteasome‐mediated pathway.