We are analyzing https://link.springer.com/article/10.1007/s11010-022-04401-8.

Title:
The profile of expression of the scaffold protein SG2NA(s) differs between cancer types and its interactome in normal vis-a-vis breast tumor tissues suggests its wide roles in regulating multiple cellular pathways | Molecular and Cellular Biochemistry
Description:
Striatin and SG2NA are scaffold proteins that form signaling complexes called STRIPAK. It has been associated with developmental abnormalities, cancer, and several other diseases. Our earlier studies have shown that SG2NA forms a complex with the cancer-associated protein DJ-1 and the signaling kinase Akt, promoting cancer cell survival. In the present study, we used bioinformatics analyses to confirm the existence of two isoforms of human SG2NA, i.e., 78 and 87 kDas. In addition, several smaller isoforms like 35 kDa were also seen in western blot analyses of human cell lysates. The expression of these isoforms varies between different cancer cell lines of human origin. Also, the protein levels do not corroborate with its transcript levels, suggesting a complex regulation of its expression. In breast tumor tissues, the expression of the 35 and 78 kDa isoforms was higher as compared to the adjacent normal tissues, while the 87 kDa isoform was found in the breast tumor tissues only. With the progression of stages of breast cancer, while the expression of 78 kDa isoform decreased, 87 kDa became undetectable. In co-immunoprecipitation assays, the profile of the SG2NA interactome in breast tumors vis-à-vis adjacent normal breast tissues showed hundreds of common proteins. Also, some proteins were interacted with SG2NA in breast tumor tissues only. We conclude that SG2NA is involved in diverse cellular pathways and has roles in cellular reprogramming during tumorigenesis of the breast.
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article, pubmed, google, scholar, cas, cancer, cell, sgna, central, breast, proteins, analysis, expression, jain, httpsdoiorgs, protein, biol, cellular, stripak, complex, kda, tissues, goswami, signaling, biochem, india, supplementary, privacy, cookies, content, data, information, tumor, human, access, variants, chen, publish, research, search, molecular, scaffold, normal, multiple, manuscript, bisoyi, devi, striatin, complexes, diseases,

Topics {✒️}

month download article/chapter adjacent normal tissues nonsense-mediated mrna decay junior/senior research fellowship breast tumor tissues breast cancer subtypes mst4-mob4 complex disrupts area-proportional venn diagrams cell-cycle nuclear autoantigen buddhi prakash jain full article pdf tanti gk wd40 repeat proteins explore cancer biology striatin-pp2a complex privacy choices/manage cookies related subjects multiple splice variants growth responsive properties diverse cellular pathways article bisoyi striatin-interacting phosphatase calmodulin-binding proteins regulates dendritic spinogenesis article molecular cellular biochemistry aims cellular reprogramming hippo signaling pathway comprehensive functional analysis bioinformatic analysis part references chen cancer cell lines protein phosphatase 2a european economic area hippo-yap pathway mol med rep wd-40 motifs expressed jawaharlal nehru university sg2na protein variants g2 phase cells glioblastoma stem cells breast cancer article log noncanonical coiled coil suppress retinal fate level affects phases asselin-labat m jain bp conditions privacy policy david bioinformatics resources

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      description:Striatin and SG2NA are scaffold proteins that form signaling complexes called STRIPAK. It has been associated with developmental abnormalities, cancer, and several other diseases. Our earlier studies have shown that SG2NA forms a complex with the cancer-associated protein DJ-1 and the signaling kinase Akt, promoting cancer cell survival. In the present study, we used bioinformatics analyses to confirm the existence of two isoforms of human SG2NA, i.e., 78 and 87 kDas. In addition, several smaller isoforms like 35 kDa were also seen in western blot analyses of human cell lysates. The expression of these isoforms varies between different cancer cell lines of human origin. Also, the protein levels do not corroborate with its transcript levels, suggesting a complex regulation of its expression. In breast tumor tissues, the expression of the 35 and 78 kDa isoforms was higher as compared to the adjacent normal tissues, while the 87 kDa isoform was found in the breast tumor tissues only. With the progression of stages of breast cancer, while the expression of 78 kDa isoform decreased, 87 kDa became undetectable. In co-immunoprecipitation assays, the profile of the SG2NA interactome in breast tumors vis-à-vis adjacent normal breast tissues showed hundreds of common proteins. Also, some proteins were interacted with SG2NA in breast tumor tissues only. We conclude that SG2NA is involved in diverse cellular pathways and has roles in cellular reprogramming during tumorigenesis of the breast.
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