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The phosphorylation status of PIP5K1C at serine 448 can be predictive for invasive ductal carcinoma of the breast

Phosphatidylinositol-4-phosphate 5-kinase type-1C (PIP5K1C) is a lipid kinase that regulates focal adhesion dynamics and cell attachment through site-specific formation of phosphatidylinositol-4,5-bisphosphate (PI4,5P(2)). By comparing normal breast tissue to carcinoma in situ and invasive ductal ca...

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Detalles Bibliográficos
Autores principales: Durand, Nisha, Borges, Sahra, Hall, Tavia, Bastea, Ligia, Döppler, Heike, Edenfield, Brandy H., Thompson, E. Aubrey, Geiger, Xochiquetzal, Storz, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6284740/
https://www.ncbi.nlm.nih.gov/pubmed/30555634
http://dx.doi.org/10.18632/oncotarget.26357
Descripción
Sumario:Phosphatidylinositol-4-phosphate 5-kinase type-1C (PIP5K1C) is a lipid kinase that regulates focal adhesion dynamics and cell attachment through site-specific formation of phosphatidylinositol-4,5-bisphosphate (PI4,5P(2)). By comparing normal breast tissue to carcinoma in situ and invasive ductal carcinoma subtypes, we here show that the phosphorylation status of PIP5K1C at serine residue 448 (S448) can be predictive for breast cancer progression to an aggressive phenotype, while PIP5K1C expression levels are not indicative for this event. PIP5K1C phosphorylation at S448 is downregulated in invasive ductal carcinoma, and similarly, the expression levels of PKD1, the kinase that phosphorylates PIP5K1C at this site, are decreased. Overall, since PKD1 is a negative regulator of cell migration and invasion in breast cancer, the phosphorylation status of this residue may serve as an indicator of aggressiveness of breast tumors.