Research Papers:

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

Nisha Durand, Sahra Borges, Tavia Hall, Ligia Bastea, Heike Döppler, Brandy H. Edenfield, Aubrey E. Thompson, Xochiquetzal Geiger and Peter Storz _

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Oncotarget. 2018; 9:36358-36370. https://doi.org/10.18632/oncotarget.26357

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Nisha Durand1, Sahra Borges1, Tavia Hall1, Ligia Bastea1, Heike Döppler1, Brandy H. Edenfield1, E. Aubrey Thompson1, Xochiquetzal Geiger2 and Peter Storz1

1Department of Cancer Biology, Mayo Clinic Comprehensive Cancer Center, Mayo Clinic, Jacksonville, FL 32224, USA

2Laboratory Medicine and Pathology, Mayo Clinic, Jacksonville, FL 32224, USA

Correspondence to:

Peter Storz, email: [email protected]

Keywords: PIP5K1C; breast cancer; invasive phenotype; phosphorylation

Received: June 09, 2018    Accepted: October 31, 2018    Published: November 20, 2018


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 (PI4,5P2). 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.

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