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. 2014 Aug 1;9(8):e103868. doi: 10.1371/journal.pone.0103868

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© 2014 Rizwani et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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These pathways can potentially lead to phosphorylation of profilin 1: (1) Receptor tyrosine kinases (RTK), (2) Insulin (Ins) and Insulin-like growth factors, (3) Estrogen receptor/Estrogen complex (ER/E), (4) Growth factors (GF) and (5) Vascular endothelial growth factors (VEGF-A) are well known pathways that activate PI3K (Phosphoinositide-3-Kinase) and most common to hormone-dependent and hormone-independent breast cancers. PI3K can in turn activate PKC’s (Protein Kinase C and its isoforms) including PKCζ. Among all PKC isoforms, PKCζ preferentially phosphorylates profilin 1 on Serine (S137) residue that leads to enhanced tumorigenic properties in breast cancer cells. VEGF-A can also lead to tyrosine phosphorylation of profilin 1 and increases angiogenic activity. It can be hypothesized that together these post-translational modifications could be instrumental in breast cancer progression.