At the proteome level we mainly observed changes in mitochondrial translation, cell division pathways and proteins related to cell cycle progression.
Upon growth factor stimulation, PI3K is activated, increasing PIP3 levels which drives phosphorylation of AKT and downstream processes such as higher protein translation, cell division and reduced apoptosis.
These genes encode proteins involved in transcription, translation, cell wall modification and oxidative phosphorylation, and were earlier repressed by the transition from log phase to hypoxia.
EBP1 is a ubiquitous protein with multiple, complex functions involved in transcription and translation, cell proliferation and survival [24], [25], [26], [27].
Consistent with the hyperproliferative and invasive phenotype of IBC these genes are notably involved in protein translation, cell cycle, RNA processing and transcription, metabolism, and cell migration.
Protein serine/threonine phosphatase 2A (PP-2A) is a major eukaryotic phosphatase, regulating many different functions including metabolism, DNA replication, transcription, RNA splicing, translation, cell cycle progression, cell senescence and apoptosis, cell transformation, morphogenesis, development, and neurotransmission [1] [6].
Protein kinases mediate signal transduction in eukaryotic cells and are involved in regulating all cellular processes such as transcription, translation, cell cycle progression, cytoskeleton rearrangements, migration, apoptosis and differentiation.
In our circuits, time delay can be accounted for by the non-instantaneous rates of reactions affecting the level and function of the E protein, including transcription, translation, cell killing by the E protein, and E protein degradation.
Upon growth factor stimulation, PI3K is activated which increases PIP3 levels and promotes phosphorylation of AKT and downstream processes such as increased protein translation, cell division and reduced apoptosis.
