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These two Mycobacterial kinases have been implicated in cell division and the maintenance of cell shape and it has been suggested that they may phosphorylate components (FtsZ and FipA) of the division apparatus [29].
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Many growth factors signal through receptor tyrosine kinases, leading to dimerization, trans-phosphorylation and activation of tyrosine kinases that phosphorylate components further downstream of the signal transduction cascade.
Alternatively, PINK1 may phosphorylate parkin and directly influence its activity.
Protein kinase C may activate the monomeric G protein Raf, causing it to phosphorylate MAPK kinase (MEK), which in turn may phosphorylate Map kinase (MAPK 47; MAPK may then phosphorylate calponin or caldesmon, and other intermediate proteins.
Our data also suggest that mTOR may phosphorylate TFEB in the nuclear compartment.
We speculated that PKC may phosphorylate other autophagy-related proteins to regulate autophagy.
In addition, roles of other kinases that may phosphorylate PDPN to control cell migration have not been investigated.
Studies have also revealed that a MAPK may phosphorylate a MAPKKK during negative feedback regulation of the MAP kinase cascade.
Thus, it is plausible that ERK may phosphorylate these histones.
However, there is evidence that Akt may phosphorylate cellular substrates at the level of a partially conserved sequence motif [29].
ERK may phosphorylate PPAR γ and reduce its genomic activity.
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