Cytoskeleton protein phosphorylation

Intracellular protein phosphorylation is enhanced by chronic antidepressant treatment. This leads to the increased synthesis of microtubules that form an important feature of the cellular cytoskeleton. Thus antidepressants might change signal transduction with the neurone. 

The target of the caspase proteins are nuclear, regulatory, and cytoskeleton proteins, whose degradation triggers the apoptotic response. The proteins of the bcl gene family modulate caspase activity and are divided into proapoptotic and anti-apoptotic fractions (see Figure 11.3). The BCL-associated death (BAD) protein is one of the proapoptotic proteins, whereas BCL-2 is one of the antiapoptotic proteins. The BCL proteins that interact with the caspases to determine whether apoptosis occurs are themselves phosphorylated by PI-3K. 

Ca-VCM-PKII is one of the protein kinases more actively involved in the control of the integrity of the cytoskeleton by phosphorylating cytoskeletal proteins, Ca VCM-PKII becomes constitutively activated when autophosphorylated in key serine or threonine residues on the autonomy site of the enzyme. Autophosphorylation is sufficient to disrupt the autoinhibitory domain of Ca VCM-PKII, leading to a permanent de-... 

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