
-   *In vitro* studies on recombinant peptides and endogenous protein from rat astrocytes indicated that MLC1 is phosphorylated at its NH~2~ and COOH terminals by both PKA and PKC and PKC alone, respectively. Inhibition of endocytosis, cholesterol lowering and protein kinases A- and C-mediated MLC1 phosphorylation favor the expression of membrane-associated MLC1 [PMID: 19931615].
-   Data indicates that PKC and PKA activation favors MLC1 expression in the plasma membrane and the presence of an endoplasmic reticulum retention motif near the PKC/PKA phosphorylation sites suggest this possibility also for the MLC1 protein [PMID: 25883547].
-   Post-translational modifications can exert an important role in MLC1 forward trafficking and stabilization in the plasma membrane. Data suggests that that the membrane expression level of MLC1 is spatially and temporally regulated by agents modulating intracellular trafficking, cytoskeletal organization and lipid composition of the plasma membrane, as observed for many ion channels and transporters [PMID: 25883547, PMID: 20519314].
