TPST-1 Activators

TPST-1 activators encompass chemicals that can indirectly modulate the function of TPST1, especially by affecting its enzymatic substrate availability or the broader context of cellular signaling and post-translational modifications. Key among these is PAPS, the primary donor molecule for the sulfate group. Without PAPS, TPST1 cannot function effectively. Chemicals like Forskolin and db-cAMP emphasize the role of cAMP in cellular signaling. Elevation of cAMP can potentially activate or inhibit various enzymes, possibly modulating TPST1's function indirectly.

Proteasome inhibitors like MG-132 highlight the importance of protein stabilization in enhancing TPST1's substrate availability. As TPST1's primary function is the sulfation of tyrosine residues, chemicals that influence tyrosine phosphorylation, such as Sodium Orthovanadate, Calyculin A, and Genistein, are crucial. The involvement of pathways like MAPK/ERK, underscored by the MEK inhibitor U0126, depicts the intricate network of protein modifications that can impact TPST1. The presence of Anisomycin and Ionomycin further underscores the multitude of pathways, from JNK signaling to calcium regulation, that can influence TPST1.