Intracellular transport, sorting, and proteolytic processing of regulated secretory proteins does not require protein sulfation.

The biological significance of protein sulfation is poorly understood. To study a possible role of protein sulfation in the regulated secretory pathway, neurointermediate lobes (NIL) of the pituitary of South-African clawed toads (Xenopus laevis) were treated with chlorate, a potent in vivo inhibitor of protein sulfation. We monitored the fates of newly synthesized proopiomelanocortin (POMC), prohormone convertase (PC2), and secretogranin III (SgIII), which are sulfated and regulated secretory proteins. Inhibition of protein sulfation had no effect on the proteolytic processing of these precursor proteins and the kinetics of release of their cleavage products. The release was sensitive to apomorphine, a drug that blocks the release of proteins via the regulated secretory pathway, indicating that no missorting to the constitutive pathway had occurred. Our results suggest that protein sulfation is not required for the intracellular transport, sorting, and proteolytic processing of regulated secretory proteins.