Melatonin Production: Proteasomal Proteolysis in Serotonin N-Acetyltransferase Regulation

See allHide authors and affiliations

Science  27 Feb 1998:
Vol. 279, Issue 5355, pp. 1358-1360
DOI: 10.1126/science.279.5355.1358

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


The nocturnal increase in circulating melatonin in vertebrates is regulated by 10- to 100-fold increases in pineal serotoninN-acetyltransferase (AA-NAT) activity. Changes in the amount of AA-NAT protein were shown to parallel changes in AA-NAT activity. When neural stimulation was switched off by either light exposure or l-propranolol–induced β-adrenergic blockade, both AA-NAT activity and protein decreased rapidly. Effects ofl-propranolol were blocked in vitro by dibutyryl adenosine 3′,5′-monophosphate (cAMP) or inhibitors of proteasomal proteolysis. This result indicates that adrenergic-cAMP regulation of AA-NAT is mediated by rapid reversible control of selective proteasomal proteolysis. Similar proteasome-based mechanisms may function widely as selective molecular switches in vertebrate neural systems.

  • * To whom correspondence should be addressed. E-mail: klein{at}

View Full Text

Stay Connected to Science