Increased Histone Acetyltransferase and Lysine Acetyltransferase Activity and Biphasic Activation of the ERK/RSK Cascade in Insular Cortex During Novel Taste Learning

This research was supported by National Institutes of Health Grants MH18390, DC00454 (M.W.S.), and MH57014 (J.D.S.), a grant from the New York Obesity Research Center (M.W.S.), and a grant from the Texas Advanced Technology Program (J.D.S.). The kind support and encouragement of Dr. Gerard P. Smith are gratefully acknowledged.

Correspondence should be addressed to Michael W. Swank, Division of Neuroscience, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030. E-mail: mswank{at}cns.bcm.tmc.edu.

^aThe term histone acetyltransferase (HAT), although it would appear to refer specifically to the lysine acetylation of histones, is commonly used in the literature to refer also to lysine acetyltransferase activity responsible for acetylation of a rapidly growing list of other nonhistone substrates such as p53, CBP, and PCAF. We believe that the use of the term lysine (K) acetyltransferase (KAT) may be a more reasonable description of lysine acetyltransferases involved in acetylation of nonhistone substrates such as p42AcK described in this report, and we reserve the use of the term histone acetyltransferase (HAT) for instances in which histones are demonstrated to be among the substrates that are acetylated.