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(Received for publication, May 23, 1996, and in revised form, September 23, 1996)
From the Cyclic AMP-dependent protein kinase
(PKA) is anchored at specific subcellular sites through the interaction
of the regulatory subunit (R) with protein kinase A-anchoring proteins
(AKAPs) via an amphipathic helix binding motif. Synthetic peptides
containing this amphipathic helix domain competitively disrupt PKA
binding to AKAPs and cause a loss of PKA modulation of cellular
responses. In this report we use S-Ht31, a cell-permeant anchoring
inhibitor peptide, to study the role of PKA anchoring in sperm. Our
analysis of three species of mammalian sperm detected three isoforms of PKA (RII
Volume 272, Number 8,
Issue of February 21, 1997
pp. 4747-4752
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Oregon Regional Primate Research Center,
Beaverton, Oregon 97006, the § Promega Corporation, Madison,
Wisconsin 53711, and the ¶ Veterans Affairs Medical Center and
Oregon Health Sciences University, Portland, Oregon 97201
, RII
, and RI) and one 110-kDa AKAP. The addition of S-Ht31 to bovine caudal epididymal sperm inhibits motility in a time-
and concentration-dependent manner. A control peptide, S-Ht31-P, identical to S-Ht31 except for a proline for isoleucine substitution to prevent amphipathic helix formation, had no effect on
motility. The inhibition of motility by S-Ht31 is reversible but only
if calcium is present in the suspension buffer, suggesting a role for
PKA anchoring in regulating cellular calcium homeostasis. Surprisingly,
inhibition of PKA catalytic activity had little effect on basal
motility or motility stimulated by agents previously thought to work
via PKA activation. These data suggest that the interaction of the
regulatory subunit of PKA with sperm AKAPs, independent of PKA
catalytic activity, is a key regulator of sperm motility and that
disruption of this interaction using cell-permeable anchoring inhibitor
peptides may form the basis of a sperm-targeted contraceptive.
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