The growth-associated and presynaptic protein GAP-43 is important for axona
l growth during brain development, for synaptic plasticity and in axonal re
generation [Benowitz, Routtenberg, TINS 12 (1987) 527]. It has been specula
ted that such growth may be mediated by cytoskeletal proteins. However, the
interaction of GAP-43 with proteins of the presynaptic terminals is poorly
characterized. Here, we analyze GAP-43 binding to cytoskeletal proteins by
two different biochemical assays, by blot overlay and sedimentation. We fi
nd that immobilized brain spectrin (BS) is able to bind GAP-43. In contrast
, little binding was observed to microtubule proteins and other elements of
the cytoskeleton. Since GAP-43 is located presynaptically, it may bind to
the presynaptic form. of BS (SpII Sigma 1). It is attractive to think that
such an interaction would participate in the structural plasticity observed
in growth cones and adult synapses. (C) 1999 Elsevier Science B.V. All rig
hts reserved.