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The Journal of Neuroscience, October 1, 1998, 18(19):7757-7767

The Neuronal Growth-Associated Protein GAP-43 Interacts with Rabaptin-5 and Participates in Endocytosis

Rachael L. Neve1, 2, Robert Coopersmith1, 2, Donna L. McPhie1, 2, Christopher Santeufemio2, Kara G. Pratt1, 2, Curran J. Murphy1, 2, and Stephanie D. Lynn1, 2

1 Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, and 2 McLean Hospital, Belmont, Massachusetts 02178

Structural plasticity of nerve cells is a requirement for activity-dependent changes in the brain. The growth-associated protein GAP-43 is thought to be one determinant of such plasticity, although the molecular mechanism by which it mediates dynamic structural alterations at the synapse is not known. GAP-43 is bound by calmodulin when Ca2+ levels are low, and releases the calmodulin when Ca2+ levels rise, suggesting that calmodulin may act as a negative regulator of GAP-43 during periods of low activity in the neurons. To identify the function of GAP-43 during activity-dependent increases in Ca2+ levels, when it is not bound to calmodulin, we sought proteins with which GAP-43 interacts in the presence of Ca2+. We show here that rabaptin-5, an effector of the small GTPase Rab5 that mediates membrane fusion in endocytosis, is one such protein. We demonstrate that GAP-43 regulates endocytosis and synaptic vesicle recycling. Modulation of endocytosis by GAP-43, in association with rabaptin-5, may constitute a common molecular mechanism by which GAP-43 regulates membrane dynamics during its known roles in activity-dependent neurotransmitter release and neurite outgrowth.

Key words: GAP-43; growth-associated protein; calmodulin; rabaptin-5; endocytosis; synaptic vesicle

Copyright © 1998 Society for Neuroscience  0270-6474/98/18197757-11$05.00/0


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