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Science 24 December 2004:
Vol. 306. no. 5705, p. 2164
DOI: 10.1126/science.306.5705.2164a
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Editors' Choice: Highlights of the recent literature

Plasticity in neurons is regulated, in part, by the degradation of specific proteins at synapses. Actively dividing cells rely on ubiquitin-dependent degradation to regulate the transitions through the phases of the cell cycle. Van Roessel et al. find that a key enzyme involved in the latter process, the anaphase-promoting complex (APC), plays a role in controlling synaptic size and plasticity. [APC has also been linked to axonal growth and patterning (Konishi et al. Reports, 13 February 2004, p. 1026).] In Drosophila, APC subunits are found at neuromuscular synapses, and when APC levels were reduced, the synaptic boutons of motor neurons increased in size because of the action of the protein Liprin-, which is a substrate for APC-stimulated ubiquitinylation and degradation. Furthermore, muscles lacking APC displayed altered synaptic transmission, and the postsynaptic levels of glutamate receptor were increased. These pre- and postsynaptic functions of APC may explain why a cell cycle regulator is expressed in differentiated postmitotic cells. -- SMH

Cell 119, 707 (2004).




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