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J Neurosci. 2009 May 6;29(18):6007-12. doi: 10.1523/JNEUROSCI.5346-08.2009.

Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin beta1 signaling.

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  • 1The Nencki Institute, 02-093 Warsaw, Poland.


Matrix metalloproteinase-9 (MMP-9) has emerged as a physiological regulator of NMDA receptor (NMDAR)-dependent synaptic plasticity and memory. The pathways by which MMP-9 affects NMDAR signaling remain, however, elusive. Using single quantum dot tracking, we demonstrate that MMP-9 enzymatic activity increases NR1-NMDAR surface trafficking but has no influence on AMPA receptor mobility. The mechanism of MMP-9 action on NMDAR is not mediated by change in overall extracellular matrix structure nor by direct cleavage of NMDAR subunits, but rather through an integrin beta1-dependent pathway. These findings describe a new target pathway for MMP-9 action in key physiological and pathological brain processes.

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