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The Journal of Neuroscience, May 6, 2009, 29(18):6007-6012; doi:10.1523/JNEUROSCI.5346-08.2009

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Brief Communications
Matrix Metalloproteinase-9 Controls NMDA Receptor Surface Diffusion through Integrin β1 Signaling

Piotr Michaluk,^1,2 Lenka Mikasova,³ Laurent Groc,³ Renato Frischknecht,⁴ Daniel Choquet,³ and Leszek Kaczmarek¹

¹The Nencki Institute, 02-093 Warsaw, Poland, ²University Medical Center, 3584 CG Utrecht, The Netherlands, ³Unité Mixte de Recherche 5091, Centre National de la Recherche Scientifique, Université Bordeaux 2, 33077 Bordeaux, France, and ⁴Leibniz Institute for Neurobiology, D-39118 Magdeburg, Germany

Correspondence should be addressed to Leszek Kaczmarek, The Nencki Institute, Pasteur 3, 02-093 Warsaw, Poland. Email: l.kaczmarek{at}nencki.gov.pl

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 β1-dependent pathway. These findings describe a new target pathway for MMP-9 action in key physiological and pathological brain processes.

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Received Nov. 6, 2008; revised March 23, 2009; accepted March 27, 2009.

Correspondence should be addressed to Leszek Kaczmarek, The Nencki Institute, Pasteur 3, 02-093 Warsaw, Poland. Email: l.kaczmarek{at}nencki.gov.pl

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