Michaluk P, Mikasova L, Groc L, Frischknecht R, Choquet D, Kaczmarek L (2009)
Publication Type: Journal article
Publication year: 2009
Book Volume: 29
Pages Range: 6007-6012
Journal Issue: 18
DOI: 10.1523/JNEUROSCI.5346-08.2009
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. Copyright © 2009 Society for Neuroscience.
APA:
Michaluk, P., Mikasova, L., Groc, L., Frischknecht, R., Choquet, D., & Kaczmarek, L. (2009). Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin β1 signaling. The Journal of Neuroscience, 29(18), 6007-6012. https://doi.org/10.1523/JNEUROSCI.5346-08.2009
MLA:
Michaluk, Piotr, et al. "Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin β1 signaling." The Journal of Neuroscience 29.18 (2009): 6007-6012.
BibTeX: Download