Sanz-Clemente, Antonio, PhD



Sanz-Clemente, Antonio, PhD


Assistant Professor


Office Phone





Searle 8-523


Areas of Research

Cell Biology, Development, Molecular Neuroscience, Neurobiology of Disease

NU Scholar Profile

Recent Publications on PubMed

Current Research

Current Research

Neurons communicate with each other at synapses, extremely specialized and plastic structures able to adjust both quantitatively and qualitatively to correctly respond to a changing environment. The majority of neuronal communication is mediated by the activation of glutamate receptors (GluRs), which triggers mechanisms able to induce changes at synaptic level that are thought to underlie higher cognitive functions. Accordingly, GluRs are extremely well regulated in a cell- and synapse-specific manner. Several mechanisms including the control of expression/degradation level, intracellular trafficking or channel properties work coordinately to regulate GluRs. Not surprisingly, an aberrant GluR trafficking and/or function is a shared hallmark for many neurological disorders, including Alzheimer’s disease, Huntington’s disease, schizophrenia and autism.

The Sanz-Clemente Lab is interested in the molecular mechanisms underlying GluR trafficking in normal and altered conditions. We use a multidisciplinary approach including biochemistry, cell and molecular biology, pharmacology as well as a variety of imaging techniques and the analysis of genetically-altered mouse lines for elucidating how GluRs are controlled during development, in response to experience or other stimuli and what is their impact on synaptic function. Similarly, we investigate how the dysregulation of these mechanisms leads to synaptic alterations and, eventually, to neurological disorders. Current research focuses on NMDA Receptor (NMDAR) regulation and its role in the pathogenesis of Alzheimer’s disease.

Current projects
• Investigating the molecular mechanisms controlling the balance between synaptic and extrasynaptic NMDARs and its role in the pathogenesis of Alzheimer’s disease
• Investigating the molecular mechanisms underlying synapse unsilencing during development
• Studying the differential reorganization of synaptic protein content by typical and atypical antipsychotic drugs

Selected Publications

Selected Publications

1. Sanz-Clemente, A., Gray J.A., Ogilvie K.A., Nicoll R.A. and Roche, K.W. (2013) “Activated CaMKII couples GluN2B and Casein Kinase 2 to control synaptic NMDA receptors.” Cell Rep, S2211-1247.

2. Sanz-Clemente A., Nicoll R.A., Roche K.W. Diversity in NMDA Receptor Composition: Many Regulators, Many Consequences (2013). The Neuroscientist. 19(1);62-75

3. Chen, B.S., Gray J.A., Sanz-Clemente, A., Wei Z, Thomas, E.V., Nicoll R.A. and Roche, K.W. (2012) “SAP102 mediates synaptic clearance of NMDA receptors.” Cell Rep, 2(5)1120-8.

4. Matta, J.A., Ashby, M.C., Sanz-Clemente, A., Roche, K.W., and Isaac, J.T.R. (2011) “mGluR5 and NMDA Receptor Activation Are Required for the Experience- and Activity-Dependent Switch in NR2B to NR2A NMDA Receptor Subunit Composition.” Neuron, 70 (2) 339-351

5. Chen, B.S., Thomas, E.V., Sanz-Clemente, A., and Roche, K.W. (2011) “NMDA receptor-dependent regulation of dendritic spine morphology by SAP102 splice variants.” J. Neurosci., 31(1)89-96.

6. Sanz-Clemente, A., Matta, J.A., Isaac, J.R.T., and Roche, K.W. (2010) “Casein kinase 2 regulates the NR2 subunit composition of Synaptic NMDA Receptors.” Neuron, 67 (6) 984-996.

7. Lamarca, V., Marzo, I., Sanz-Clemente, A, Carrodeguas, JA. (2008) “Exposure of any of two proapoptotic domains of presenilin 1-associated protein/mitochondrial carrier homolog 1 on the surface of mitochondria is sufficient for induction of apoptosis in a Bax/Bak-independent manner.” Eur J. Cell Biol., 87 (5), 325-34.

8. Lamarca, V., Sanz-Clemente, A., Perez-Pe, R., Martinez-Lorenzo, M.J., Halaihel, N., Muniesa, P., and Carrodeguas, J.A. (2007) “Two isoforms of PSAP/MTCH1 share two proapoptotic domains and multiple internal signals for import into the mitochondrial outer membrane". Am J. Physiol. Cell Physiol., Oct; 293(4):C1347-61.

9. Lacor, P.N., Buniel, M.C., Furlow, P.W., Sanz-Clemente, A., Velasco, P.T., Wood, M., Viola, K.L., and Klein, W.L. (2007) “Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease”. J. Neurosci., 27:796-807.

10. Carrodeguas JA, Rodolosse A, Garza MV, Sanz-Clemente A, Perez-Pe R, Lacosta AM, Dominguez L, Monleon I, Sanchez-Diaz R, Sorribas V, Sarasa M (2005) The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing. Neuroscience 134:1285-1300