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    Last Name

    Maria A Morabito PhD

    TitleAssistant Professor
    InstitutionUniversity of Massachusetts Medical School
    DepartmentCell and Developmental Biology
    AddressUniversity of Massachusetts Medical School
    55 Lake Avenue North
    Worcester MA 01655
      Other Positions
      InstitutionUMMS - Graduate School of Biomedical Sciences
      DepartmentCell Biology

      InstitutionUMMS - Graduate School of Biomedical Sciences


        CDB Department Website

        Regulation of Glutamatergic Synapses in Development and Disease

        Dynamic changes in synaptic communication between neurons underlie normal processes such as brain development and learning and memory and are dysregulated in developmental, psychiatric and neurological disorders such as autism, schizophrenia, drug addiction, mood disorders, and Alzheimer's disease. The focus of our research is the identification of the molecular mechanisms that regulate glutamatergic synapses in order to better understand brain function and the etiology of neurological and psychiatric disorders.

        Neuronal circuits are formed during development and can undergo modifications throughout adulthood, for example in response to learning. The basic unit of neuronal circuitry and site of contact between neurons is the synapse. Glutamatergic synapses constitute the majority of excitatory synapses in the brain and their inputs are received by dendritic spines, which are actin-rich structures crucial for the regulation of synaptic function. Structural and functional alterations of glutamatergic synapses, including abnormalities in dendritic spines density and morphology, synapse loss, and altered synaptic signaling and plasticity have been associated with developmental, psychiatric, and neurologic disorders such as autism, schizophrenia, and Alzheimer's.

        An integral component of dendritic spines is the postsynaptic density (PSD), a cytoskeletal structure which organizes the postsynaptic signaling machinery. The PSD is molecularly complex and contains many classes of proteins including adhesion molecules and scaffolding, cytoskeletal, and signaling proteins. The PSD also contains NMDA and AMPA receptors, two types of glutamate receptors that play critical roles in learning and memory, neurological and psychiatric disorders. Studies from many laboratories have indicated that dendritic spines and their PSD are dynamic structures that are modified by neuronal activity, underlying LTP and LTD, two forms of synaptic plasticity related to learning and memory.

        My lab is interested in understanding the molecular and functional organization of dendritic spines in normal physiological conditions and in identifying alterations associated with synaptic dysfunction. We are using genetic, pharmacological, cellular, molecular, and imaging approaches to gain insight into the postsynaptic networks that regulate NMDA and AMPA receptor signaling and the morphology and stability of dendritic spines.

        Current projects in the laboratory:

        • Regulation of postsynaptic signaling and protein trafficking
        • Regulation of trans-synaptic adhesion and actin cytoskeleton dynamics
        • Synaptic dysfunction in brain disorders




        Figure 1: Rat hippocampal neuron in culture expressing -Gal to visualize the dendrites, and immunostained for -Gal (green) and PSD-95 (red), a protein enriched in postsynaptic structures, the dendritic spines.

        Rat hippocampal neuron in culture (above) expressing b-Gal (to visualize the dendrites) and immunostained for b-Gal (green) and PSD-95 (red), a protein enriched in dendritic spines.

        Synapse 3 Synapse EM
        Presynaptic and Postynaptic

        The postsynaptic density (dark area, above) is a highly organized, dynamic structure that contains NMDA and AMPA receptors (left). We are interested in identifying the molecular mechanisms that regulate NMDA and AMPA receptors signaling and their alterations in neurodegenerative and psychiatric disorders.


        Academic Background

        Ph.D., University of Rome, Italy, 1979


        Rotation Projects


        Research in our lab is focused on the regulation of glutamatergic synapses in the formation and function of synapses, and their dysfunction in neurological and psychiatric disorders. We identified novel mechanisms by which the Cdk5 kinase regulates glutamatergic synapses (Morabito et al., 2004; Roselli et al., 2005; Zhang et al., 2008). Available projects include the study of the function of postsynaptic scaffolding protein PSD-95 in brain development, synaptic plasticity, and psychiatric and neurodegenerative disorders using imaging, cell biological, and molecular techniques.

        selected publications
        List All   |   Timeline
        1. Bianchetta MJ, Lam TT, Jones SN, Morabito MA. Cyclin-Dependent Kinase 5 Regulates PSD-95 Ubiquitination in Neurons. J Neurosci. 2011 Aug 17; 31(33):12029-35.
          View in: PubMed
        2. Zhang S, Edelmann L, Liu J, Crandall JE, Morabito MA. Cdk5 regulates the phosphorylation of tyrosine 1472 NR2B and the surface expression of NMDA receptors. J Neurosci. 2008 Jan 9; 28(2):415-24.
          View in: PubMed
        3. Morabito MA, Sheng M, Tsai LH. Cyclin-dependent kinase 5 phosphorylates the N-terminal domain of the postsynaptic density protein PSD-95 in neurons. J Neurosci. 2004 Jan 28; 24(4):865-76.
          View in: PubMed
        4. Patzke H, Maddineni U, Ayala R, Morabito M, Volker J, Dikkes P, Ahlijanian MK, Tsai LH. Partial rescue of the p35-/- brain phenotype by low expression of a neuronal-specific enolase p25 transgene. J Neurosci. 2003 Apr 1; 23(7):2769-78.
          View in: PubMed
        5. Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH. The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner. J Neurosci. 2002 Sep 15; 22(18):7879-91.
          View in: PubMed
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        This is an official Page/Publication of the University of Massachusetts Worcester Campus
        Office of the Vice Provost for Research, 55 Lake Ave North, Worcester, Massachusetts 01655
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