Gerardo A Morfini

    Email Address:
    College: Medicine Department: Anatomy and Cell Biology
    Title: Associate Profesor
    Office: COMRB 7053 Phone: 312-996-6869
    Participating in the Chancellor’s Undergraduate Research Awards program: Yes

    Research Interest:
    The exquisitely organized distribution of cellular components within discrete subcellular compartments underlies the unique ability of neurons to receive, process, and transmit information. Targeting and delivery of these components in mature neurons largely depends upon axonal transport (AT), a cellular mediated by molecular motor proteins including conventional kinesin and cytoplasmic dynein.

    An illumination of molecular mechanisms regulating AT is critical for a comprehensive understanding of neuronal function. Within this context, our studies over the last years identified specific protein kinase pathways that regulate AT through phosphorylation of motor proteins. Interestingly, genetic evidence indicates that alterations in AT may play a critical role in various human neurodegenerative diseases including Alzheimer’s disease, Huntington’s disease, Parkinson’s disease, and Amyotrophic Lateral Sclerosis, among others. Based on these observations, our current research aims to evaluate the contribution of specific protein kinases to the progressive loss of neuronal connectivity that characterizes these diseases. Knowledge derived from this work will provide a conceptual framework for the development of novel therapeutic strategies aimed to preserve neuronal connectivity.

    Selected publications

    1. Gatto et al (2015). Analysis of YFP(J16)-R6/2 reporter mice and postmortem brains reveals early pathology and increased vulnerability of callosal axons in Huntington's disease. Hum Mol Genet. 24(18):5285-98.
    2. Morfini et al (2013). Inhibition Of Fast Axonal Transport By Pathogenic SOD1 Involves Activation of P38 MAP Kinase. PLOS One 8(6):e65235.
    3. Kanaan et al (2011) Pathogenic Forms of Tau Inhibit Kinesin-Dependent Axonal Transport Through a Mechanism Involving Activation of Axonal Phosphotransferases. J. Neurosci. 31(27):9858-68.
    4. Bosco et al (2010) Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat. Neurosci. 13(11):1396-403.
    5. Pigino, et al. (2009) Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid beta. Proc. Natl. Acad. Sci. USA 106, 5907-5912.
    6. Morfini et al (2009) Axonal transport defects in neurodegenerative diseases. J. Neurosci. 29, 12776-12786.
    7. Morfini et al (2009) Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin. Nat. Neurosci. 12, 864-871.

    Minimum time commitment in hours per week: 15

    Qualifications of a Student:
    Priority is given primarily to Biology/Chemistry majors with top GPAs (>3.5). Taken a course in at least one and preferably tow of the following areas: neuroscience, cell biology, biochemistry or molecular biology. Sophomores pursuing Medical/Graduate school are encouraged to apply. Prior research experience is an advantage but not necessary. Applicant should have excellent communication and team-work skills, be mature, organized and reliable. Candidate must be able to devote at least 15 hours/week.

    Brief Summary of what is expected from the student:
    The student should be willing to make a sustained commitment with a regular schedule during the school year. Summer research options are only available to students that have been involved during the academic year. Students interested in a multiyear experience are preferred.Lab time is expected to be devoted to lab activities only. Students should expect to start a training period where they will be under the supervision of a senior lab member to learn general lab duties and techniques. After this period and with evidence of gained precision, commitment and trouble-shooting skills, students are expected to become fully embedded in a particular project under the direction of a project leader.

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