Gerardo A Morfini
Email Address: gmorfini@uic.eduCollege: 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 unique ability of neurons to receive, process, and transmit information depends upon the polarized distribution of cellular components within discrete subcellular compartments (i.e., axons and dendrites). Such distribution in turn depends upon intracellular trafficking events executed by motor proteins, a process collectively referred to as axonal transport. An illumination of molecular mechanisms regulating axonal transport is therefore critical for a comprehensive understanding of neuronal function. Within this context above, our studies over the last years identified specific protein kinases that regulate AT by phosphorylating motor proteins. These findings bear significant implications for the pathogenesis of human neurodegenerative diseases including Alzheimer’s disease, Huntington’s disease, Parkinson’s disease, and Amyotrophic Lateral Sclerosis, as all these diseases feature abnormal activation of protein kinases and deficits in axonal transport. Our current research aims to evaluate the contribution of specific protein kinases to the progressive loss of neuronal connectivity that characterizes neurodegenerative diseases. Knowledge derived from this work will provide a conceptual framework for the development of novel therapeutic targeting based on kinase inhibitors to preserve axonal transport and neuronal function. Selected publications - Leo L, Weissmann C, Burns M, Kang M, Song Y, Qiang L, Brady ST, Baas PW, Morfini G. (2017) Mutant spastin proteins promote deficits in axonal transport through an isoform-specific mechanism involving casein kinase 2 activation. Hum Mol Genet. 15;26(12):2321-2334. - 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. - Morfini et al (2013). Inhibition Of Fast Axonal Transport By Pathogenic SOD1 Involves Activation of P38 MAP Kinase. PLOS One 8(6):e65235. - 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. - 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. - Morfini et al (2009) Axonal transport defects in neurodegenerative diseases. J. Neurosci. 29, 12776-12786. - 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), which have taken a course in at least one and preferably two 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. 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. Contact researcher via URE Email Webform
