Overview

Division of Cell Biology, Yale University School of Medicine, Fulbright Fellow, April 1979-May 1980
Department of Cell Biology, Harvard Medical School, Postdoctoral Fellow, September 1993-August
2001
Department of Cell and Developmental Biology, Oregon Health Sciences University, Research
Assistant Professor, August 2001-December 2001
Department of Physiology and Biophysics, Case Western Reserve University (Case Medical School),
Assistant Professor, January 2002-April 2007
Department of Pharmacology and Physiology, New Jersey Medical School, University of Medicine
and Dentistry of New Jersey, Associate Professor, April 2007-June 2013
Department of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers
University, Associate Professor, July 2013-Present

Education

PHD, 1993, University of Kansas
M.S., 1975, University of Bucharest, Romania

Curriculum Vitae

View CV

Relevant Publications

Muresan, V., and Ladescu Muresan, Z. Shared Molecular Mechanisms in Alzheimer's Disease and Amyotrophic Lateral Sclerosis: Neurofilament-dependent Transport of sAPP, FUS, TDP-43, and SOD1, with Endoplasmic Reticulum-like Tubules. Neurodegenerative Diseases. 16: 55-61, 2016. PubMed Central PMCID: PMC4681536.

Villegas, C., Muresan, V., and Ladescu Muresan, Z. Dual-tagged Amyloid-?? Precursor Protein Reveals Distinct Transport Pathways of its N- and C-terminal Fragments. Human Molecular Genetics. 23: 1631- 1643, 2014. PubMed Central PMCID: PMC3929097.

Muresan, V., and Muresan, Z. A Persistent Stress Response to Impeded Axonal Transport Leads to Accumulation of Amyloid-?? in the Endoplasmic Reticulum, and Is Probable Cause of Sporadic Alzheimer's Disease. Neurodegenerative Diseases. 10: 60-63, 2012. PubMed Central PMCID: PMC3363352.

Muresan, V., Varvel, N.H., Lamb, B.T., and Muresan, Z. The Cleavage Products of Amyloid-?? Precursor Protein Are Sorted to Distinct Carrier Vesicles that Are Independently Transported within Neurites. Journal of Neuroscience 29: 3565-3578, 2009. Featured in This week in the Journal. PubMed Central PMCID: PMC2669751.

Muresan, Z., and Muresan, V. 2007. Seeding Neuritic Plaques from the Distance: A Possible Role for Brainstem Neurons in the Development of Alzheimer's Disease Pathology. Neurodegenerative Diseases. 5: 250-253, 2008. PubMed Central PMCID: PMC2562573.

Muresan, Z., and Muresan, V. 2007. The Amyloid-?? Precursor Protein is Phosphorylated via Distinct Pathways during Differentiation, Mitosis, Stress, and Degeneration. Mol. Biol. Cell. 18: 3835-3844. PubMed Central PMCID: PMC1995701.

Muresan, Z., and Muresan, V. 2006. Neuritic Deposits of Amyloid-beta Peptide in a Subpopulation of Central Nervous System-derived Neuronal Cells. Mol. Cell. Biol. 26: 4982-4997. PubMed Central PMCID: PMC1489158.

Muresan, Z., and Muresan, V. 2005. Coordinated Transport of Phosphorylated Amyloid-beta Precursor Protein and cJun NH2-terminal Kinase-Interacting Protein-1. J. Cell Biol. 171: 615-625. PubMed Central PMCID: PMC2171566.

Muresan, Z., and Muresan, V. 2005. JNK-Interacting Protein-3 Facilitates Phosphorylation, and Controls Localization of Amyloid-beta Precursor Protein. J. Neurosci. 25: 3741-3751. PubMed Central PMCID: PMC6724916.

Muresan, Z., and Muresan, V. 2004. A Phosphorylated, Carboxy-terminal Fragment of beta-Amyloid Precursor Protein Localizes to the Splicing Factor Compartment. Hum. Mol. Genet 13: 475-488. PubMed PMID: 14722157.

Areas Of Interest

Axonal transport

Cell death in neurodegeneration

Crosstalk between mechanisms of disease

Mechanisms of neuronal homeostasis

Nonconventional functions of microtubule motors

Pathogenic mechanisms in Alzheimers disease

Course List

DENT7106Q		Dental Histology
PHPYN5030		Topics in Pharmacology
67185600Q
CBMMN5001		Basic Histology
CBNP5036Q		Mol Phys of Cell Comm

Pathogenic Mechanisms in Neurodegenerative Diseases

Presently, most of our research is disease-oriented. Starting from the analysis of axonal transport in
neurodegenerative diseases (specifically, Alzheimer???s disease - AD, Down???s syndrome, amyotrophic
lateral sclerosis, and lissencephaly), we became more and more interested in the mechanism of the
disease, even if this transgressed the study of axonal transport.

1. Based initially on work that compared the propensity to generate, accumulate, and export amyloid-
??? (A???), of neurons from different brain regions, we proposed that the A??? oligomers first appear within
locus ceruleus neurons, and are then transmitted remotely to lesion-prone areas by the neurites of
the locus coeruleus (LC) neurons, which project throughout the CNS. According to our hypotheses,
while plaques do not develop in the LC, the ???bad seed??? of aggregated A???, which later nucleates the
plaques, is initially produced in LC neurons. We currently test this hypothesis using post-mortem
human brain.

2. We recently proposed a novel pathogenic, molecular mechanism in late onset AD: it links the
deficiencies in long-distance transport, typical for old age, to the generation and oligomerization of A??,
and to Tau phosphorylation and aggregation. Few - if any - mechanisms of AD proposed so far can
explain both the A?? and the Tau pathology. Ours does: both pathologies are part of a mechanism o
homeostasis, and begin as a reaction of the neuron to impeded axonal transport. They are aimed at
(1) preventing the clogging of the secretory pathway (the A?? that accumulates in ER exerts a
chaperone-like activity, and prevents futile exit of proteins along the blocked secretory route), and (2)
speeding up transport (by phosphorylation ??? and release from microtubules ??? of Tau, and by
nucleation of microtubules by the newly formed phosphorylated Tau droplets).

3. We proposed a novel form of intracellular transport of membrane, membrane-associated, and
secretory proteins. We hypothesized that a fraction of the cargo destined for delivery to the neurites
is transported with specialized endoplasmic reticulum (ER) tubules penetrating into the neurites,
reaching the terminal. Also, we proposed that these ER protrusions are likely carried by attaching to
moving cytoskeletal polymers, such as short neurofilament segments and/or ???squiggles???, rather than
recruiting kinesin motors themselves, and moving along microtubules. Thus, ER tubules could take a
ride by piggybacking on short intermediate filaments, which themselves move along stationary
microtubules. We continue to examine the possibility of cargo transport with ER tubules, and the role
of neurofilaments in this novel form of motility. We focus on the transport of disease-relevant proteins
(APP, SOD1, FUS, and TDP-43), which we tentatively identified as cargo carried to neurite terminals
with ER protrusions, in a peripherin (a neurofilament protein)-dependent manner.