ELIZABETH SCOTTO-LAVINO, PH.D.

** ****** ****, **** ********, New York 11733

H: 631-***-**** - bfok2t@r.postjobfree.com - C: 631-***-****

EXPERIENCED SCIENTIST

Diligent researcher possessing a PhD in Molecular and Cellular Pharmacology and an excellent set of transferable skills to positively contribute to positions within the biotechnology and pharmaceutical research fields.

RESEARCH EXPERIENCE

Stony Brook University, Stony Brook, NY January 2011-present

POSTDOCTORAL ASSOCIATE, DEPARTMENT OF ORAL BIOLOGY & PATHOLOGY

Brookhaven National Laboratory, Upton, NY 2009-2011

POSTDOCTORAL ASSOCIATE, DEPARTMENT OF BIOLOGY

Overexpressed several endogenous cytoplasmic proteins identified as substrates for GroEL-mediated folding to examine effects on protein folding under conditions of saturated chaperone activity. Four different effects were observed: (i), normal folding; (ii), production of insoluble aggregates; (iii), production of soluble protein with membrane-lytic activity; and (iv), production of soluble protein that was mislocalized to the periplasmic space.

Stony Brook University, Stony Brook, NY 2006-2009

GRADUATE RESEARCHER (2006-2009)

Investigated the regulation of epithelial cell migration, wound healing, and cellular morphology by the myosin phosphatase (MP) enzyme complex. The MP complex includes a catalytic subunit (type 1 protein phosphatase, PP1), and a myosin light chain (MLC) targeting subunit (MYPT). Phosphatidic acid (PA) has been reported to inhibit the catalytic activity of MP in vitro. Identified the enzyme phospholipase D2 (PLD2) as the in vivo generator of the PA pool that regulates MP activity at the plasma membrane in the context of cell morphology (upon attachment and spreading from a state of suspension). Increased PLD2 activity suppresses MP activity, which leads to increased MLC phosphorylation at the plasma membrane and inhibition of cell spreading. Conversely, inhibition or depletion of PLD2 leads to hyperactivation of MP, which results in MLC dephosphorylation and accelerated spreading. This model system can be used to determine the role of the PLD2 MP signaling pathway in cellular morphology and migration in tumor cells as the initial step in developing a new approach for cancer therapeutics. This information can drive the development of chemotherapeutic agents such as Taxol®, which target components of the cell infrastructure particularly important for tumor cell metastasis. This data can be used to determine the role of MYPT1 and PP1 in cellular morphology and migration as well as to confirm the role of phospholipids in the regulation of myosin phosphatase activity.

GRADUATE RESEARCHER (2003-2006)

Examined the role of of ubiquitination in the regulation Ras activity. The small GTPase Ras plays a role in several biological pathways. There are three different isoforms of Ras named H, N and KRas. H and KRas are nearly 90% homologous to one another, and differ only in a region at their C-terminus termed the hypervariable region (HVR). KRas is preferentially mutated in 30% of all cancers. H and KRas traffic and localize to different subdomains of the plasma membrane and also differentially activate downstream effector pathways of Ras. HRas but not KRas is sorted to the endocytic pathway. Ubiquitination of membrane-associated proteins and receptors often serves to target proteins to the endocytic pathway. Studied the ubiquitination of HRas within the cell and the relationship between HRas ubiquitination and the sorting of HRas in the endocytic pathway. HRas is subject to ubiquitin conjugation, whereas KRas is refractory to this modification. The membrane-anchoring domain of HRas is necessary and sufficient to

ELIZABETH SCOTTO-LAVINO, PH.D. - PAGE 2

RESEARCH EXPERIENCE (CONTINUED)

direct the mono- and diubiquitination of HRas. Ubiquitin attachment to HRas stabilizes its association with endosomes and modulates its ability to activate the Raf/MAPK signaling pathway. Therefore, differential ubiquitination of Ras proteins may control their location-specific signaling activities.

UNDERGRADUATE RESEARCH (1998-2002)

Worked on developing a sequential enzymatic digestion protocol for determining the components of the extracellular matrix secreted by human prostate cancer cells. Tested the permeability of certain drug compounds on epithelial cells using the MatTek© EpiAirway™ Tissue Model System.

TEACHING EXPERIENCE

Stony Brook University, Stony Brook, NY 2005

TEACHING ASSISTANT

Teaching assistant for the Undergraduate Pharmacology Program; aided both the lecture and laboratory courses (Practicum in Teaching Pharmacology).

EDUCATION & AFFILIATIONS

Doctor of Philosophy, Molecular and Cellular Pharmacology

STONY BROOK UNIVERSITY, SCHOOL OF MEDICINE, Stony Brook, NY

Bachelor of Science, Pharmacology

STONY BROOK UNIVERSITY, Stony Brook, NY

Memberships

Brookhaven Women in Science

Sigma Xi (The Scientific Research Society)

ASPET (The American Society for Pharmacology and Experimental Therapeutics)

SKILLS

Western Blotting

Fluorescence Microscopy

SDS-PAGE Gel electrophoresis Molecular Cloning

Mammalian Tissue Culture

Odyssey Infrared Imaging System

HONORS & AWARDS

2009 OSI Fellow Mentoring Program February 2009-December 2010

Stony Brook University: NIH Training Grant Molecular Genetics and Microbiology 2003-2006

Stony Brook University: NIH Training Grant Pharmacological Sciences 2002-2003

ABSTRACTS

Roemer, E., Simon, S., Easow, J., Scotto-Lavino, E. (2002) An In Vitro Model for the Rapid Screening of Potential Components and Formulations for Nasal Drug Delivery; Evaluation of the Penetration and Cytotoxic Effects of Drug Formulations on an In Vitro Nasal Mucousal Model. Journal of the Society for In Vitro Toxicology: IN VITRO, Cellular and Developmental Biology; Volume 38; ABSTRACT; Spring 2002.

ELIZABETH SCOTTO-LAVINO, PH.D. - PAGE 3

ABSTRACTS (CONTINUED)

Roemer, E., Simon, S., Sawka, H., Scotto-Lavino, E. (2001) A Method for the Synthesis of Stromal Extracellular Matrix (ECM) by Normal Human Prostate Cells in Culture. Journal of the Society for In Vitro Toxicology: IN VITRO, Cellular and Developmental Biology; Volume 37; Number 3, Part II; March 2001.

Roemer, E., Simon, S., Sawka, H., Scotto-Lavino, E. (2000) Evaluation of the Composition of the Extracellular Matrix (ECM) Synthesized by Human Prostate Stromal Cells in Culture. Journal of the Society for In Vitro Toxicology: IN VITRO, Cellular and Developmental Biology; Volume 36; Number 3, Part II; March 2000.

Poster Presenter Molecular Genetics & Microbiology Departmental Retreat, Stony Brook University, October 2009.

PUBLICATIONS

Jura N., Scotto-Lavino E., Sobczyk A., Bar-Sagi D.; Differential modification of ras proteins by ubiquitination.; Mol Cell. (2006); 21(5): 679-687.

Scotto-Lavino E, Du G, Frohman MA.; Amplification of 5' end cDNA with 'new RACE'; Nat Protoc. (2006); 1(6):3056-61.

Scotto-Lavino E, Du G, Frohman MA.; 3' end cDNA amplification using classic RACE.; Nat Protoc. (2006); 1(6):2742-5.

Scotto-Lavino E, Du G, Frohman MA.; 5' end cDNA amplification using classic RACE; Nat Protoc. (2006); 1(6):2555-62.

Zamurrad, S., L.J. Crawford, E. Scotto-Lavino, N. Napolitano, S.R. Simon and E.J. Roemer; In Vitro Synthesis of Stromal ECM by Normal Human Cells (2009); Manuscript in preparation.

Yeku O., Scotto-Lavino E., Frohman MA.; Identification of alternative transcripts using rapid amplification of cDNA ends (RACE); Methods Mol Biol. (2009); 590:279-94.

Scotto-Lavino E., Garcia-Diaz M., Du G, Frohman MA.; Basis for the isoform-specific interaction of myosin phosphatase subunits protein phosphatase 1c beta and myosin phosphatase targeting subunit 1; J Biol Chem. (2010); 285(9):6419-6424.

Scotto-Lavino E, Bai M, Zhang YB, Freimuth P.; Export is the default pathway for soluble unfolded polypeptides that accumulate during expression in Escherichia coli; Protein Exp

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