Camberg Cell Physiology and Protein Mechanics Lab

University of Rhode Island
Department of Cell and Molecular Biology

Welcome to our lab website. We study protein machines and their impacts on cell growth. We work in a variety of model systems to understand how protein reorganization and remodeling events drive cellular changes.

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Cell Division & Developmental Growth Programs

Understanding the Molecular Mechanism of Cell Division

FtsZ is a highly conserved bacterial cell division protein that is a structural homolog of tubulin and polymerizes to form a dynamic protein structure called the Z-ring at midcell. At the Z-ring, the center of an E. coli cell constricts and new cell wall is built at the septum to divide the cell into two identical progeny cells. Using live cell tracking in vivo and reconstituted division machinery in vitro, we investigate proteins that recruit, stabilize and destabilize the Z-ring, as well as systems responsible for precise timing and placement of the Z-ring in vivo. The actin-like ATPase FtsA polymerizes, coassembles with FtsZ polymers, and together they form the nascent Z-ring at the site of division. We are pioneering methods to study FtsA-FtsZ complexes and determine how they contribute to initiating cell wall synthesis during division.

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Protein Homeostasis

Chaperone-mediated remodeling and proteolysis

Molecular chaperone proteins maintain intracellular protein homeostasis in all living organisms. When these homeostatic mechanisms are disrupted, cells are less able to cope with environmental stress and maintain normal physiology and function. We study how proteins misfold and aggregate, how molecular chaperones promote reactivation from aggregates and amyloids, and how chaperones partner with proteases for degradation in vivo and in vitro.
Protein homeostasis in bacteria, yeast & differentiated neurons:
We are currently studying key cellular events that are proteolytically regulated across multiple model organisms, including cell division, toxin-antitoxin systems, dormancy, prion inheritance and clearance of amyloids and other aggregates.

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The Antibiotic-Tolerant State of Quiescence in Bacteria is Regulated by Peptidoglycan Cues

Uropathogenic E. coli is responsible for the majority of urinary tract infections. We investigate how this organism enters a dormant, non-proliferative and antibiotic-tolerant state, which may allow it to evade killing by antibiotics or the immune system during infection. Our work is focused on understanding how external cues, including peptidoglycan peptides and TCA cycle metabolites, stimulate proliferation of E. coli from the quiescent state. We are developing a new model of bladder epithelial cell invasion to study intracellular quiescence and antibiotic tolerance. 

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For our full list of publications:

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