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Bruce E. Vogel, PhD

Academic Title:

Assistant Professor

Primary Appointment:

Physiology

Location:

BioMET 307B

Phone (Primary):

(410) 706-4516

Fax:

(410) 706-8184

Education and Training

B.A.     Biochemistry, Rutgers College, New Brunswick, NJ

Ph.D.    Biochemistry, Rutgers Medical School and Rutgers   University, Piscataway, NJ

Postdoctoral fellow -La Jolla Cancer Research Foundation, La Jolla, CA.  

Postdoctoral fellow  Department of Biology, Johns Hopkins University

Biosketch

My laboratory is interested in the regulation of morphogenesis during development, with a specific interest in how extracellular matrix proteins, transmembrane receptors, and cytoskeletal adapters work together to specify tissue architecture. We primarily use C. elegans as a model organism to study the nematode orthologs of conserved extracellular proteins that are defective in human diseases. In the past we have discovered hemicentin and identified functional interactions between hemicentin and fibulin. These two proteins have been implicated in Age-Related Macular Degeneration (ARMD), a common human disease that is characterized by progressive degeneration of sensory neurons, called photoreceptors, in the retina. Currently, we are studying how interactions between these two proteins and complement factor H (a secreted protein that is frequently mutated in ARMD patients) affect sensory neuron function in C. elegans.

 

Highlighted Publications

Vogel, BE and Hedgecock, EM. (2001) Hemicentin, a conserved extracellular member of the immunoglobulin superfamily, organizes epithelial and other cell attachments into oriented line-shaped junctionsDevelopment 128:883-894. 

Muriel, JM, Dong, C, Hutter, H and Vogel, BE. (2005) Fibulin-1C and Fibulin-1D splice variants have distinct functions in C. elegans development and assemble in a hemicentin dependent manner. Development 132:4223-4234. 

Dong, C, Muriel, JM, Ramirez, S, Hutter, H, Hedgecock, EM, Breydo, L, Baskakov, IV and Vogel, BE (2006) Hemicentin assembly in the extracellular matrix is mediated by distinct structural modulesJ. Biol. Chem. 281:23606-23610. 

Muriel, JM, Xu, X and Vogel, BE. (2006) Selective assembly of fibulin-1 splice variants reveals distinct extracellular matrix networks and novel functions for Perlecan/UNC-52 splice variantsDev. Dyn. 235:2632-40. 

Vogel BE, Muriel JM, Dong C, Xu X. (2006) Hemicentins: what have we learned from wormsCell Res. 16:872-8. 

Xu X, Dong C, Vogel BE. (2007) Hemicentins assemble on diverse epithelia in the mouseJ Histochem Cytochem. 55:119-26.

Xu X and Vogel BE. (2011) A secreted protein promotes cleavage furrow maturation during cytokinesisCurr Biol. 21:114-9.  PMCID: PMC3046554

Vogel BE, Wagner C, Paterson JM, Xu X, Yanowitz JL.  (2011)  An extracellular matrix protein prevents cytokinesis failure and aneuploidy in the C. elegans germline.  Cell Cycle. Jun 15;10(12):1916-20. Epub 2011 Jun 15.  PMCID: PMC3154414

Xu X, Vogel BE.  (2011) A new job for ancient extracellular matrix proteins: Hemicentins stabilize cleavage furrowsCommun Integr Biol. Jul; 4(4):433-5. doi: 10.4161/cib.4.4.15324. Epub 2011 Jul 1.  PMCID: PMC3181513

Muriel JM, Dong C, Vogel BE.  (2012) Distinct regions within fibulin-1D modulate interactions with hemicentin.  Exp Cell Res. 2012 Dec 10; 318 (20) : 2543-7. doi: 10.1016/j.yexcr.2012.08.007. Epub 2012 Sep 7.  

Zhong Y, Wang J, Henderson MJ, Yang P, Hagen BM, Siddique T, Vogel BE, Deng HX, Fang S.  (2017) Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus.  Elife. 2017 May 2;6. pii: e23759. doi: 10.7554/eLife.23759. PMCID: PMC5449186

Research Interests

Research Specialties: Developmental Cell Biology, cell architecture, tissue morphogenesis, extracellular matrix



Where is hemicentin expressed?

We have constructed a functional fusion between hemicentin and green fluorescent protein (GFP), enabling us to monitor hemicentin-GFP localization in live animals during development. Hemicentin accumulates at sites where epithelial cells make long, line-shaped attachments to a number of tissues including specific uterine cells and subsets of neurons, including those involved in mechanosensation (figure 2). 

Our current focus is on using molecular, genetic and biochemical techniques to identify the functional significance of hemicentin structural domains and on identifying cell surface receptors and other extracellular proteins that functionally interact with hemicentin. 

The long-term goal is to understand the function of extracellular matrix proteins in the modification of epithelial cell architecture. Specific questions that we plan to address include: What are the roles of vertebrate hemicentins? How can hemicentin be used in the design of bioactive synthetic matrices to regulate the morphogenesis of engineered tissues?

Research Images

Figure 1. Schematic of hemicentin structure. Unique, but highly conserved N and C terminii flank 48 tandem Ig and 3 EGF modules.
Figure 2. Hemicentin-GFP assembles into polymers on the surface of neurons (A,B), between head muscles and pharynx (C), and in the ovary (D).

Lab Techniques and Equipment

We use a wide variety of Molecular, Genetic, Biochemical and Cell Biology techniques that include (but are not limited to): 
 
Forward Genetic Screens using random mutagenesis, Reverse Genetic Screens Using RNAi, site directed mutagenesis, GFP tags of proteins, light and electron microscopy, immunohistochemistry, protein purification