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Basic Science Leadership Changes

Dear Colleagues,

As 2009 comes to a close, I would like to take this opportunity to wish you well and to announce these important changes for senior leadership within the departments of Cell and Developmental Biology and Cancer Biology. These changes are effective January 1.

First, I would like to address leadership changes within the Department of Cell and Developmental Biology.

In order to better address increasing responsibilities in her role as the associate vice chancellor for Research and senior associate dean for Biomedical Sciences, Susan Wente has decided to step down as chair of the Department of Cell and Developmental Biology after serving in this role since 2002.

Under Susan’s leadership Cell and Developmental Biology has recruited and retained a number of highly sought faculty, nurtured cross-campus collaborations, and helped launch many new research initiatives. The department’s extramural research grant portfolio increased nearly 73 percent during this time. Of great importance, she also devoted critical effort to mentoring faculty, students and fellows and developing new programs to support these endeavors. With Susan’s stewarding, the department’s contributions to our graduate and medical education efforts have grown. In fact, the number of department graduate students has expanded from 45 to 85 over the past 7 years.

Susan will continue to serve actively as professor within the department and oversee her NIH-funded research program. I am grateful for her service to the department and her willingness to continue leading initiatives on an institutional level.

We are quite fortunate that Bill Tansey, Ingram Professor of Cancer Research and professor of Cell and Developmental Biology, has agreed to take over as the department’s interim chair.

Bill was recently recruited to VUMC and is fully prepared to handle this transition given his prior leadership roles directing the Watson School of Biological Sciences at Cold Spring Harbor Laboratory, and his current efforts as co-leader of the VICC Genome Maintenance Program and scientific director of the Vanderbilt Microarray Shared Resource. Bill’s internationally recognized research program uses model systems to study mechanisms of transcriptional regulation. I am most pleased to welcome Bill to this key position within our leadership.

Secondly, please join me in welcoming home Lynn Matrisian as she returns from a scholarly leave to resume her service as chair of Cancer Biology.

As many of you know, Lynn and Vanderbilt were honored by the National Cancer Institute’s invitation to Lynn to serve on the NCI’s Translational Research Working Group. This important endeavor has resulted in the creation of Translational Research Advisory Committees (internal and external to NIH), a new system for coding translational grants, and the inception of an annual meeting of more than 800 translational cancer researchers.

The Working Group also initiated a new process to identify translational research opportunities which merit acceleration and developed a new funding mechanism for these opportunities (“STRAPs” -- Special Translational Research Acceleration Projects). The first cycle of applications and awards is now unfolding, and Lynn will continue to assist the Working Group in guiding this process over the next year. I am thrilled that Lynn has represented Vanderbilt in helping to shape the national vision for translational cancer research.

I want to offer special thanks also to Hal Moses for so ably serving as interim chair during Lynn’s service at NCI. The department and Medical Center have been fortunate indeed in benefitting from this latest example of Hal’s leadership and service to Vanderbilt.

Please join me in offering Susan, Bill, Lynn, and Hal congratulations and appreciation for their past and future contributions to Vanderbilt.

Best wishes for a wonderful holiday season. I expect that 2010 will provide us with many opportunities to extend VUMC’s ever-growing record of contributions.

Sincerely,
Jeffrey R. Balser, M.D., Ph.D.
Vice Chancellor for Health Affairs
Dean, School of Medicine
Vanderbilt University Medical Center

Fall Newsletter November 2009

11.09 CDB Fall Newsletter

Chancellor’s Awards for Research

Irina Kaverina and others, recognized with Chancellor’s Awards for Research, which recognizes excellence in research, scholarship or creative expression.

Chancellor's Awards Page

 

VUcast faculty assembly

Sonic hedgehog signaling regulates a novel epithelial progenitor

Sonic hedgehog signaling regulates a novel epithelial
progenitor domain of the hindbrain choroid plexus.

Huang X, Ketova T, Fleming JT, Wang H, Dey SK, Litingtung Y, Chiang C.

Development. 2009 Aug;136(15):2535-43. Epub 2009 Jul 1.

Note that VUMC reporter will do an aliquot report on this paper on August 14

2. Shh and Gli3 activities are required for timely generation of motor neuron progenitors.

 

Abstract

Generation of distinct ventral neuronal subtypes in the developing spinal cord requires Shh signaling mediated by the Gli family of transcription factors. Genetic studies of Shh−/−;Gli3−/− double mutants indicated that the inhibition of Gli3 repressor activity by Shh is sufficient for the generation of different neurons including motor neurons. In this study, we show that although ventral neural progenitors are initiated in normal numbers in Shh−/−;Gli3−/− mutants, the subsequent appearance of motor neuron progenitors shows a  20-hour lag, concomitant with a delay in the activation of a pan-neuronal differentiation program and cell cycle exit of ventral neural progenitors. Accordingly, the Shh−/−;Gli3−/− mutant spinal cord exhibits a delay in motor neuron differentiation and an accumulation of a ventral neural progenitor pool. The requirement of Shh and Gli3 activities to promote the timely appearance of motor neuron progenitors is further supported by the analysis of Ptch1−/− mutants, in which constitutive Shh pathway activity is sufficient to elicit ectopic and premature differentiation of motor neurons at the expense of ventral neural progenitors. Taken together, our analysis suggests that, beyond its well established dorso-ventral patterning function through a Gli3-derepression mechanism, Shh signaling is additionally required to promote the timely appearance of motor neuron progenitors in the developing spinal cord.

Oh S, Huang X, Liu J, Litingtung Y, Chiang C.

Dev Biol. 2009 Jul 15;331(2):261-9. Epub 2009 May 9.

 

Microvilli give gut vesicles the brush-off

Microvilli give gut vesicles the brush-off

A surprising new function for intestinal cells in shaping theirlocal environment.Every cell lining the small intestine bristles with thousandsof tightly packed microvilli that project into the gut lumen,forming a brush border that absorbs nutrients and protects thebody from intestinal bacteria. McConnell et al. now find thatmicrovilli extend their functional reach even further usinga molecular motor to send vesicles packed with gut enzymes outinto the lumen to get a head start on breaking down their substrate

CDB June 09 Newsletter

"VCDB June 2009 Binary" Newsletter

Chemicals turn human embryonic stem cells towards beta cells

Chemicals turn human embryonic stem cells towards beta cells

 

nature chemical biology 5, 195 - 196 (2009) doi:10.1038/nchembio0409-195

Yu-Ping Yang1 & Chris Wright1

  1. Yu-Ping Yang and Chris Wright are in the Department of Cell and Developmental Biology and the Vanderbilt University Program in Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee, USA. e-mail: chris.wright@vanderbilt.edu

Small-molecule library screening identifies simple imitators of the cellular signaling events that normally guide formation of the pancreas and its insulin-secreting beta cells, further enabling detailed analysis in vitro, or eventual diabetes therapies via large-scale differentiation
of human stem cells.

Defining elements in contractile ring assembly

Defining elements in contractile ring assembly

 

 

Vanderbilt Reporter, Lords of the contractile ring

 


Cell division requires the formation of a contractile ring. While many protein components of this ring are known, how they interact with each other and with the plasma membrane remains unclear.

Rachel Roberts-Galbraith, Kathy Gould, Ph.D., and colleagues are studying these ring proteins in yeast. One such protein, Cdc15, has two “domains” that carry out different functions – the F-BAR domain, which binds and curves the plasma membrane, and the SH3 domain, which had not been characterized.

In the January Journal of Cell Biology, the researchers show that the SH3 domains of Cdc15 and of another member of the same protein family (Imp2) recruit other proteins (including a paxillin-like protein Pxl1 and a highly conserved C2-domain protein Fic1) to the contractile ring. Together, Pxl1 and Fic1 add structural integrity to the contractile ring and prevent it from fragmenting during cell division. The SH3 domains of Cdc15 and Imp2 overlap in function, and the authors suggest that this redundancy is essential for division of the cellular contents.

 


RR_Gould.jpg

 

— Melissa Marino, Vanderbilt Reporter

 

 

 

See Also PubMed Article

 

Roberts-Galbraith, R.H., Chen, J.-S., Wang, J. and Gould, K.L. (2009) The SH3 domains of two PCH family members cooperate in construction of the Schizosaccharomyces pombe contractile ring. J. Cell Biol. 184:113-127.

 

Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA.

Schizosaccharomyces pombe cdc15 homology (PCH) family members participate in many cellular processes by bridging the plasma membrane and cytoskeleton. Their F-BAR domains bind and curve membranes, whereas other domains, typically SH3 domains, are expected to provide cytoskeletal links. We tested this prevailing model of functional division in the founding member of the family, Cdc15, which is essential for cytokinesis in S. pombe, and in the related PCH protein, Imp2. We find that the distinct functions of Imp2 and Cdc15 are SH3 domain independent. However, the Cdc15 and Imp2 SH3 domains share an essential role in recruiting proteins to the contractile ring, including Pxl1 and Fic1. Together, Pxl1 and Fic1, a previously uncharacterized C2 domain protein, add structural integrity to the contractile ring and prevent it from fragmenting during division. Our data indicate that the F-BAR proteins Cdc15 and Imp2 contribute to a single biological process with both distinct and overlapping functions.