Mount Desert Island Biological Laboratory

Salisbury Cove, ME, United States

Mount Desert Island Biological Laboratory

Salisbury Cove, ME, United States

The MDI Biological Laboratory is an independent non-profit biomedical research institution founded in 1898 and located in Salisbury Cove, Maine, on Mount Desert Island. Its mission is to improve human health and well- being through basic research, education, and development ventures that transform discoveries into cures. In 2013, the Laboratory was designated a Center for Biomedical Research Excellence by the National Institutes of Health, which awarded the Laboratory a grant of $13 million over five years to expand the institution’s research program. The MDI Biological Laboratory has a full-time staff of 63, and will offer 23 research training courses in 2014. Wikipedia.

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Strange K.,Mount Desert Island Biological Laboratory | Yin V.P.,Mount Desert Island Biological Laboratory
Current Biology | Year: 2012

Pacemaker cells are specialized cell types that drive biological rhythms like the heartbeat and intestinal peristalsis. What determines whether a cell functions as a pacemaker? Studies in Caenorhabditis elegans suggest that pacemaking activity may be controlled in part by microRNAs. © 2012 Elsevier Ltd.

Strome S.,University of California at Santa Cruz | Updike D.,Mount Desert Island Biological Laboratory
Nature Reviews Molecular Cell Biology | Year: 2015

Germ cells are the special cells in the body that undergo meiosis to generate gametes and subsequently entire new organisms after fertilization, a process that continues generation after generation. Recent studies have expanded our understanding of the factors and mechanisms that specify germ cell fate, including the partitioning of maternally supplied 'germ plasm', inheritance of epigenetic memory and expression of transcription factors crucial for primordial germ cell (PGC) development. Even after PGCs are specified, germline fate is labile and thus requires protective mechanisms, such as global transcriptional repression, chromatin state alteration and translation of only germline-appropriate transcripts. Findings from diverse species continue to provide insights into the shared and divergent needs of these special reproductive cells. © 2015 Macmillan Publishers Limited. All rights reserved.

Strange K.,Mount Desert Island Biological Laboratory
Channels (Austin, Tex.) | Year: 2011

CLC anion transport proteins function as Cl (-) channels and Cl (-) /H (+) exchangers and are found in all major groups of life including archaebacteria. Early electrophysiological studies suggested that CLC anion channels have two pores that are opened and closed independently by a "fast" gating process operating on a millisecond timescale, and a "common" or "slow" gate that opens and closes both pores simultaneously with a timescale of seconds (Figure 1A). Subsequent biochemical and molecular experiments suggested that CLC channels/transporters are homodomeric proteins ( 1-3) .

Lee E.C.-H.,Mount Desert Island Biological Laboratory | Strange K.,Mount Desert Island Biological Laboratory
American Journal of Physiology - Cell Physiology | Year: 2012

Increased gpdh-1 transcription is required for accumulation of the organic osmolyte glycerol and survival of Caenorhabditis elegans during hypertonic stress. Our previous work has shown that regulators of gpdh-1 (rgpd) gene knockdown constitutively activates gpdh-1 expression. Fifty-five rgpd genes play essential roles in translation suggesting that inhibition of protein synthesis is an important signal for regulating osmoprotective gene transcription. We demonstrate here that translation is reduced dramatically by hypertonic stress or knockdown of rgpd genes encoding aminoacyl-tRNA synthetases and eukaryotic translation initiation factors (eIFs). Toxin-induced inhibition of translation also activates gpdh-1 expression. Hypertonicityinduced translation inhibition is mediated by general control nonderepressible (GCN)-2 kinase signaling and eIF-2α phosphoryation. Loss of gcn-1 or gcn-2 function prevents eIF-2α phosphorylation, completely blocks reductions in translation, and inhibits gpdh-1 transcription. gpdh-1 expression is regulated by the highly conserved with-no-lysine kinase (WNK) and Ste20 kinases WNK-1 and GCK-3, which function in the GCN-2 signaling pathway downstream from eIF-2α phosphorylation. Our previous work has shown that hypertonic stress causes rapid and dramatic protein damage in C. elegans and that inhibition of translation reduces this damage. The current studies demonstrate that reduced translation also serves as an essential signal for activation of WNK-1/GCK-3 kinase signaling and subsequent transcription of gpdh-1 and possibly other osmoprotective genes. © 2012 the American Physiological Society.

All eukaryotic and some prokaryotic ClC anion transport proteins have extensive cytoplasmic C-termini containing two cystathionine-β-synthase (CBS) domains. CBS domain secondary structure is highly conserved and consists of two α-helices and three β-strands arranged as β1-α1-β2-β3-α2. ClC CBS domain mutations cause muscle and bone disease and alter ClC gating. However, the precise functional roles of CBS domains and the structural bases by which they regulate ClC function are poorly understood. CLH-3a and CLH-3b are C. elegans ClC anion channel splice variants with strikingly different biophysical properties. Splice variation occurs at cytoplasmic N- and C-termini and includes several amino acids that form α2 of the second CBS domain (CBS2). We demonstrate that interchanging α2 between CLH-3a and CLH-3b interchanges their gating properties. The "R-helix" of ClC proteins forms part of the ion-conducting pore and selectivity filter and is connected to the cytoplasmic C-terminus via a short stretch of cytoplasmic amino acids termed the "R-helix linker". C-terminus conformation changes could cause R-helix structural rearrangements via this linker. X-ray structures of three ClC protein cytoplasmic C-termini suggest that α2 of CBS2 and the R-helix linker could be closely apposed and may therefore interact. We found that mutating apposing amino acids in α2 and the R-helix linker of CLH-3b was sufficient to give rise to CLH-3a-like gating. We postulate that the R-helix linker interacts with CBS2 α2, and that this putative interaction provides a pathway by which cytoplasmic C-terminus conformational changes induce conformational changes in membrane domains that in turn modulate ClC function.

Christie A.E.,Mount Desert Island Biological Laboratory
Cell and Tissue Research | Year: 2011

Decapod crustaceans have long served as important models for the study of neuroendocrine signaling. For example, the process of neurosecretion was first formally demonstrated by using a member of this order. In this review, the major decapod neuroendocrine organs are described, as are their phylogenetic conservation and neurochemistry. In addition, recent advances in crustacean neurohormone discovery and tissue mapping are discussed, as are several recent advances in our understanding of hormonal control in this group of animals. © 2011 Springer-Verlag.

Mount Desert Island Biological Laboratory | Date: 2016-09-21

Methods and pharmaceutical compositions are provided for enhancing or stimulating regeneration of a tissue in a subject. In one aspect, the invention provides a method including administering to a subject in need thereof a therapeutically effective amount of an aminosterol or a pharmaceutically acceptable salt thereof to stimulate or enhance regeneration of a tissue. In another aspect, the invention provides a method including administering to a subject a therapeutically effective amount of an aminosterol or a pharmaceutically acceptable salt thereof to stimulate or enhance regeneration of a tissue to treat or prevent a disease, disorder, trauma, or condition resulting from an injury of the tissue. In an additional aspect, the invention provides a pharmaceutical composition comprising a therapeutically effective amount of an aminosterol to stimulate or enhance regeneration of a tissue.

Agency: NSF | Branch: Standard Grant | Program: | Phase: RSCH EXPER FOR UNDERGRAD SITES | Award Amount: 209.70K | Year: 2015

This REU Site award to Mount Desert Island Biological Laboratory, Salisbury Cove, Maine, will support the training of 10 students for 10 weeks during the summers of 2016- 2017. The scientific focus of the MDI Biological Laboratory REU Site is comparative approaches in cellular, molecular and environmental biology. Students will engage in scientific research using diverse model systems under the close guidance of a research scientist. The students will have access to state of the art research facilities and the coastal ecological setting offered by MDI Biological Laboratory. Students will have a wide range of opportunities for training in cutting edge interdisciplinary approaches to molecular, cellular, and environmental biology. Students will attend regularly scheduled seminars, which include instruction on responsible conduct of research, as well as symposia and workshops.

It is anticipated that a total of 20 students, primarily from schools with limited research opportunities, will be trained in the program. Students will learn how research is conducted, and many will present the results of their work at scientific conferences. Students will be engaged in various outreach opportunities such as Family Science Night, a community-based event which draws hundreds of participants. These outreach experiences help to strengthen the ties between MDI Biological Laboratory and the local community. Through participation in these programs they will learn to discuss with lay audiences the broader impacts of their NSF-funded work.

Interested students are asked to apply online, and submit an application form, short answer/essay questions, two faculty recommendations, and a transcript. Applications are reviewed, scored, and ranked by a faculty committee. Applications are due in March, with offers made in April and May. A common web-based assessment tool used by all REU programs funded by the Division of Biological Infrastructure (Directorate for Biological Sciences) will be used to determine the effectiveness of the training program. Students are required to be tracked after the program and must respond to an automatic email sent via the NSF reporting system. More information is available by visiting, or by contacting the PI (Dr. Paulyn Cartwright at ) or the co-PI (Dr. Robert Morris

Agency: NSF | Branch: Standard Grant | Program: | Phase: AISL | Award Amount: 249.85K | Year: 2012

The Mount Desert Island Biological Laboratory, the National Park Service, and the Schoodic Education and Research Center Institute are investigating whether DNA-based identification of organisms (DNA barcoding) can enhance the publics understanding of biodiversity by helping volunteer citizen scientists identify unknown species. DNA barcoding allows non-scientists to identify unknown organisms at the species level by comparing short DNA sequences taken from unknown organisms to DNA sequences in a reference library for known species. Project deliverables include preliminary data on science learning outcomes among adult citizen scientists; preliminary biodiversity data for invertebrates collected from two habitats in Acadia National Park (forest and eelgrass); and two DNA barcode reference libraries for park invertebrates.

Eighty adult volunteers are collecting invertebrates along two transects (one terrestrial; one marine) in Acadia National Park in Maine. Volunteers are sorting and identifying the unknown organisms by (1) traditional morphological analysis, (2) morphological analysis supplemented with existing DNA barcoding data, or (3) generating DNA barcoding sequencing data through hands-on laboratory work. Project personnel are using observation, interviews, questionnaires, and evaluation instruments to determine how the three species identification strategies impact volunteers science awareness, knowledge, understanding, attitudes, and behavior.

Agency: NSF | Branch: Continuing grant | Program: | Phase: RSCH EXPER FOR UNDERGRAD SITES | Award Amount: 556.15K | Year: 2010

An award was made to the Mount Desert Island Biological Laboratory, Salisbury Cove, Maine, to provide research training for 10 weeks for 10 undergraduates, for the summers of 2010-2015. This award is also supported by the Division of Ocean Sciences (OCE) in the Directorate for Geosciences (GEO). The scientific focus of the MDIBL REU Site is marine molecular physiology and environmental stress. Of particular interest are marine and freshwater environments in which organisms are constantly exposed to changes in tide, salinity, temperature, pH, as well as both natural and human-made toxins. Using a variety of model organisms, students will investigate osmoregulation, acid base regulation, ion transport, functional genomics, and environmental toxicology using state-of-the-art technology. Key program elements are mentored laboratory research, weekly lectures and seminars, participation in science outreach to a public audience, student presentations of research to the MDIBL community, and training in responsible conduct in research. Students live on campus in close proximity to the research laboratories, conference center, and dining hall. Targeted students include rising sophomores and juniors majoring in biology or a related discipline such as biochemistry, environmental sciences, or science education. The MDIBL REU Site makes a special effort to recruit underrepresented minorities in science, as well as students from small colleges and other institutions lacking the research faculty or infrastructure necessary for a robust undergraduate research program. Interested students are asked to apply online, including: an Application Form, Short Answer/Essay Questions, two Faculty Recommendations, and a Transcript. Applications are reviewed, scored, and ranked by faculty committee. Applications are due in January, with offers made in February and March. Students will complete the REU common assessment tool at the end of their research fellowship and will be contacted in successive years to track their progress in science. For further information contact James B. Claiborne, Ph.D. (, the Principal Investigator, at Georgia Southern University, or see .

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