Is my DNA fixed yet?

A broken chromosome (a double-strand DNA break) activates the DNA damage checkpoint to prevent cells from carrying out mitosis until the break has been repaired.  Repair of the break involves the modification and the removal of histone protein octamers from DNA around the break and these must be reestablished when repair is complete.  In a new paper in PNAS, Brandeis alumnus Jung-Ae Kim (Ph.D., Molecular and Cell Biology, 2008) and Professor James Haber show that when two of the major histone chaperone protein complexes (Asf1 and CAF-1) are deleted in yeast cells, their absence prevents cells from turning off the DNA damage checkpoint and hence cells stay permanently arrested.   These results suggest that cells specifically monitor the re-establishment of normal chromatin status after DNA repair.

How actin networks assemble in cells

A new review article in Current Opinion in Cell Biology by Molecular and Cell Biology grad student Melissa Chesarone and Biology’s Professor Bruce Goode focuses on a group of remarkable protein machines that rapidly assemble actin polymers in cells. These factors are essential for cell division, cell movement, and cell shape determination in virtually all organisms. Their catalytic mechanisms involve intricate fast-moving parts, which enables them to construct entire actin networks in a matter of seconds.

Sense from Chaos in Neural Networks

Distinguished physicist and neuroscientist, former Brandeis professor and alumnus Larry Abbott (Ph.D., Physics, 1977) will return to campus on Monday to speak in the IGERT Computational Neuroscience Seminar Series. Larry will talk about new work on “Sense and Chaos in Neural Networks”. The talk will be in Gerstenzang 121 at 4 pm on Monday, Jan 26. Refreshments are available at 3:45 PM.

New building approaching completion

There’s a new slideshow of the Shapiro Science Center on the main campus website. Looks like we are still on track for labs to start moving in February.

Recent Grant Awards

Neuroscience Ph.D. candidate Melanie Gainey received an NRSA Fellowship from NINDS. Working in the Turrigiano lab, Melanie plans to study the role of the AMPA receptor subunit GluR2 in synaptic scaling in cultural neurons and in vivo using a conditional GluR2 knockout mouse.

Assistant Professor Suzanne Paradis received a Smith Family New Investigator Award from the Richard & Susan Smith Family Foundation. $300,000 in support over three years will support the lab’s efforts to study synapse development and specifically the role of the Sema4B protein in controlling synapse formation.

Professor Leslie Griffith received $1.1 million over 5 years from NIMH to study why sleep is required for effective memory formation. To understand this linkage at a cellular and molecular level, the Griffith lab is defining the circuits that regulate sleep in Drosophila and how these circuits affect memory formation.

Professor Larry Wangh received $1.38 million over the next year from Smiths Detection to continue research and invention of LATE-PCR et al., platform technologies for highly informative detection and diagnosis of nucleic acids in a single tube.  There are ongoing projects looking at applications to cancer, prenatal genetics, and several infectious diseases in people and animals.

Channel proteins that aren't

What happens when you take an ion channel and remove all the parts that conduct ions? The answer might be surprising.

The Drosophila ether-à-go-go gene codes for a potassium channel involved in olfaction, learning, and locomotion. It is not solely a potassium channel, however. In a recent paper in Mol. Cell. Neurosci., Brandeis postdoc alum Xiu Xia Sun and Neuroscience grad student Lynn Bostrom from the Griffith lab show that an alternatively spliced form, Eag80, contains no channel domains and localizes to the nucleus. They further show that Eag80 can act to activate signal transduction pathways. This splicing can be stimulated by calcium and protein kinases, suggesting that this splice form may have a significant role in regulating neuronal function.

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