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This profile was last updated on 6/18/15  and contains information from public web pages and contributions from the ZoomInfo community.

Prof. Ehud Y. Isacoff

Wrong Prof. Ehud Y. Isacoff?

Board Member

Phone: (510) ***-****  HQ Phone
UC Berkeley
2200 University Ave. Rm. 41
Berkeley , California 94720
United States

Company Description: The UC Berkeley School of Public Health offers a university course on health impact assessment in which students critically evaluate a local, regional, or state...   more
Background

Employment History

Board Memberships and Affiliations

Education

  • PhD.
39 Total References
Web References
Kerentech
www.kerentech.com, 5 April 2011 [cached]
Ehud Isacoff, Professor of Neurobiology and Chair, Graduate Group in Biophysics at Berkeley
Using a unique and relatively simple cell-based fluorescent assay they developed, scientists with the U.S. Department of Energy (DOE)'s Lawrence Berkeley National Laboratory (Berkeley Lab) and the University of California (UC), Berkeley have identified a means by which fluoxetine, the active ingredient in Prozac, suppresses the activity of the TREK1 potassium channel. TREK1 activity has been implicated in mood regulation and could be an important target for fluoxetine and other antidepressant drugs.
"Whereas the inhibiting of serotonin re-uptake remains fluoxetine's primary antidepression mechanism, many pharmacological agents have more than one target," says Ehud Isacoff, a neurobiophysicist who holds joint appointments with Berkeley Lab's Physical Biosciences Division and UC Berkeley's Department of Molecular and Cell Biology. "Our study shows that the inhibition of TREK1 by fluoxetine, which was found in earlier studies, is accompanied by an unbinding of the protein's C-terminal domain from the membrane. This is the first observation of the mechanism by which TREK1 might be regulated by antidepressant drugs."
Isacoff is the corresponding author on a paper reporting the results of this study that appears in the Proceedings of the National Academy of Sciences (PNAS). The paper is titled "Optical probing of a dynamic membrane interaction that regulates the TREK1 channel. Co-authoring this paper were Guillaume Sandoz, a TREK1 specialist with France's National Center for Scientific Research at the Institute for Molecular and Cellular Physiology, and PhD student Sarah Bell, both of whom were with Isacoff's research group at the time the work was done.
...
"Studying what the different protein parts of an ion channel do is a huge challenge," Isacoff says. "Over the years, my group has developed techniques by which the domains of channel proteins can be labeled with site-specific fluorescent dyes. Structural rearrangements of the labeled sites in the channel can then be detected through changes in the fluorescence."
Isacoff and his group separated the C-terminal domain from the rest of the protein and tagged it with a green fluorescent protein (GFP) - a fluorescent protein from jellyfish commonly used to paint cells green for biological studies. Whereas the pore of the TREK1 ion channel is embedded in the plasma membrane of a neuron, the C-terminal is a short tail that protrudes out into the surrounding cytoplasm.
Using voltage clamps to measure electrical currents through the channel and fluorescence to monitor the disposition of the C-terminal domain, Isacoff and his group found that when the C-terminal tail is fully bound to the plasma membrane, the TREK1 potassium channel opens more; when the tail is unbound from the plasma membrane, the ion channel tends to close.
"We found that fluoxetine causes the isolated C-terminal domain to unbind from the membrane and also causes an inhibition of current from the full TREK1 channel," Isacoff says.
The next step will be to see how the C-terminal tail is affected by the presence of fluoxetine when the tail is still attached to the rest of the TREK1 protein. In the meantime, Isacoff and his team feel they now have a valuable assay that can be used to monitor the reversible plasma membrane association of protein domains without the need for scanning, optical slicing or imaging.
"Pharmaceutical companies screening for potential new drugs, such as improved antidepressants, prefer assays that are fast and simple," Isacoff says.
Photoswitch Biosciences, Inc.
www.photoswitchbio.com, 12 Feb 2015 [cached]
Ehud Isacoff, PhD. Co-founder. Professor and Head of Division of Neurobiology, UC Berkeley; Member, Lawrence Berkeley National Laboratory; Director of UC Berkeley-LBNL Nanomedicine Development Center. Internationally recognized expert in ion channels and synaptic function. Co-inventor of photoswitched ion channels.
To learn more about Ehud Isacoff, please take a look at his UC Berkeley page and Isacoff Lab website.
Ehud Isacoff, Professor of ...
www.kerentech.com, 9 Feb 2011 [cached]
Ehud Isacoff, Professor of Neurobiology and Chair, Graduate Group in Biophysics at Berkeley
Using a unique and relatively simple cell-based fluorescent assay they developed, scientists with the U.S. Department of Energy (DOE)'s Lawrence Berkeley National Laboratory (Berkeley Lab) and the University of California (UC), Berkeley have identified a means by which fluoxetine, the active ingredient in Prozac, suppresses the activity of the TREK1 potassium channel. TREK1 activity has been implicated in mood regulation and could be an important target for fluoxetine and other antidepressant drugs.
"Whereas the inhibiting of serotonin re-uptake remains fluoxetine's primary antidepression mechanism, many pharmacological agents have more than one target," says Ehud Isacoff, a neurobiophysicist who holds joint appointments with Berkeley Lab's Physical Biosciences Division and UC Berkeley's Department of Molecular and Cell Biology. "Our study shows that the inhibition of TREK1 by fluoxetine, which was found in earlier studies, is accompanied by an unbinding of the protein's C-terminal domain from the membrane. This is the first observation of the mechanism by which TREK1 might be regulated by antidepressant drugs."
Isacoff is the corresponding author on a paper reporting the results of this study that appears in the Proceedings of the National Academy of Sciences (PNAS). The paper is titled "Optical probing of a dynamic membrane interaction that regulates the TREK1 channel. Co-authoring this paper were Guillaume Sandoz, a TREK1 specialist with France's National Center for Scientific Research at the Institute for Molecular and Cellular Physiology, and PhD student Sarah Bell, both of whom were with Isacoff's research group at the time the work was done.
...
"Studying what the different protein parts of an ion channel do is a huge challenge," Isacoff says. "Over the years, my group has developed techniques by which the domains of channel proteins can be labeled with site-specific fluorescent dyes. Structural rearrangements of the labeled sites in the channel can then be detected through changes in the fluorescence."
Isacoff and his group separated the C-terminal domain from the rest of the protein and tagged it with a green fluorescent protein (GFP) - a fluorescent protein from jellyfish commonly used to paint cells green for biological studies. Whereas the pore of the TREK1 ion channel is embedded in the plasma membrane of a neuron, the C-terminal is a short tail that protrudes out into the surrounding cytoplasm.
Using voltage clamps to measure electrical currents through the channel and fluorescence to monitor the disposition of the C-terminal domain, Isacoff and his group found that when the C-terminal tail is fully bound to the plasma membrane, the TREK1 potassium channel opens more; when the tail is unbound from the plasma membrane, the ion channel tends to close.
"We found that fluoxetine causes the isolated C-terminal domain to unbind from the membrane and also causes an inhibition of current from the full TREK1 channel," Isacoff says.
The next step will be to see how the C-terminal tail is affected by the presence of fluoxetine when the tail is still attached to the rest of the TREK1 protein. In the meantime, Isacoff and his team feel they now have a valuable assay that can be used to monitor the reversible plasma membrane association of protein domains without the need for scanning, optical slicing or imaging.
"Pharmaceutical companies screening for potential new drugs, such as improved antidepressants, prefer assays that are fast and simple," Isacoff says.
Faculty | QB3
www.qb3.org, 12 Feb 2015 [cached]
Ehud Isacoff
"The dog has a retina very ...
newscenter.berkeley.edu, 9 Dec 2014 [cached]
"The dog has a retina very similar to ours, much more so than mice, so when you want to bring a visual therapy to the clinic, you want to first show that it works in a large animal model of the disease," said lead researcher Ehud Isacoff, professor of molecular and cell biology at UC Berkeley.
...
Isacoff, Flannery and UC Berkeley colleagues have developed several optogenetic techniques for restoring light-sensitivity to surviving retinal cells other than the photoreceptors.
...
The researchers then inject a chemical photoswitch into the eye, "basically, a glutamate dangling on a light-sensitive string," said Isacoff, "which anchors to the modified receptor and stuffs the glutamate into its docking site on the receptor when activated by light.
...
Our next step is to figure out how good they are at telling images apart," said Isacoff, who holds the Class of 1933 chair.
...
"And along the way, we developed tools that could be applied to the basic science of how synapses work and how neural circuits work," Isacoff added.
...
"When we put the photoswitched channels into bipolar cells and record the output of the ganglion cells, we see complicated patterns that look a lot like the activity you get in a normal retina, compared to the on-off activity you get when you put the same photoswitch into a ganglion cell," Isacoff said.
...
"This is not necessarily a disadvantage," Isacoff said, "because the therapy can be stopped, and new photo-sensitive chemicals can be tried as they are improved."
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