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<div><font face="Arial" size="+2" color="#000000">Seminar
on</font></div>
<div><font face="Arial" size="+2" color="#000000"><b>Modern Optics and
Spectroscopy</b></font><font face="Arial" size="+1"
color="#000000"><b><br>
<br>
</b>Alice Ting, MIT<br>
<br>
<i><b>Fluorescent reporters of protein trafficking and function<br>
<br>
</b></i>May 10, 2005<br>
12:00 - 1:00 p.m.<br>
<br>
Abstract<br>
<br>
Our research program focuses on the development of new methodology for
probing the biochemistry of living cells. We will describe a project
in which we have used the bacterial enzyme biotin ligase to develop
new site-specific protein labeling methodology. This methodology,
which allows introduction of probes of any structure onto a 15-amino
acid acceptor peptide sequence, should provide a much less invasive
alternative to GFP (which is 238 amino acids), as well as allow access
to non-fluorescence applications such as MRI, electron microscopy,
EPR, and photocrosslinking, for which GFP is useless. We will also
describe our efforts to develop new families of FRET-type reporters
for imaging post-translational modification events in live
cells.</font></div>
<div><font face="Arial" size="+1" color="#000000">In addition to
methodology development, our lab has become increasingly interested in
neuroscience problems. For instance, we have applied the site-specific
protein labeling methodology described above to image the trafficking
behavior of AMPA receptors on the surface of hippocampal neurons and
obtained interesting preliminary data showing subunit-dependent
trafficking in response to induction of long-term
potentiation.</font></div>
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