Valuable Insights – Scientists
of Helmholtz Zentrum München and the Technische
Universität München Elucidate the Structural Details
of a Key Protein for Cellular Signal Transduction
26 July 2010Neuherberg, Germany
Scientists of the Institute of
Structural Biology of Helmholtz Zentrum
München and the Technische Universität
München have succeeded in elucidating the
structure of an important region of the
Sam68 protein. The renowned Journal of
Biological Chemistry has selected the report
of these research findings as one of two
“papers of the week” for its September 10,
2010 issue and has chosen the structural
model as cover image.
Using NMR spectroscopy, Professor
Michael Sattler and his team elucidated the
spatial structure of the Qua1 region of
Sam68, which is responsible for the
dimerization of the protein. In
collaboration with the research group of
Professor Ruth Brack-Werner of the Institute
of Virology, the authors showed that this
region is essential for the biological
function of Sam68. The image reveals an
unusual spatial structure, in which two
helices of respectively one Qua1 region
(green and blue) interact with each other
and mediate the dimerization of Qua1 and
thus of Sam68.
Sam68
belongs to the family of STAR
proteins which carry out important
tasks in the signal-regulated
processing of genetic information
and its translation into protein.
Among others, Sam68 regulates
specific processes linked to the
cell cycle and apoptosis and plays a
key role in the pathogenesis of
cancer.
Original publication:
Meyer, NH. et al.: Structural basis
for homodimerization of the Src-associated
during mitosis, 68 kD protein
(Sam68) Qua1 domain. –The Journal of
Biological Chemistry, Vol. 285,
Issue 37, 28893-28901, 10. September
2010;
www.jbc.org/content/early/2010/07/06/jbc.M110.126185.abstract
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