Disordered Motifs and Domains in Cell Control
Welcome Letter
October 2014
Dear Colleagues,
On behalf of the Biophysical Society, we would like to welcome you to the
Disordered Motifs
and Domains in Cell Control
meeting. Interest in intrinsically disordered proteins (IDPs) has
exploded in recent years. It is now widely recognized that ~50% of human proteins are IDPs, or
contain disordered regions, and that disorder is often essential for function. Furthermore,
disorder is prevalent in the proteomes of most higher organisms. However, despite this broad
awareness, in most cases we lack knowledge of the molecular functions associated with protein
disorder. Consequently, numerous unresolved questions remain relating to the contribution of
IDPs to biological processes in living systems. An emerging theme is that many disordered
protein regions contain short linear motifs, or somewhat longer disordered domains, that mediate
biomolecular interactions and thus drive biological function. These disordered motifs and
domains are the subject of this thematic meeting.
While we recognize the importance of disordered motifs and domains in the function of proteins,
and there are more and more examples where the molecular details of their biological functions
are understood, in general we currently can only speculate about their roles in the vast swaths of
disorder within proteomes. At this meeting, structural biologists, biophysicists, cell biologists,
systems biologists, computational biologists and bioinformaticians will assemble to reveal how
disordered motifs and domains drive biological function. Key questions to be addressed include:
What are the physical features of disordered motifs and how do these mediate their functional
interactions? And how are these interactions regulated? Given our current knowledge of
disordered motifs and domains, how can we identify others within uncharacterized regions of
proteomes? And can their functions be predicted? How diverse are the molecular mechanisms
associated with disordered motifs and domains? What are the links between the dynamics and
conformational heterogeneity of disordered protein regions and function? What types of
structures do disordered motifs and domains form? How diverse are the length scales of these
structures? What are the selective pressures that have given rise to disordered protein regions
through evolution? And how are the functions of disordered motifs and domains altered in
disease? By bringing together scientists with widely ranging expertise and perspectives, we seek
to collectively address these questions and transform our understanding of the roles of protein
disorder in biology.
This meeting offers a diverse program covering all aspects of the field with almost 40 lectures
and over 50 posters. We hope to expand everyone’s view of disordered motifs and domains
within proteins and achieve synergy to drive the field forward in future years.
Most of all, we wish everyone a great meeting!
Sincerely yours,
Anna Akhmanova, Norman Davey, Ashok Deniz, Richard Kriwacki, and Sonia Longhi
The Organizing Committee
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