[Seminars] PSB event reminder

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Calendar Name: seminars
Scheduled for: Thursday, January 6 2011, 11:00 - 12:30
Event text:    Dr Arp Schnittger
	       
	       Institut de Biologie Moléculaire des Plantes du CNRS,
	       IBMP-CNRS - UPR2357
	       
	       Strasbourg
	       FRANCE
Details:       "Toward Deciphering the Network Architecture of
	       Cyclin-Dependent Kinase Action"
	       
	       ABSTRACT
	       Cyclin-dependent kinases are the central regulators of
	       the cell cycle and as such key to growth, development
	       and reproduction. The function of CDKs is conserved from
	       yeast to plants and for example, expression of CDKA;1,
	       the plant Cdk1 homolog, can complement yeast cdc2 or
	       Cdc28 mutants. In addition, recent studies have shown
	       that the molecular mechanistics of Cdk1-like kinases are
	       conserved across kingdoms, e.g. the requirement for its
	       activation through phosphorylation of a conserved Thr
	       residue in their T-loop. In contrast to the conserved
	       enzymatic function, the regulatory network of their
	       action appears to have undergone dramatic changes during
	       two billion years of eukaryotic evolution. This is
	       illustrated by the recent finding that a Cdc25-Wee1
	       regulatory module is absent in the flowering plant
	       Arabidopsis. Through extensive studies in yeast and
	       humans, a comprehensive picture of CDK function has been
	       revealed. We are interested in the properties of the
	       network architecture of CDK action to understand general
	       principles of cellular organization and coordination by
	       cell-cycle control. As a starting point, we are
	       following three complementing approaches to identify
	       CDKA;1 substrates in Arabidopsis as a eukaryote very
	       distantly related to metazoans and yeast. First, we
	       exploit a modified bimolecular complementation assays to
	       identify kinase substrates. Second, we have generated a
	       gatekeeper mutant of CDKA;1 that can rescue cdka;1
	       mutants. In the gatekeeper variant the ATP binding
	       pocket is mutated in such a way that bulky derivatives
	       of ATP can be accepted by the kinase allowing the
	       identification of proteins that were phosphorylated by
	       this kinase variant. Third, we are analyzing the
	       phospho-proteome of weak-loss-of-function mutants of
	       CDKA;1. These approaches are providing a growing list of
	       putative CDKA;1 substrates in Arabidopsis. Here, I will
	       give a progress report of our current attempts and
	       compare the so far identified substrates with data from
	       yeast and humans.

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