A docking interface in the cyclin Cln2 promotes multi-site phosphorylation of substrates and timely cell-cycle entry.

ABSTRACT:

Background

Eukaryotic cell division is driven by cyclin-dependent kinases (CDKs). Distinct cyclin-CDK complexes are specialized to drive different cell-cycle events, though the molecular foundations for these specializations are only partly understood. In budding yeast, the decision to begin a new cell cycle is regulated by three G1 cyclins (Cln1-Cln3). Recent studies revealed that some CDK substrates contain a novel docking motif that is specifically recognized by Cln1 and Cln2, and not by Cln3 or later S- or M-phase cyclins, but the responsible cyclin interface was unknown.

Results

Here, to explore the role of this new docking mechanism in the cell cycle, we first show that it is conserved in a distinct cyclin subtype (Ccn1). Then, we exploit phylogenetic variation to iden

SUBMITTER: Bhaduri S 

PROVIDER: S-EPMC4318751 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature