Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1

A novel cyclin, CCNY, was identified as a PFTK1 interacting protein in a yeast two-hybrid screen. The cyclin box in CCNY and the PFTAIRE motif in PFTK1 are both required for the interaction which was confirmed by in vivo and in vitro assays. Two transcripts (4 and 2 kb), of CCNY were detected by Northern blot analysis and CCNY was enriched at the plasma membrane due to an N-terminal myristoylation signal. We propose that binding of CCNY to PFTK1 enhances PFTK1 kinase activity and changes its intracellular location. Structured summary: MINT-7147585, MINT-7147598, MINT-7147614, MINT-7147628, MINT-7147647, MINT-7147665, MINT7147680: pftk1 (uniprotkb: O94921) physically interacts (MI: 0915) with CCNY (uniprotkb: Q8ND76) by two hybrid (MI: 0018) MINT-7147725, MINT-7147743: pftk1 (uniprotkb: O94921) physically interacts (MI: 0914) with CCNY (uniprotkb: Q8ND76) by anti tag coimmunoprecipitation (MI: 0007) MINT-7147758: pftk1 (uniprotkb: O35495) physically interacts (MI: 0914) with CCNY (uniprotkb: Q8BGU5) by anti bait coimmunoprecipitation (MI: 0006) MINT-7147695, MINT-7147713: pftk1 (uniprotkb: O94921) and CCNY (uniprotkb: Q8ND76) colocalize (MI: 0403) by. uorescence microscopy (MI: 0416) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.