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 2kb), 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.
Jiang
Mei
M
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, SIBS, Chinese Academy of Sciences, Shanghai, China.
Gao
Yankun
Y
Yang
Tao
T
Zhu
Xueliang
X
Chen
Jiangye
J
D000595:Amino Acid Sequence; D016203:CDC2 Protein Kinase / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D018844:Cyclin-Dependent Kinases; D016213:Cyclins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D014162:Transfection; D020798:Two-Hybrid System Techniques
C543319:CCNY protein, human; D016213:Cyclins; D008565:Membrane Proteins; D016203:CDC2 Protein Kinase; C515076:CDK14 protein, human; D018844:Cyclin-Dependent Kinases