title: Another piece of the p27Kip1 puzzle.
abstract: How extracellular signals communicate with the cell cycle is poorly understood. In this issue, two papers address this problem by reporting phosphorylation of the cyclin-dependent kinase inhibitor p27Kip1 on a tyrosine residue by nonreceptor tyrosine kinases, which decreases p27 stability. This new mechanism could explain how cells enter the cell cycle from a quiescent state.
authors.affiliation: Mouse Cancer Genetics Program, Center for Cancer Research, National Cancer Institute-Frederick, Building 560/22-56, 1050 Boyles Street, Frederick, MD 21702, USA. kaldis@ncifcrf.gov
authors.forename: Philipp
authors.initials: P
authors.lastname: Kaldis
mesh_terms: D000818:Animals; D002453:Cell Cycle / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002471:Cell Transformation, Neoplastic / Q000235:genetics / Q000378:metabolism; D050760:Cyclin-Dependent Kinase Inhibitor p27 / Q000235:genetics / Q000378:metabolism*; D005110:Extracellular Space / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D014443:Tyrosine / Q000378:metabolism
chemical_list: D018797:Cell Cycle Proteins; D050760:Cyclin-Dependent Kinase Inhibitor p27; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases