Erich A. Nigg

TL;DR: An overview of the many mitotic kinases that regulate cell division and the fidelity of chromosome transmission is given.

TL;DR: High-resolution mass spectrometry–based proteomics was applied to investigate the proteome and phosphoproteome of the human cell cycle on a global scale and quantified 6027 proteins and 20,443 unique phosphorylation sites and their dynamics, finding that nuclear proteins and proteins involved in regulating metabolic processes have high phosphorylated site occupancy in mitosis, suggesting that these proteins may be inactivated by phosphorylate in mitotic cells.

TL;DR: A mass-spectrometry-based proteomic analysis of human centrosomes in the interphase of the cell cycle by quantitatively profiling hundreds of proteins across several centrifugation fractions identified and validated 23 novel components and identified 41 likely candidates as well as the vast majority of the known centrosomal proteins in a large background of nonspecific proteins.

TL;DR: These unexpected results suggest a role for these major nucleolar proteins in the nucleocytoplasmic transport of ribosomal components and suggest that transient exposure of shuttling proteins to the cy toplasm may provide a mechanism for cytop lasmic regulation of nuclear activities.

TL;DR: Polo-like kinases are increasingly recognized as key regulators of mitosis, meiosis and cytokinesis and their targeting to different cellular structures through interactions with phosphorylated docking proteins is uncovered.