Nuclear lamin proteins: domains required for nuclear targeting, assembly, and cell-cycle-regulated dynamics.
The nuclear lamin proteins assemble at the nuclear membrane into a highly dynamic network whose integrity is exquisitely controlled by the major cell cycle regulators. Although the actual cellular functions of the lamins remain elusive, the processes of targeted lamin assembly and phosphorylation-induced disassembly have come to light recently. These processes require functionally interacting lamin domains to execute targeting to the nucleus and the nuclear membranes, lamina assembly, and the disassembly response to cell-cycle-dependent phosphorylation.
McKeon
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Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.
D000595:Amino Acid Sequence; D000818:Animals; D002453:Cell Cycle; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000378:metabolism*
D008565:Membrane Proteins