Nonlamin components of the lamina: a paucity of proteins.
Current models of nuclear organization propose that nuclear functions are modulated in part by reversible tethering of chromatin loops to structural elements of the nucleoplasm and the nuclear envelope. Lamins are the best-characterized proteins of the lamina portion of the nuclear envelope and are involved in binding chromatin to the inner nuclear membrane. However, they are not a universal feature of eukaryotic nuclei and do not account fully for the putative functions of the lamina in all organisms. It is possible that nonlamin components of the lamina may substitute for lamins in organisms from which they are absent and modify the properties of lamins during development and the cell cycle. We review the properties of the relatively small number of such components that have been reported, including the young arrest (fs(1)Ya) protein of Drosophila, statin, circumferin, and the MAN antigens. The experimental evidence indicates they are a diverse group of proteins, and that at least some have the potential to modulate the interactions of chromatin, lamins, and the nuclear membranes.
Chaly
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Department of Biology (ELBA), Carleton University, Ottawa, ON, Canada. Nathalie_Chaly@carleton.ca
Stochaj
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D000818:Animals; D034961:Antigens, Nuclear; D018797:Cell Cycle Proteins; D002843:Chromatin / Q000502:physiology; D006801:Humans; D034882:Lamins; D009685:Nuclear Envelope / Q000502:physiology*; D009687:Nuclear Proteins / Q000502:physiology*; D020648:Peptide Elongation Factor 1; D011506:Proteins / Q000502:physiology
D034961:Antigens, Nuclear; D018797:Cell Cycle Proteins; D002843:Chromatin; C503234:EEF1A2 protein, human; D034882:Lamins; D009687:Nuclear Proteins; D020648:Peptide Elongation Factor 1; D011506:Proteins