title: [Structure and biological functions of mammalian LEM-domain proteins].
abstract: During the process of open mitosis in higher eukaryotic cells, the nuclear envelope (NE) is disassembled and reassembled with highly organized and periodical dynamic morphological changes. Recent studies demonstrated that LEM-domain protein family mediates interactions among inner nuclear membrane, nuclear lamina protein and chromatin by interacting with barrier-to-autointegration-factor (BAF). The structure and function of the ternary complex formed by LEM-domain protein, nuclear lamina protein and BAF are dependent on each other. Moreover, the network formation based on this structure and function is critical for the development of basic biological processes of nuclear, and it plays important roles in chromatin separation in late metaphase and anaphase, NE reassembly after mitosis, morphological maintenance of nuclear and NE in interphase, regulation of DNA replication and DNA damage repair, regulation of gene expression and signaling pathway, and infection of retrovirus. Mutations in genes encoding LEM family proteins have important impacts on development and progression of laminopathic diseases and tumorigenesis. This review provides a detailed summary of structural and functional studies of the LEM family proteins.
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Qing-Xia
authors: QX
authors: Hu
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Ang
authors: A
authors: Gao
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Wei-Jia
authors: WJ
authors: Zeng
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Yan-Xin
authors: YX
authors: Wang
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Jin-Tang
authors: JT
authors: Dong
authors: Tianjin Key Laboratory of Protein Sciences, Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
authors: Zheng-Mao
authors: ZM
authors: Zhu
mesh_terms: D000818:Animals; D004260:DNA Repair; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D009687:Nuclear Proteins / Q000737:chemistry / Q000502:physiology*; D017434:Protein Structure, Tertiary
chemical_list: D004268:DNA-Binding Proteins; C405329:LEMD3 protein, human; D008565:Membrane Proteins; D009687:Nuclear Proteins; C092710:emerin; C093413:lamina-associated polypeptide 2