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English: Structure and function of the nuclear lamina. The nuclear lamina lies on the inner surface of the inner nuclear membrane (INM), where it serves to maintain nuclear stability, organize chromatin and bind nuclear pore complexes (NPCs) and a steadily growing list of nuclear envelope proteins (purple) and transcription factors (pink). Nuclear envelope proteins that are bound to the lamina include nesprin, emerin, lamina-associated proteins 1 and 2 (LAP1 and LAP2), the lamin B receptor (LBR) and MAN1. Transcription factors that bind to the lamina include the retinoblastoma transcriptional regulator (RB), germ cell-less (GCL), sterol response element binding protein (SREBP1), FOS and MOK2. Barrier to autointegration factor (BAF) is a chromatin-associated protein that also binds to the nuclear lamina and several of the aforementioned nuclear envelope proteins. Heterochromatin protein 1 (HP1) binds both chromatin and the LBR. ONM, outer nuclear membrane [9]. Coutinho et al. Immunity & Ageing 2009 6:4 doi:10.1186/1742-4933-6-4
Русский: "Структура и функции ядерной ламины". Ядерная ламина прилегает к внутренней поверхности внутренней ядерной мембраны (INM) и помогает поддерживать ядро в стабильном состоянии, участвует в организации хроматина, связывает ядерные поры. Также ядерная ламина взаимодействует с белками ядерной оболочки, число которых в последнее время постоянно растёт благодаря новым открытиям. Белки отмечены пурпурным цветом. Среди белков оболочки, связывающихся с мембраной - такие белки, как несприн, эмерин, LAP1, LAP2, рецептор ламина B и MAN1. Также к ламине присоединяются факторы транскрипции, такие как retinoblastoma transcriptional regulator (RB), germ cell-less (GCL), sterol response element binding protein (SREBP1), FOS and MOK2.
Datum
Izvor Molecular ageing in progeroid syndromes: Hutchinson-Gilford progeria syndrome as a model (Review)
Autor Henrique Douglas M Coutinho , Vivyanne S Falcão-Silva, Gregório Fernandes Gonçalves and Raphael Batista da Nóbrega
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© 2009 Coutinho et al; licensee BioMed Central Ltd.

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