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The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. [4] The space between the membranes is called the perinuclear space. It is usually about 10–50 nm wide. [5] [6] The outer nuclear membrane is continuous with the endoplasmic reticulum membrane. [4]
Tumor cells often show an aberrant nuclear structure, which is used by pathologists in diagnostics. As changes in the nuclear envelope correspond to functional changes in the nucleus, morphological changes in the nucleus may be involved in carcinogenesis. The regulatory functions of inner nuclear membrane proteins strongly suggest this ...
1 Outer membrane. 1.1 Porin. 2 Intermembrane space. 2.1 Intracristal space 2.2 Peripheral space. 3 Lamella. 3.1 Inner membrane 3.11 Inner boundary membrane 3.12 Cristal membrane 3.2 Matrix You are here 3.3 Cristæ. 4 Mitochondrial DNA 5 Matrix granule 6 Ribosome 7 ATP synthase
The nuclear lamina is associated with the inner face of the inner nuclear membrane of the nuclear envelope, whereas the outer face of the outer nuclear membrane is continuous with the endoplasmic reticulum. [1] The nuclear lamina is similar in structure to the nuclear matrix, that extends throughout the nucleoplasm.
The outer nuclear membrane is continuous with the rough endoplasmic reticulum membrane, and like that structure, features ribosomes attached to the surface. The outer membrane is also continuous with the inner nuclear membrane since the two layers are fused together at numerous tiny holes called nuclear pores that perforate the nuclear envelope.
Within the perinuclear space (between inner and outer nuclear membranes) are SUN-1 and -2 which form connections with the KASH domain proteins on nesprin and the nuclear envelope lumen. [3] Interestingly, the removal of either SUN -1 or -2 individually will not disrupt LINC complex connectivity, indicating the similarity between the two proteins.
Cardiolipin (IUPAC name 1,3-bis(sn-3’-phosphatidyl)-sn-glycerol, "sn" designating stereospecific numbering) is an important component of the inner mitochondrial membrane, where it constitutes about 20% of the total lipid composition.
Later in 1978, immunolabeling techniques revealed that lamins are localized at the nuclear envelope under the inner nuclear membrane. It wasn't until 1986 that an analysis of lamin cDNA clones across a variety of species supported that lamins belong to the intermediate filament (IF) protein family. [ 4 ]