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The nuclear lamina consists of two components, lamins and nuclear lamin-associated membrane proteins. The lamins are type V intermediate filaments which can be categorized as either A-type (lamin A, C) or B-type (lamin B 1, B 2) according to homology of their DNA sequences, biochemical properties and cellular localization during the cell cycle.
Nuclear lamins interact with inner nuclear membrane proteins to form the nuclear lamina on the interior of the nuclear envelope. Lamins have elastic and mechanosensitive properties, and can alter gene regulation in a feedback response to mechanical cues. [1] Lamins are present in all animals but are not found in microorganisms, plants or fungi.
The nuclear envelope, also known as the nuclear membrane, [1] [a] is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus, which encloses the genetic material. The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. [ 4 ]
The nuclear pore complex (NPC), is a large protein complex giving rise to the nuclear pore. Nuclear pores are found in the nuclear envelope that surrounds the cell nucleus in eukaryotic cells . The nuclear envelope is studded by a great number of nuclear pores that give access to various molecules, to and from the nucleoplasm and the cytoplasm.
[4] [6] Some of these biological functions of laminin have been associated with specific amino-acid sequences or fragments of laminin. [4] For example, the peptide sequence [GTFALRGDNGDNGQ], which is located on the alpha-chain of laminin, promotes the adhesion of endothelial cells.
Lamin proteins are thought to be involved in nuclear stability, chromatin structure, and gene expression. Vertebrate lamins consist of two types, A and B. This gene encodes one of the two B type proteins, B1. [7] Lamin B, along with heterochromatin, is anchored to the inner surface of the nuclear membrane by the lamin B receptor.
The c-terminal tail domain contains a nuclear localization signal (NLS), an Ig-fold-like domain, and in most cases a carboxy-terminal CaaX box that is isoprenylated and carboxymethylated (lamin C does not have a CAAX box). Lamin A is further processed to remove the last 15 amino acids and its farnesylated cysteine.
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). [1] The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm.