Nuclear membrane

The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes which in eukaryotic cells surrounds the nucleus, which encases the genetic material. The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes which in eukaryotic cells surrounds the nucleus, which encases the genetic material. The nuclear envelope consists of two lipid bilayer membranes, an inner nuclear membrane, and an outer nuclear membrane. The space between the membranes is called the perinuclear space. It is usually about 20–40 nm wide. The outer nuclear membrane is continuous with the endoplasmic reticulum membrane. The nuclear envelope has many nuclear pores that allow materials to move between the cytosol and the nucleus. Intermediate filaments form a lamina internally to the inner nuclear membrane, and more loosely externally to the outer nuclear membrane to give structural support to the nucleus. The nuclear envelope is made up of two lipid bilayer membranes. An inner nuclear membrane and an outer nuclear membrane. These membranes are connected to each other by nuclear pores. Two sets of intermediate filaments provide support for the nuclear envelope. An internal network forms the nuclear lamina on the inner nuclear membrane. A looser network forms outside to give external support. The outer nuclear membrane also shares a common border with the endoplasmic reticulum. While it is physically linked, the outer nuclear membrane contains proteins found in far higher concentrations than the endoplasmic reticulum. All four nesprin proteins (nuclear envelope spectrin repeat proteins) present in mammals are expressed in the outer nuclear membrane. Nesprin proteins connect cytoskeletal filaments to the nucleoskeleton. Nesprin-mediated connections to the cytoskeleton contribute to nuclear positioning and to the cell’s mechanosensory function. KASH domain proteins of Nesprin-1 and -2 are part of a LINC complex (linker of nucleoskeleton and cytoskeleton) and can bind directly to cystoskeletal components, such as actin filaments, or can bind to proteins in the perinuclear space. Nesprin-3 and-4 may play a role in unloading enormous cargo; Nesprin-3 proteins bind plectin and link the nuclear envelope to cytoplasmic intermediate filaments. Nesprin-4 proteins bind the plus end directed motor kinesin-1. The outer nuclear membrane is also involved in development, as it fuses with the inner nuclear membrane to form nuclear pores. The inner nuclear membrane encloses the nucleoplasm, and is covered by the nuclear lamina, a mesh of intermediate filaments which stabilizes the nuclear membrane as well as being involved in chromatin function and entire expression. It is connected to the outer membrane by nuclear pores which penetrate the membranes. While the two membranes and the endoplasmic reticulum are linked, proteins embedded in the membranes tend to stay put rather than dispersing across the continuum. It is lined with a fiber network called as nuclear lamina which is 10-40 nm thick and provide strength. Mutations in the inner nuclear membrane proteins can cause several nuclear envelopathies. The nuclear envelope is punctured by thousands of nuclear pores, large hollow protein complexes about 100 nm across, with an inner channel about 40 nm wide. They link the inner and outer nuclear membranes. During the G2 phase of interphase, the nuclear membrane increases its surface area and doubles its number of nuclear pore complexes.In eukaryotes, such as yeast, which undergo closed mitosis, the nuclear membrane stays intact during cell division. The spindle fibers either form within the membrane, or penetrate it without tearing it apart.In other eukaryotes (animals as well as plants), the nuclear membrane must break down during the prometaphase stage of mitosis to allow the mitotic spindle fibers to access the chromosomes inside. The breakdown and reformation processes are not well understood. In mammals, the nuclear membrane can break down within minutes, following a set of steps during the early stages of mitosis. First, M-Cdk's phosphorylate nucleoporin polypeptides and they are selectively removed from the nuclear pore complexes. After that, the rest of the nuclear pore complexes break apart simultaneously. Biochemical evidence suggests that the nuclear pore complexes disassemble into stable pieces rather than disintegrating into small polypeptide fragments. M-Cdk's also phosphorylate elements of the nuclear lamina (the framework that supports the envelope) leading to the disassembly of the lamina and hence the envelope membranes into small vesicles. Electron and fluorescence microscopy has given strong evidence that the nuclear membrane is absorbed by the endoplasmic reticulum—nuclear proteins not normally found in the endoplasmic reticulum show up during mitosis.