the nuclear membrane forms around chromosomes during telophase of mitosis.
the nuclear membrane forms around chromosomes during telophase of mitosis.
when does the nuclear membrane form around chromosomes?
during telophase of mitosis
aberrant nuclear envelope breakdown has also been observed in laminopathies and in cancer cells leading to mislocalization of cellular proteins, the formation of micronuclei and genomic instability.









































section::::cell division.:reformation.









































exactly how the nuclear membrane reforms during telophase of mitosis is debated. two theories exist—









































bullet::::- vesicle fusion — where vesicles of nuclear membrane fuse together to rebuild the nuclear membrane









































bullet::::- reshaping of the endoplasmic reticulum—where the parts of the endoplasmic reticulum containing the absorbed nuclear membrane envelop the nuclear space, reforming a closed membrane.









































section::::origin of the nuclear membrane.
nuclear envelope
there are several proteins associated with the inner nuclear membrane. it is likely that the majority of them are also associated with the nuclear lamina. some may interact directly with the nuclear lamina, and some may be associated with it through scaffold proteins. all inm proteins are arranged such that their n-termini is facing the nucleoplasm and targeted by various kinases. they are synthesized in one of three places; in the cytoplasm, the cytoplasmic er, or the outer nuclear membrane (onm). all require localisation to the inm. since the outer nuclear membrane is continuous with the endoplasmic reticulum it is possible that the inner nuclear membrane proteins are translated on the rough endoplasmic reticulum, whereby the proteins move into the nucleus by lateral diffusion through a nuclear pore. in this model, proteins diffuse freely from the er to the inner nuclear membrane, where association with nuclear lamina or chromatin immobilizes them. a nuclear localisation signal (nls) is not sufficient to target a protein to the inm, and the n-terminal domain of lbr cannot translocate into the nuclear lumen if its size is increased from 22 to approximately 70 kda, supporting this view. current opinion is that inm proteins synthesised in the cytoplasm are transported to the inm through nuclear pore complexes (npc).
inner nuclear membrane protein