By Philippe Collas
This quantity offers an exhaustive overview of the most up-tp-date wisdom of the composition, structure and dynamics of the nuclear envelope. not like different finished works on mobile membranes in most cases, this e-book is the 1st to particularly tackle the nuclear envelope. specialists within the box relate the several domain names of the nuclear envelope, their biogenesis, their composition, their mode of concentrating on to chromosomes and the way they dissociate from chromosomes upon mobile department. A wealth of knowledge from a number of experimental platforms is equipped, equivalent to dividing somatic cells, embryos and nuclear meeting assays in cell-free extracts, in a variety of vertebrate and invertebrate organisms starting from people to yeast. The booklet additionally includes updated reports at the courting among mutations in proteins of the nuclear envelope and Emery-Dreifuss muscular dystrophy. The breadth of issues lined in what could seem to be a box as slender because the nuclear envelope makes this quantity a invaluable reference.
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Additional info for Nuclear Envelope Dynamics in Embryos and Somatic Cells
90. Nehls S, Snapp EL, Cole NB et al. Dynamics and retention of misfolded proteins in native ER membranes. Nat Cell Biol 2000; 2:288-295. CHAPTER 3 Targeting and Retention of Proteins in the Inner and Pore Membranes of the Nuclear Envelope Cecilia Östlund, Wei Wu and Howard J. Worman Abstract T he targeting of integral proteins to the inner and pore membranes of the nuclear envelope occurs through different mechanisms than the targeting of soluble proteins to the nucleus. Most nuclear integral membrane proteins reach their sites through a diffusion-retention mechanism, where the proteins are inserted into the endoplasmic reticulum membrane during translation, and then laterally diffuse along the endoplasmic reticulum membrane to the pore and inner nuclear membranes.
The lamins differ from cytoplasmic intermediate filaments as their carboxyl-terminal domains contain a NLS and, except in lamin C, a CAAX-motif, which gets post-translationally modified by prenylation. The rod domains of the lamins are 42 amino acids longer than those of cytoplasmic intermediate filaments. Lamins, like other nonmembrane nuclear proteins, enter the nucleus through the nuclear pores in a NLS-dependent manner.
When the luminal and transmembrane domains of CD8 are fused to the endoplasmic carboxyl-terminus of gp210, the chimeric protein is also in part targeted to the pore membrane, with this targeting being dependent on the last 20 amino acids of gp210. 57 Studies of POM121 fused to GFP showed that amino acids 129-618 of the endoplasmic, carboxyl-terminal region of the protein were sufficient for targeting to the nuclear pores. Amino acids 1-128, comprising the luminal region and transmembrane spanning segment, localized to the ER.
Nuclear Envelope Dynamics in Embryos and Somatic Cells by Philippe Collas