Sorry, I haven't been writing much in the past few days.
Here are some cool ER papers I've seen recently:
When the nuclear envelope reforms after mitosis, ER vesicles must bind to the condensed chromatin, but how does this occur? Well about half of the nuclear envelope (NE) proteins have basic luminal domains that mediate electrostatic interactions with the DNA itself. (In comparison about 4% of general ER and Golgi proteins have basic luminal domains.) To prevent ER/DNA association during mitosis, these basic NE proteins are phosphorylated.
How does the ER remain extended in cells? This becomes a problem once you realize that actin, which is constantly polymerized at the cell's edge, is constantly being pushed towards the nucleus, and taking everything else along with it. Now it seems like the ER can interact with focal adhesions via protein tyrosine phosphatase 1B. This interaction may help anchor the ER at peripheral focal adhesion sites. Whether this is the only ER protein that can interact with focal adhesions remains unclear.
In Drosophila melanogaster embryogenesis, the first 13 nuclear division cycles are not accompanied by any cellularization. What you get is a giant single syncytium with over 6000 nuclei. At a specific time point all the nuclei migrate to the surface of the syncytium and then around each nuclei a cell membrane is constructed. In this paper the authors examined how the ER and Golgi of the syncytium are formed. After nuclear migration, the ER which previously was one giant cortical network, compartmentalizes around each nucleus. This even occurs prior to cellularization and requires a functional microtubule array.
(cross-posted on Science Sampler)
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